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Gene Information
Gene symbol: APLP2
Gene name: amyloid beta (A4) precursor-like protein 2
HGNC ID: 598
Synonyms: APPH
Related Genes
Related Sentences
| # | PMID | Sentence |
| 1 | 47333 | Using the radioactively-labeled alkaline-degraded acid-soluble fraction of amyloid ([ 125I ]DAA), we developed a radioimmunoassay for the previously described amyloid-related component of the human serum (SAA). |
| 2 | 416984 | The quantity of insular amyloid correlated significantly with glucose clearance in intravenous glucose tolerance tests and with serum glucose, triglycerides, immunoreactive insulin, and prebetallipoprotein measured after an overnight fast. |
| 3 | 970128 | The combination of haematoxylin-eosin, elastin (Weigert), alkaline Congo red and Sirius red for amyloid and PTAH is specially to be recommended. |
| 4 | 1282806 | Characterization of the human islet amyloid polypeptide/amylin gene transcripts: identification of a new polyadenylation site. |
| 5 | 1282806 | Islet amyloid polypeptide (IAPP) or Amylin is synthesized by the pancreatic beta-cells. |
| 6 | 1282806 | IAPP is the major component of islet amyloid in the pancreas of patients with non-insulin-dependent diabetes mellitus. |
| 7 | 1282806 | Characterization of the human islet amyloid polypeptide/amylin gene transcripts: identification of a new polyadenylation site. |
| 8 | 1282806 | Islet amyloid polypeptide (IAPP) or Amylin is synthesized by the pancreatic beta-cells. |
| 9 | 1282806 | IAPP is the major component of islet amyloid in the pancreas of patients with non-insulin-dependent diabetes mellitus. |
| 10 | 1282806 | Characterization of the human islet amyloid polypeptide/amylin gene transcripts: identification of a new polyadenylation site. |
| 11 | 1282806 | Islet amyloid polypeptide (IAPP) or Amylin is synthesized by the pancreatic beta-cells. |
| 12 | 1282806 | IAPP is the major component of islet amyloid in the pancreas of patients with non-insulin-dependent diabetes mellitus. |
| 13 | 1299966 | [A novel hormone in islet of pancreas--islet amyloid polypeptide]. |
| 14 | 1326785 | Islet amyloid polypeptide-producing pancreatic islet cell tumor. |
| 15 | 1326785 | The release of insulin and pancreatic polypeptide (PP) was totally absent after an oral glucose load and a mixed meal, respectively. |
| 16 | 1337737 | Homologous islet amyloid polypeptide: effects on plasma levels of glucagon, insulin and glucose in the mouse. |
| 17 | 1337737 | We examined the effects of a single intravenous injection of homologous islet amyloid polypeptide (IAPP) on the plasma levels of glucagon, insulin and glucose in the freely fed mouse. |
| 18 | 1337737 | Further, IAPP inhibited the insulin secretory response to beta 2-adrenoceptor stimulation. |
| 19 | 1337737 | It might also exhibit a negative feedback inhibition on beta 2-adrenoceptor-induced insulin secretion, but has little influence on glucose-induced insulin release. |
| 20 | 1337737 | Homologous islet amyloid polypeptide: effects on plasma levels of glucagon, insulin and glucose in the mouse. |
| 21 | 1337737 | We examined the effects of a single intravenous injection of homologous islet amyloid polypeptide (IAPP) on the plasma levels of glucagon, insulin and glucose in the freely fed mouse. |
| 22 | 1337737 | Further, IAPP inhibited the insulin secretory response to beta 2-adrenoceptor stimulation. |
| 23 | 1337737 | It might also exhibit a negative feedback inhibition on beta 2-adrenoceptor-induced insulin secretion, but has little influence on glucose-induced insulin release. |
| 24 | 1356906 | Immunochemical investigation of insulinomas for islet amyloid polypeptide and insulin: evidence for differential synthesis and storage. |
| 25 | 1356906 | An affinity purified antibody to fragment 14-29 of islet amyloid polypeptide (IAPP) has been prepared. |
| 26 | 1356906 | Islet amyloid polypeptide was found in six out of six insulinoma amyloid deposits, suggesting that the peptide is an invariable component of these deposits. |
| 27 | 1356906 | Over-expression of IAPP, with aberrant processing and/or secretion, may be the causative factor for amyloid deposition in insulinomas and in the islets of type 2 (non-insulin dependent) diabetic patients. |
| 28 | 1356906 | Immunochemical investigation of insulinomas for islet amyloid polypeptide and insulin: evidence for differential synthesis and storage. |
| 29 | 1356906 | An affinity purified antibody to fragment 14-29 of islet amyloid polypeptide (IAPP) has been prepared. |
| 30 | 1356906 | Islet amyloid polypeptide was found in six out of six insulinoma amyloid deposits, suggesting that the peptide is an invariable component of these deposits. |
| 31 | 1356906 | Over-expression of IAPP, with aberrant processing and/or secretion, may be the causative factor for amyloid deposition in insulinomas and in the islets of type 2 (non-insulin dependent) diabetic patients. |
| 32 | 1356906 | Immunochemical investigation of insulinomas for islet amyloid polypeptide and insulin: evidence for differential synthesis and storage. |
| 33 | 1356906 | An affinity purified antibody to fragment 14-29 of islet amyloid polypeptide (IAPP) has been prepared. |
| 34 | 1356906 | Islet amyloid polypeptide was found in six out of six insulinoma amyloid deposits, suggesting that the peptide is an invariable component of these deposits. |
| 35 | 1356906 | Over-expression of IAPP, with aberrant processing and/or secretion, may be the causative factor for amyloid deposition in insulinomas and in the islets of type 2 (non-insulin dependent) diabetic patients. |
| 36 | 1356906 | Immunochemical investigation of insulinomas for islet amyloid polypeptide and insulin: evidence for differential synthesis and storage. |
| 37 | 1356906 | An affinity purified antibody to fragment 14-29 of islet amyloid polypeptide (IAPP) has been prepared. |
| 38 | 1356906 | Islet amyloid polypeptide was found in six out of six insulinoma amyloid deposits, suggesting that the peptide is an invariable component of these deposits. |
| 39 | 1356906 | Over-expression of IAPP, with aberrant processing and/or secretion, may be the causative factor for amyloid deposition in insulinomas and in the islets of type 2 (non-insulin dependent) diabetic patients. |
| 40 | 1359959 | The islet amyloid polypeptide gene and non-insulin-dependent diabetes mellitus in south Indians. |
| 41 | 1359959 | Islet amyloid polypeptide (IAPP), otherwise called amylin, is the monomeric component of islet amyloid. |
| 42 | 1359959 | Deposition of this amyloid is a characteristic feature of non-insulin-dependent diabetes mellitus in humans and may play a role in the pathogenesis of the disease. |
| 43 | 1359959 | The islet amyloid polypeptide gene and non-insulin-dependent diabetes mellitus in south Indians. |
| 44 | 1359959 | Islet amyloid polypeptide (IAPP), otherwise called amylin, is the monomeric component of islet amyloid. |
| 45 | 1359959 | Deposition of this amyloid is a characteristic feature of non-insulin-dependent diabetes mellitus in humans and may play a role in the pathogenesis of the disease. |
| 46 | 1359959 | The islet amyloid polypeptide gene and non-insulin-dependent diabetes mellitus in south Indians. |
| 47 | 1359959 | Islet amyloid polypeptide (IAPP), otherwise called amylin, is the monomeric component of islet amyloid. |
| 48 | 1359959 | Deposition of this amyloid is a characteristic feature of non-insulin-dependent diabetes mellitus in humans and may play a role in the pathogenesis of the disease. |
| 49 | 1360719 | Human cytomegalovirus in the pancreas of patients with type 2 diabetes: is there a relation to clinical features, mRNA and protein expression of insulin, somatostatin, and MHC class II? |
| 50 | 1360719 | The present study addresses the question as to whether type 2 diabetes with an HCMV-positive pancreas differs from those with HCMV-negative pancreases with respect to age, sex, treatment, duration of disease, volume densities of B-cells and D-cells, mRNA levels of insulin and somatostatin, islet amyloid peptide deposits and major histocompatibility complex (MHC) class I and class II gene transcription, and protein expression. |
| 51 | 1362147 | Restriction fragment length polymorphisms near the islet amyloid polypeptide gene in Japanese subjects. |
| 52 | 1362147 | Two restriction fragment length polymorphisms (RFLPs) near the human islet amyloid polypeptide (IAPP) gene were examined in 50 Japanese patients with non-insulin-independent diabetes mellitus (NIDDM) and 54 non-diabetic controls. |
| 53 | 1362147 | Restriction fragment length polymorphisms near the islet amyloid polypeptide gene in Japanese subjects. |
| 54 | 1362147 | Two restriction fragment length polymorphisms (RFLPs) near the human islet amyloid polypeptide (IAPP) gene were examined in 50 Japanese patients with non-insulin-independent diabetes mellitus (NIDDM) and 54 non-diabetic controls. |
| 55 | 1371737 | Molecular biology of islet amyloid polypeptide. |
| 56 | 1371737 | We investigated the relationship between non-insulin-dependent diabetes mellitus (NIDDM) and islet amyloid polypeptide (IAPP) gene by restriction fragment length polymorphism (RFLP) and polymerase chain reaction (PCR)-direct sequencing analysis. |
| 57 | 1371737 | Molecular biology of islet amyloid polypeptide. |
| 58 | 1371737 | We investigated the relationship between non-insulin-dependent diabetes mellitus (NIDDM) and islet amyloid polypeptide (IAPP) gene by restriction fragment length polymorphism (RFLP) and polymerase chain reaction (PCR)-direct sequencing analysis. |
| 59 | 1383068 | Islet amyloid polypeptide/amylin in pancreatic beta-cell line derived from transgenic mouse insulinoma. |
| 60 | 1395480 | Failure to detect autoantibodies to islet amyloid polypeptide in sera from type 1 diabetic patients. |
| 61 | 1407245 | Amylin, also called islet amyloid polypeptide (IAPP), or diabetes-associated peptide (DAP) is a recently discovered 37 amino acid polypeptide which has been shown to be co-secreted with insulin from the pancreatic beta-cell. |
| 62 | 1407245 | The peptide turned out to be the major constituent of pancreatic amyloid deposits which are frequently found in the pancreas of type II diabetic patients. |
| 63 | 1407245 | Furthermore, it has been shown that amylin has the potential to antagonize the action of insulin on glucose metabolism by increasing hepatic glucose production and by decreasing muscle, but not adipocyte glucose uptake. |
| 64 | 1407245 | Amylin, also called islet amyloid polypeptide (IAPP), or diabetes-associated peptide (DAP) is a recently discovered 37 amino acid polypeptide which has been shown to be co-secreted with insulin from the pancreatic beta-cell. |
| 65 | 1407245 | The peptide turned out to be the major constituent of pancreatic amyloid deposits which are frequently found in the pancreas of type II diabetic patients. |
| 66 | 1407245 | Furthermore, it has been shown that amylin has the potential to antagonize the action of insulin on glucose metabolism by increasing hepatic glucose production and by decreasing muscle, but not adipocyte glucose uptake. |
| 67 | 1413495 | Immunohistology of islet amyloid polypeptide in diabetes mellitus: semi-quantitative studies in a post-mortem series. |
| 68 | 1413495 | Immunoreactivity for islet amyloid polypeptide (IAPP) in the islets of Langerhans of non-insulin-dependent diabetic patients and non-diabetic patients of a non-selected post-mortem series was studied with a new polyclonal IAPP antibody. |
| 69 | 1413495 | Of 100 patients with non-insulin-dependent diabetes mellitus (NIDDM) and islet amyloid, 98 exhibited IAPP-positive deposits and 71 exhibited intracellular immunoreactivity. |
| 70 | 1413495 | Immunohistology of islet amyloid polypeptide in diabetes mellitus: semi-quantitative studies in a post-mortem series. |
| 71 | 1413495 | Immunoreactivity for islet amyloid polypeptide (IAPP) in the islets of Langerhans of non-insulin-dependent diabetic patients and non-diabetic patients of a non-selected post-mortem series was studied with a new polyclonal IAPP antibody. |
| 72 | 1413495 | Of 100 patients with non-insulin-dependent diabetes mellitus (NIDDM) and islet amyloid, 98 exhibited IAPP-positive deposits and 71 exhibited intracellular immunoreactivity. |
| 73 | 1413495 | Immunohistology of islet amyloid polypeptide in diabetes mellitus: semi-quantitative studies in a post-mortem series. |
| 74 | 1413495 | Immunoreactivity for islet amyloid polypeptide (IAPP) in the islets of Langerhans of non-insulin-dependent diabetic patients and non-diabetic patients of a non-selected post-mortem series was studied with a new polyclonal IAPP antibody. |
| 75 | 1413495 | Of 100 patients with non-insulin-dependent diabetes mellitus (NIDDM) and islet amyloid, 98 exhibited IAPP-positive deposits and 71 exhibited intracellular immunoreactivity. |
| 76 | 1414504 | Amylin (also known as islet amyloid polypeptide and diabetes-associated peptide) has recently been shown by us to have a potent hypocalcemic effect in rat and rabbit owing to inhibition of osteoclast-mediated bone resorption. |
| 77 | 1434057 | Therefore we suspected cystatin C deposit amyloid angiopathy. |
| 78 | 1453875 | Amylin can precipitate out in these cells to form amyloid. |
| 79 | 1453875 | Amylin has a number of effects that may counteract the effect of secreted insulin, i.e., decreased second phase insulin secretion, increased hepatic glucose output, and inhibition of insulin effects on skeletal muscle. |
| 80 | 1473619 | Detection of autoantibodies against islet amyloid polypeptide in human serum. |
| 81 | 1473619 | Lack of association with type 1 (insulin-dependent) diabetes mellitus, or with conditions favouring amyloid deposition in islets. |
| 82 | 1473619 | A radiobinding assay for the detection of autoantibodies against islet amyloid polypeptide was developed, analytically validated, and--in parallel with a similar assay for the detection of autoantibodies against insulin--applied to sera from recent-onset Type 1 (insulin-dependent) diabetic patients and from age- and sex-matched control subjects. |
| 83 | 1473619 | There was no difference in islet amyloid polypeptide autoantibody titres between patient groups and matched control subjects, nor within subject groups according to age. |
| 84 | 1473619 | At onset of Type 1 diabetes, elevated islet amyloid polypeptide-autoantibody levels (> 97th percentile of control subjects) were only detected in 1 of 30 patients aged 0-19 years and in 2 of 35 patients aged 20-39 years. |
| 85 | 1473619 | Islet amyloid polypeptide autoantibodies were not detectable in 3 insulinoma patients nor in 37 patients (aged 33-70 years) with Type 2 diabetes (vs 1 of 40 in matched control subjects). |
| 86 | 1473619 | In positive serum, adsorption onto protein A-Sepharose removed islet amyloid polypeptide binding activity, hereby confirming its antibody nature. |
| 87 | 1473619 | In conclusion, Type 1 diabetes is associated with an age-dependent autoantibody reaction against insulin but not against islet amyloid polypeptide. |
| 88 | 1473619 | Conditions associated with amyloid deposition in islets (Type 2 diabetes, insulinoma and ageing) do not favour the formation of autoantibodies against islet amyloid polypeptide. |
| 89 | 1473619 | Detection of autoantibodies against islet amyloid polypeptide in human serum. |
| 90 | 1473619 | Lack of association with type 1 (insulin-dependent) diabetes mellitus, or with conditions favouring amyloid deposition in islets. |
| 91 | 1473619 | A radiobinding assay for the detection of autoantibodies against islet amyloid polypeptide was developed, analytically validated, and--in parallel with a similar assay for the detection of autoantibodies against insulin--applied to sera from recent-onset Type 1 (insulin-dependent) diabetic patients and from age- and sex-matched control subjects. |
| 92 | 1473619 | There was no difference in islet amyloid polypeptide autoantibody titres between patient groups and matched control subjects, nor within subject groups according to age. |
| 93 | 1473619 | At onset of Type 1 diabetes, elevated islet amyloid polypeptide-autoantibody levels (> 97th percentile of control subjects) were only detected in 1 of 30 patients aged 0-19 years and in 2 of 35 patients aged 20-39 years. |
| 94 | 1473619 | Islet amyloid polypeptide autoantibodies were not detectable in 3 insulinoma patients nor in 37 patients (aged 33-70 years) with Type 2 diabetes (vs 1 of 40 in matched control subjects). |
| 95 | 1473619 | In positive serum, adsorption onto protein A-Sepharose removed islet amyloid polypeptide binding activity, hereby confirming its antibody nature. |
| 96 | 1473619 | In conclusion, Type 1 diabetes is associated with an age-dependent autoantibody reaction against insulin but not against islet amyloid polypeptide. |
| 97 | 1473619 | Conditions associated with amyloid deposition in islets (Type 2 diabetes, insulinoma and ageing) do not favour the formation of autoantibodies against islet amyloid polypeptide. |
| 98 | 1473619 | Detection of autoantibodies against islet amyloid polypeptide in human serum. |
| 99 | 1473619 | Lack of association with type 1 (insulin-dependent) diabetes mellitus, or with conditions favouring amyloid deposition in islets. |
| 100 | 1473619 | A radiobinding assay for the detection of autoantibodies against islet amyloid polypeptide was developed, analytically validated, and--in parallel with a similar assay for the detection of autoantibodies against insulin--applied to sera from recent-onset Type 1 (insulin-dependent) diabetic patients and from age- and sex-matched control subjects. |
| 101 | 1473619 | There was no difference in islet amyloid polypeptide autoantibody titres between patient groups and matched control subjects, nor within subject groups according to age. |
| 102 | 1473619 | At onset of Type 1 diabetes, elevated islet amyloid polypeptide-autoantibody levels (> 97th percentile of control subjects) were only detected in 1 of 30 patients aged 0-19 years and in 2 of 35 patients aged 20-39 years. |
| 103 | 1473619 | Islet amyloid polypeptide autoantibodies were not detectable in 3 insulinoma patients nor in 37 patients (aged 33-70 years) with Type 2 diabetes (vs 1 of 40 in matched control subjects). |
| 104 | 1473619 | In positive serum, adsorption onto protein A-Sepharose removed islet amyloid polypeptide binding activity, hereby confirming its antibody nature. |
| 105 | 1473619 | In conclusion, Type 1 diabetes is associated with an age-dependent autoantibody reaction against insulin but not against islet amyloid polypeptide. |
| 106 | 1473619 | Conditions associated with amyloid deposition in islets (Type 2 diabetes, insulinoma and ageing) do not favour the formation of autoantibodies against islet amyloid polypeptide. |
| 107 | 1473619 | Detection of autoantibodies against islet amyloid polypeptide in human serum. |
| 108 | 1473619 | Lack of association with type 1 (insulin-dependent) diabetes mellitus, or with conditions favouring amyloid deposition in islets. |
| 109 | 1473619 | A radiobinding assay for the detection of autoantibodies against islet amyloid polypeptide was developed, analytically validated, and--in parallel with a similar assay for the detection of autoantibodies against insulin--applied to sera from recent-onset Type 1 (insulin-dependent) diabetic patients and from age- and sex-matched control subjects. |
| 110 | 1473619 | There was no difference in islet amyloid polypeptide autoantibody titres between patient groups and matched control subjects, nor within subject groups according to age. |
| 111 | 1473619 | At onset of Type 1 diabetes, elevated islet amyloid polypeptide-autoantibody levels (> 97th percentile of control subjects) were only detected in 1 of 30 patients aged 0-19 years and in 2 of 35 patients aged 20-39 years. |
| 112 | 1473619 | Islet amyloid polypeptide autoantibodies were not detectable in 3 insulinoma patients nor in 37 patients (aged 33-70 years) with Type 2 diabetes (vs 1 of 40 in matched control subjects). |
| 113 | 1473619 | In positive serum, adsorption onto protein A-Sepharose removed islet amyloid polypeptide binding activity, hereby confirming its antibody nature. |
| 114 | 1473619 | In conclusion, Type 1 diabetes is associated with an age-dependent autoantibody reaction against insulin but not against islet amyloid polypeptide. |
| 115 | 1473619 | Conditions associated with amyloid deposition in islets (Type 2 diabetes, insulinoma and ageing) do not favour the formation of autoantibodies against islet amyloid polypeptide. |
| 116 | 1473619 | Detection of autoantibodies against islet amyloid polypeptide in human serum. |
| 117 | 1473619 | Lack of association with type 1 (insulin-dependent) diabetes mellitus, or with conditions favouring amyloid deposition in islets. |
| 118 | 1473619 | A radiobinding assay for the detection of autoantibodies against islet amyloid polypeptide was developed, analytically validated, and--in parallel with a similar assay for the detection of autoantibodies against insulin--applied to sera from recent-onset Type 1 (insulin-dependent) diabetic patients and from age- and sex-matched control subjects. |
| 119 | 1473619 | There was no difference in islet amyloid polypeptide autoantibody titres between patient groups and matched control subjects, nor within subject groups according to age. |
| 120 | 1473619 | At onset of Type 1 diabetes, elevated islet amyloid polypeptide-autoantibody levels (> 97th percentile of control subjects) were only detected in 1 of 30 patients aged 0-19 years and in 2 of 35 patients aged 20-39 years. |
| 121 | 1473619 | Islet amyloid polypeptide autoantibodies were not detectable in 3 insulinoma patients nor in 37 patients (aged 33-70 years) with Type 2 diabetes (vs 1 of 40 in matched control subjects). |
| 122 | 1473619 | In positive serum, adsorption onto protein A-Sepharose removed islet amyloid polypeptide binding activity, hereby confirming its antibody nature. |
| 123 | 1473619 | In conclusion, Type 1 diabetes is associated with an age-dependent autoantibody reaction against insulin but not against islet amyloid polypeptide. |
| 124 | 1473619 | Conditions associated with amyloid deposition in islets (Type 2 diabetes, insulinoma and ageing) do not favour the formation of autoantibodies against islet amyloid polypeptide. |
| 125 | 1473619 | Detection of autoantibodies against islet amyloid polypeptide in human serum. |
| 126 | 1473619 | Lack of association with type 1 (insulin-dependent) diabetes mellitus, or with conditions favouring amyloid deposition in islets. |
| 127 | 1473619 | A radiobinding assay for the detection of autoantibodies against islet amyloid polypeptide was developed, analytically validated, and--in parallel with a similar assay for the detection of autoantibodies against insulin--applied to sera from recent-onset Type 1 (insulin-dependent) diabetic patients and from age- and sex-matched control subjects. |
| 128 | 1473619 | There was no difference in islet amyloid polypeptide autoantibody titres between patient groups and matched control subjects, nor within subject groups according to age. |
| 129 | 1473619 | At onset of Type 1 diabetes, elevated islet amyloid polypeptide-autoantibody levels (> 97th percentile of control subjects) were only detected in 1 of 30 patients aged 0-19 years and in 2 of 35 patients aged 20-39 years. |
| 130 | 1473619 | Islet amyloid polypeptide autoantibodies were not detectable in 3 insulinoma patients nor in 37 patients (aged 33-70 years) with Type 2 diabetes (vs 1 of 40 in matched control subjects). |
| 131 | 1473619 | In positive serum, adsorption onto protein A-Sepharose removed islet amyloid polypeptide binding activity, hereby confirming its antibody nature. |
| 132 | 1473619 | In conclusion, Type 1 diabetes is associated with an age-dependent autoantibody reaction against insulin but not against islet amyloid polypeptide. |
| 133 | 1473619 | Conditions associated with amyloid deposition in islets (Type 2 diabetes, insulinoma and ageing) do not favour the formation of autoantibodies against islet amyloid polypeptide. |
| 134 | 1473619 | Detection of autoantibodies against islet amyloid polypeptide in human serum. |
| 135 | 1473619 | Lack of association with type 1 (insulin-dependent) diabetes mellitus, or with conditions favouring amyloid deposition in islets. |
| 136 | 1473619 | A radiobinding assay for the detection of autoantibodies against islet amyloid polypeptide was developed, analytically validated, and--in parallel with a similar assay for the detection of autoantibodies against insulin--applied to sera from recent-onset Type 1 (insulin-dependent) diabetic patients and from age- and sex-matched control subjects. |
| 137 | 1473619 | There was no difference in islet amyloid polypeptide autoantibody titres between patient groups and matched control subjects, nor within subject groups according to age. |
| 138 | 1473619 | At onset of Type 1 diabetes, elevated islet amyloid polypeptide-autoantibody levels (> 97th percentile of control subjects) were only detected in 1 of 30 patients aged 0-19 years and in 2 of 35 patients aged 20-39 years. |
| 139 | 1473619 | Islet amyloid polypeptide autoantibodies were not detectable in 3 insulinoma patients nor in 37 patients (aged 33-70 years) with Type 2 diabetes (vs 1 of 40 in matched control subjects). |
| 140 | 1473619 | In positive serum, adsorption onto protein A-Sepharose removed islet amyloid polypeptide binding activity, hereby confirming its antibody nature. |
| 141 | 1473619 | In conclusion, Type 1 diabetes is associated with an age-dependent autoantibody reaction against insulin but not against islet amyloid polypeptide. |
| 142 | 1473619 | Conditions associated with amyloid deposition in islets (Type 2 diabetes, insulinoma and ageing) do not favour the formation of autoantibodies against islet amyloid polypeptide. |
| 143 | 1473619 | Detection of autoantibodies against islet amyloid polypeptide in human serum. |
| 144 | 1473619 | Lack of association with type 1 (insulin-dependent) diabetes mellitus, or with conditions favouring amyloid deposition in islets. |
| 145 | 1473619 | A radiobinding assay for the detection of autoantibodies against islet amyloid polypeptide was developed, analytically validated, and--in parallel with a similar assay for the detection of autoantibodies against insulin--applied to sera from recent-onset Type 1 (insulin-dependent) diabetic patients and from age- and sex-matched control subjects. |
| 146 | 1473619 | There was no difference in islet amyloid polypeptide autoantibody titres between patient groups and matched control subjects, nor within subject groups according to age. |
| 147 | 1473619 | At onset of Type 1 diabetes, elevated islet amyloid polypeptide-autoantibody levels (> 97th percentile of control subjects) were only detected in 1 of 30 patients aged 0-19 years and in 2 of 35 patients aged 20-39 years. |
| 148 | 1473619 | Islet amyloid polypeptide autoantibodies were not detectable in 3 insulinoma patients nor in 37 patients (aged 33-70 years) with Type 2 diabetes (vs 1 of 40 in matched control subjects). |
| 149 | 1473619 | In positive serum, adsorption onto protein A-Sepharose removed islet amyloid polypeptide binding activity, hereby confirming its antibody nature. |
| 150 | 1473619 | In conclusion, Type 1 diabetes is associated with an age-dependent autoantibody reaction against insulin but not against islet amyloid polypeptide. |
| 151 | 1473619 | Conditions associated with amyloid deposition in islets (Type 2 diabetes, insulinoma and ageing) do not favour the formation of autoantibodies against islet amyloid polypeptide. |
| 152 | 1473619 | Detection of autoantibodies against islet amyloid polypeptide in human serum. |
| 153 | 1473619 | Lack of association with type 1 (insulin-dependent) diabetes mellitus, or with conditions favouring amyloid deposition in islets. |
| 154 | 1473619 | A radiobinding assay for the detection of autoantibodies against islet amyloid polypeptide was developed, analytically validated, and--in parallel with a similar assay for the detection of autoantibodies against insulin--applied to sera from recent-onset Type 1 (insulin-dependent) diabetic patients and from age- and sex-matched control subjects. |
| 155 | 1473619 | There was no difference in islet amyloid polypeptide autoantibody titres between patient groups and matched control subjects, nor within subject groups according to age. |
| 156 | 1473619 | At onset of Type 1 diabetes, elevated islet amyloid polypeptide-autoantibody levels (> 97th percentile of control subjects) were only detected in 1 of 30 patients aged 0-19 years and in 2 of 35 patients aged 20-39 years. |
| 157 | 1473619 | Islet amyloid polypeptide autoantibodies were not detectable in 3 insulinoma patients nor in 37 patients (aged 33-70 years) with Type 2 diabetes (vs 1 of 40 in matched control subjects). |
| 158 | 1473619 | In positive serum, adsorption onto protein A-Sepharose removed islet amyloid polypeptide binding activity, hereby confirming its antibody nature. |
| 159 | 1473619 | In conclusion, Type 1 diabetes is associated with an age-dependent autoantibody reaction against insulin but not against islet amyloid polypeptide. |
| 160 | 1473619 | Conditions associated with amyloid deposition in islets (Type 2 diabetes, insulinoma and ageing) do not favour the formation of autoantibodies against islet amyloid polypeptide. |
| 161 | 1497641 | Establishment of hypersensitive radioimmunoassay for islet amyloid polypeptide using antiserum specific for its N-terminal region. |
| 162 | 1497641 | Using a synthetic N-terminal hexadecapeptide of islet amyloid polypeptide (IAPP), we prepared an antiserum specific for IAPP[1-16] and established an extremely sensitive radioimmunoassay (RIA) for the peptide with a minimum detection level of 0.26 fmol/tube. |
| 163 | 1497641 | Establishment of hypersensitive radioimmunoassay for islet amyloid polypeptide using antiserum specific for its N-terminal region. |
| 164 | 1497641 | Using a synthetic N-terminal hexadecapeptide of islet amyloid polypeptide (IAPP), we prepared an antiserum specific for IAPP[1-16] and established an extremely sensitive radioimmunoassay (RIA) for the peptide with a minimum detection level of 0.26 fmol/tube. |
| 165 | 1516756 | Islet amyloid polypeptide--a novel controversy in diabetes research. |
| 166 | 1524461 | Localization of the basement membrane heparan sulfate proteoglycan in islet amyloid deposits in type II diabetes mellitus. |
| 167 | 1524461 | Although the mechanisms of islet amyloid fibrillogenesis are unknown, the presence of heparan sulfate proteoglycan in many other forms of amyloid suggests a role for this proteoglycan in amyloidogenesis in general. |
| 168 | 1524461 | In this study, islet amyloid was evaluated for the presence of the basement membrane heparan sulfate proteoglycan using histochemical and immunohistochemical techniques. |
| 169 | 1524461 | Staining with sodium sulfate-alcian blue identified highly sulfated glycosaminoglycans within all islet amyloid deposits, and anti-basement membrane heparan sulfate proteoglycan antisera localized this specific proteoglycan within the islet amyloid. |
| 170 | 1524461 | The presence of the basement membrane heparan sulfate proteoglycan links islet amyloid to other disparate forms of amyloid and further supports the hypothesis that it has a role in a common pathway of amyloid fibrillogenesis. |
| 171 | 1524461 | Localization of the basement membrane heparan sulfate proteoglycan in islet amyloid deposits in type II diabetes mellitus. |
| 172 | 1524461 | Although the mechanisms of islet amyloid fibrillogenesis are unknown, the presence of heparan sulfate proteoglycan in many other forms of amyloid suggests a role for this proteoglycan in amyloidogenesis in general. |
| 173 | 1524461 | In this study, islet amyloid was evaluated for the presence of the basement membrane heparan sulfate proteoglycan using histochemical and immunohistochemical techniques. |
| 174 | 1524461 | Staining with sodium sulfate-alcian blue identified highly sulfated glycosaminoglycans within all islet amyloid deposits, and anti-basement membrane heparan sulfate proteoglycan antisera localized this specific proteoglycan within the islet amyloid. |
| 175 | 1524461 | The presence of the basement membrane heparan sulfate proteoglycan links islet amyloid to other disparate forms of amyloid and further supports the hypothesis that it has a role in a common pathway of amyloid fibrillogenesis. |
| 176 | 1524461 | Localization of the basement membrane heparan sulfate proteoglycan in islet amyloid deposits in type II diabetes mellitus. |
| 177 | 1524461 | Although the mechanisms of islet amyloid fibrillogenesis are unknown, the presence of heparan sulfate proteoglycan in many other forms of amyloid suggests a role for this proteoglycan in amyloidogenesis in general. |
| 178 | 1524461 | In this study, islet amyloid was evaluated for the presence of the basement membrane heparan sulfate proteoglycan using histochemical and immunohistochemical techniques. |
| 179 | 1524461 | Staining with sodium sulfate-alcian blue identified highly sulfated glycosaminoglycans within all islet amyloid deposits, and anti-basement membrane heparan sulfate proteoglycan antisera localized this specific proteoglycan within the islet amyloid. |
| 180 | 1524461 | The presence of the basement membrane heparan sulfate proteoglycan links islet amyloid to other disparate forms of amyloid and further supports the hypothesis that it has a role in a common pathway of amyloid fibrillogenesis. |
| 181 | 1524461 | Localization of the basement membrane heparan sulfate proteoglycan in islet amyloid deposits in type II diabetes mellitus. |
| 182 | 1524461 | Although the mechanisms of islet amyloid fibrillogenesis are unknown, the presence of heparan sulfate proteoglycan in many other forms of amyloid suggests a role for this proteoglycan in amyloidogenesis in general. |
| 183 | 1524461 | In this study, islet amyloid was evaluated for the presence of the basement membrane heparan sulfate proteoglycan using histochemical and immunohistochemical techniques. |
| 184 | 1524461 | Staining with sodium sulfate-alcian blue identified highly sulfated glycosaminoglycans within all islet amyloid deposits, and anti-basement membrane heparan sulfate proteoglycan antisera localized this specific proteoglycan within the islet amyloid. |
| 185 | 1524461 | The presence of the basement membrane heparan sulfate proteoglycan links islet amyloid to other disparate forms of amyloid and further supports the hypothesis that it has a role in a common pathway of amyloid fibrillogenesis. |
| 186 | 1524461 | Localization of the basement membrane heparan sulfate proteoglycan in islet amyloid deposits in type II diabetes mellitus. |
| 187 | 1524461 | Although the mechanisms of islet amyloid fibrillogenesis are unknown, the presence of heparan sulfate proteoglycan in many other forms of amyloid suggests a role for this proteoglycan in amyloidogenesis in general. |
| 188 | 1524461 | In this study, islet amyloid was evaluated for the presence of the basement membrane heparan sulfate proteoglycan using histochemical and immunohistochemical techniques. |
| 189 | 1524461 | Staining with sodium sulfate-alcian blue identified highly sulfated glycosaminoglycans within all islet amyloid deposits, and anti-basement membrane heparan sulfate proteoglycan antisera localized this specific proteoglycan within the islet amyloid. |
| 190 | 1524461 | The presence of the basement membrane heparan sulfate proteoglycan links islet amyloid to other disparate forms of amyloid and further supports the hypothesis that it has a role in a common pathway of amyloid fibrillogenesis. |
| 191 | 1534057 | With isolated perfused pancreases from normal and diabetic model rats, we studied alterations of the secretion of islet amyloid polypeptide, or amylin, which has been recently identified as a major component of amyloid deposits in the pancreatic islets of patients with non-insulin-dependent diabetes mellitus. |
| 192 | 1541229 | Relationship between islet amyloid polypeptide (IAPP) deposition and insulin response and beta-cell volume in diabetes mellitus. |
| 193 | 1541230 | Islet amyloid polypeptide-derived amyloid deposition increases along with the duration of type 2 diabetes mellitus. |
| 194 | 1541230 | To investigate the involvement of islet amyloid polypeptide (IAPP) and amyloid deposits in the pathophysiology of this disease, we studied the relationship between IAPP-derived amyloid deposition and the clinical features in type 2 diabetes mellitus. |
| 195 | 1541230 | Islet amyloid polypeptide-derived amyloid deposition increases along with the duration of type 2 diabetes mellitus. |
| 196 | 1541230 | To investigate the involvement of islet amyloid polypeptide (IAPP) and amyloid deposits in the pathophysiology of this disease, we studied the relationship between IAPP-derived amyloid deposition and the clinical features in type 2 diabetes mellitus. |
| 197 | 1541231 | To investigate the possible role of islet amyloid polypeptide (IAPP) in the development of type 2 diabetes mellitus, we examined the IAPP content and secretion in pancreatic islets isolated from ventromedial hypothalamic (VMH)-lesioned rats and genetically obese Zucker rats, using a specific radioimmunoassay for IAPP. |
| 198 | 1541232 | Islet amyloid polypeptide (IAPP) and pancreatic islet amyloid deposition in diabetic and non-diabetic patients. |
| 199 | 1541232 | Twenty pancreata of non-diabetic patients and 17 pancreata of diabetic patients, including two patients with insulin-dependent diabetes mellitus, were immunohistochemically studied using antiserum against human islet amyloid polypeptide (IAPP). |
| 200 | 1541232 | The decreased immunoreactivity for IAPP suggested an initial stage of disturbed beta-cell function, even if the immunoreactivity for insulin was apparently intact or the amyloid deposition in the islets was insignificant. |
| 201 | 1541232 | Islet amyloid polypeptide (IAPP) and pancreatic islet amyloid deposition in diabetic and non-diabetic patients. |
| 202 | 1541232 | Twenty pancreata of non-diabetic patients and 17 pancreata of diabetic patients, including two patients with insulin-dependent diabetes mellitus, were immunohistochemically studied using antiserum against human islet amyloid polypeptide (IAPP). |
| 203 | 1541232 | The decreased immunoreactivity for IAPP suggested an initial stage of disturbed beta-cell function, even if the immunoreactivity for insulin was apparently intact or the amyloid deposition in the islets was insignificant. |
| 204 | 1541232 | Islet amyloid polypeptide (IAPP) and pancreatic islet amyloid deposition in diabetic and non-diabetic patients. |
| 205 | 1541232 | Twenty pancreata of non-diabetic patients and 17 pancreata of diabetic patients, including two patients with insulin-dependent diabetes mellitus, were immunohistochemically studied using antiserum against human islet amyloid polypeptide (IAPP). |
| 206 | 1541232 | The decreased immunoreactivity for IAPP suggested an initial stage of disturbed beta-cell function, even if the immunoreactivity for insulin was apparently intact or the amyloid deposition in the islets was insignificant. |
| 207 | 1541233 | Molecular forms of islet amyloid polypeptide (IAPP/amylin) in four mammals. |
| 208 | 1541233 | Using reverse-phase high performance liquid chromatography combined with radioimmunoassays for human and rat/mouse islet amyloid polypeptide (IAPP), we identified molecular forms of IAPPs in pancreata of four mammals including species in which islet amyloid deposition occurs (human and cat) and those in which amyloid deposition does not occur (rat and mouse). |
| 209 | 1541233 | Molecular forms of islet amyloid polypeptide (IAPP/amylin) in four mammals. |
| 210 | 1541233 | Using reverse-phase high performance liquid chromatography combined with radioimmunoassays for human and rat/mouse islet amyloid polypeptide (IAPP), we identified molecular forms of IAPPs in pancreata of four mammals including species in which islet amyloid deposition occurs (human and cat) and those in which amyloid deposition does not occur (rat and mouse). |
| 211 | 1541234 | Islet amyloid polypeptide (IAPP) gene analysis in a Japanese diabetic with marked islet amyloid deposition. |
| 212 | 1541234 | Islet amyloid polypeptide (IAPP) is a major constituent of pancreatic amyloid deposits in many patients with non-insulin-dependent diabetes mellitus (NIDDM). |
| 213 | 1541234 | Islet amyloid polypeptide (IAPP) gene analysis in a Japanese diabetic with marked islet amyloid deposition. |
| 214 | 1541234 | Islet amyloid polypeptide (IAPP) is a major constituent of pancreatic amyloid deposits in many patients with non-insulin-dependent diabetes mellitus (NIDDM). |
| 215 | 1541235 | Effects of islet amyloid polypeptide (IAPP) on insulin biosynthesis or secretion in rat islets and mouse beta TC3 cells. |
| 216 | 1541235 | Effects of rat islet amyloid polypeptide (IAPP) on insulin biosynthesis and secretion were examined in isolated rat islets and mouse beta TC3 cells. |
| 217 | 1541235 | Effects of islet amyloid polypeptide (IAPP) on insulin biosynthesis or secretion in rat islets and mouse beta TC3 cells. |
| 218 | 1541235 | Effects of rat islet amyloid polypeptide (IAPP) on insulin biosynthesis and secretion were examined in isolated rat islets and mouse beta TC3 cells. |
| 219 | 1541236 | Islet amyloid polypeptide (IAPP/amylin) causes insulin resistance in perfused rat hindlimb muscle. |
| 220 | 1541236 | It has been reported that islet amyloid polypeptide (IAPP) has insulin antagonistic effects in vivo and in vitro. |
| 221 | 1541236 | Rat calcitonin gene-related peptide (CGRP), which has sequence homology with IAPP and has been reported to inhibit insulin action, was also administered. |
| 222 | 1541236 | Therefore, IAPP directly reduced only the insulin-mediated GU in the skeletal muscle, and this effect of IAPP occurred at the same dose as that of CGRP. |
| 223 | 1541236 | These data suggest that both IAPP and CGRP may cause insulin resistance in skeletal muscle not through a CGRP receptor but a yet unknown receptor, which has similar binding affinity for both IAPP and CGRP. |
| 224 | 1541236 | Islet amyloid polypeptide (IAPP/amylin) causes insulin resistance in perfused rat hindlimb muscle. |
| 225 | 1541236 | It has been reported that islet amyloid polypeptide (IAPP) has insulin antagonistic effects in vivo and in vitro. |
| 226 | 1541236 | Rat calcitonin gene-related peptide (CGRP), which has sequence homology with IAPP and has been reported to inhibit insulin action, was also administered. |
| 227 | 1541236 | Therefore, IAPP directly reduced only the insulin-mediated GU in the skeletal muscle, and this effect of IAPP occurred at the same dose as that of CGRP. |
| 228 | 1541236 | These data suggest that both IAPP and CGRP may cause insulin resistance in skeletal muscle not through a CGRP receptor but a yet unknown receptor, which has similar binding affinity for both IAPP and CGRP. |
| 229 | 1541237 | Effects of islet amyloid polypeptide (amylin) and calcitonin gene-related peptide (CGRP) on glucose metabolism in the rat. |
| 230 | 1541237 | In this study, we compared the effects of islet amyloid polypeptide (IAPP) and calcitonin gene-related peptide (CGRP) on glucose metabolism both in vivo and in vitro in the rat. |
| 231 | 1541237 | Intravenous injection of rat CGRP caused a significant increase in plasma glucose concentration with a simultaneous increase in plasma insulin levels, whereas neither IAPP-NH2 nor IAPP-COOH had any effect. |
| 232 | 1541237 | Moreover, intravenous infusion of CGRP decreased tolerance to intragastric administration of glucose (O-GTT) without altering plasma insulin levels, but again IAPPs had no effect. |
| 233 | 1541237 | Conversely, CGRP as well as IAPP-NH2 but not IAPP-COOH evoked dose-dependent activation of adenylate cyclase in the membranes, and these effects were significantly inhibited by a CGRP receptor antagonist, human CGRP-I(8-37). |
| 234 | 1541237 | These results suggest that (1) IAPP-NH2 but not IAPP-COOH induces adenylate cyclase activation via CGRP receptors on rat liver plasma membranes, and (2) CGRP might not involve its action on the liver in the changes of glucose metabolism. |
| 235 | 1541237 | Effects of islet amyloid polypeptide (amylin) and calcitonin gene-related peptide (CGRP) on glucose metabolism in the rat. |
| 236 | 1541237 | In this study, we compared the effects of islet amyloid polypeptide (IAPP) and calcitonin gene-related peptide (CGRP) on glucose metabolism both in vivo and in vitro in the rat. |
| 237 | 1541237 | Intravenous injection of rat CGRP caused a significant increase in plasma glucose concentration with a simultaneous increase in plasma insulin levels, whereas neither IAPP-NH2 nor IAPP-COOH had any effect. |
| 238 | 1541237 | Moreover, intravenous infusion of CGRP decreased tolerance to intragastric administration of glucose (O-GTT) without altering plasma insulin levels, but again IAPPs had no effect. |
| 239 | 1541237 | Conversely, CGRP as well as IAPP-NH2 but not IAPP-COOH evoked dose-dependent activation of adenylate cyclase in the membranes, and these effects were significantly inhibited by a CGRP receptor antagonist, human CGRP-I(8-37). |
| 240 | 1541237 | These results suggest that (1) IAPP-NH2 but not IAPP-COOH induces adenylate cyclase activation via CGRP receptors on rat liver plasma membranes, and (2) CGRP might not involve its action on the liver in the changes of glucose metabolism. |
| 241 | 1541239 | Amylin is a 37-amino acid peptide isolated from pancreatic islet amyloid of patients with non-insulin-dependent diabetes mellitus (NIDDM). |
| 242 | 1541240 | Islet amyloid polypeptide (IAPP) secretion from islet cells and its plasma concentration in patients with non-insulin-dependent diabetes mellitus. |
| 243 | 1541240 | Islet amyloid polypeptide (IAPP/Amylin) is a novel peptide which was extracted from islet amyloid deposits in patients with non-insulin-dependent diabetes mellitus (NIDDM). |
| 244 | 1541240 | Islet amyloid polypeptide (IAPP) secretion from islet cells and its plasma concentration in patients with non-insulin-dependent diabetes mellitus. |
| 245 | 1541240 | Islet amyloid polypeptide (IAPP/Amylin) is a novel peptide which was extracted from islet amyloid deposits in patients with non-insulin-dependent diabetes mellitus (NIDDM). |
| 246 | 1541238 | Effect of islet amyloid polypeptide (IAPP/amylin) on 2-deoxyglucose uptake in mouse pancreatic acini. |
| 247 | 1541238 | In order to examine the effect of islet amyloid polypeptide (IAPP/amylin), a product of the pancreatic beta cell and a major component of islet amyloid deposits, on exocrine pancreatic function, we studied the effect of rat IAPP amide (IAPP-NH2) on 2-deoxy-D-glucose (2-DG) uptake in isolated mouse pancreatic acini. |
| 248 | 1541238 | Effect of islet amyloid polypeptide (IAPP/amylin) on 2-deoxyglucose uptake in mouse pancreatic acini. |
| 249 | 1541238 | In order to examine the effect of islet amyloid polypeptide (IAPP/amylin), a product of the pancreatic beta cell and a major component of islet amyloid deposits, on exocrine pancreatic function, we studied the effect of rat IAPP amide (IAPP-NH2) on 2-deoxy-D-glucose (2-DG) uptake in isolated mouse pancreatic acini. |
| 250 | 1541241 | Plasma islet amyloid polypeptide levels in obesity, impaired glucose tolerance and non-insulin-dependent diabetes mellitus. |
| 251 | 1541241 | We examined the response of plasma islet amyloid polypeptide (IAPP) to an oral glucose load in non-obese and obese subjects with normal glucose tolerance or impaired glucose tolerance (IGT), and in non-obese patients with non-insulin-dependent diabetes mellitus (NIDDM). |
| 252 | 1541241 | Plasma islet amyloid polypeptide levels in obesity, impaired glucose tolerance and non-insulin-dependent diabetes mellitus. |
| 253 | 1541241 | We examined the response of plasma islet amyloid polypeptide (IAPP) to an oral glucose load in non-obese and obese subjects with normal glucose tolerance or impaired glucose tolerance (IGT), and in non-obese patients with non-insulin-dependent diabetes mellitus (NIDDM). |
| 254 | 1556951 | Lack of effect of islet amyloid polypeptide on hepatic glucose output in the in situ-perfused rat liver. |
| 255 | 1556951 | Islet amyloid polypeptide (IAPP), a novel peptide isolated from islet amyloid deposits in patients with insulinoma and non-insulin-dependent diabetes mellitus (NIDDM), has been reported to be cosecreted with insulin from pancreatic beta cells and to inhibit glucose uptake and glycogen synthesis in muscle tissue in vitro. |
| 256 | 1556951 | Lack of effect of islet amyloid polypeptide on hepatic glucose output in the in situ-perfused rat liver. |
| 257 | 1556951 | Islet amyloid polypeptide (IAPP), a novel peptide isolated from islet amyloid deposits in patients with insulinoma and non-insulin-dependent diabetes mellitus (NIDDM), has been reported to be cosecreted with insulin from pancreatic beta cells and to inhibit glucose uptake and glycogen synthesis in muscle tissue in vitro. |
| 258 | 1563328 | Effects of aging on plasma islet amyloid polypeptide basal level and response to oral glucose load. |
| 259 | 1563328 | To delineate the effects of aging on basal and glucose-stimulated secretion of islet amyloid polypeptide (IAPP), we compared the basal level of plasma IAPP and its response to an oral glucose load in elderly subjects with those of young subjects. |
| 260 | 1563328 | Effects of aging on plasma islet amyloid polypeptide basal level and response to oral glucose load. |
| 261 | 1563328 | To delineate the effects of aging on basal and glucose-stimulated secretion of islet amyloid polypeptide (IAPP), we compared the basal level of plasma IAPP and its response to an oral glucose load in elderly subjects with those of young subjects. |
| 262 | 1563587 | Islet amyloid polypeptide plasma concentrations in individuals at increased risk of developing type 2 (non-insulin-dependent) diabetes mellitus. |
| 263 | 1563587 | To study whether abnormal secretion of islet amyloid polypeptide is involved in the development of insulin resistance and impaired insulin secretion in Type 2 (non-insulin-dependent) diabetes mellitus, we measured islet amyloid polypeptide concentrations in 56 first-degree relatives of Type 2 diabetic subjects and in 10 healthy control subjects. |
| 264 | 1563587 | Fasting islet amyloid polypeptide concentrations were similar in control subjects, glucose-tolerant and glucose-intolerant relatives (8 +/- 1, 9 +/- 1 and 11 +/- 2 fmol/ml; p = NS). |
| 265 | 1563587 | The area under the islet amyloid polypeptide curve measured during an oral glucose load was larger in glucose-intolerant relatives (115 +/- 13 fmol/ml) compared to glucose tolerant relatives and control subjects (88 +/- 3 and 79 +/- 12 fmol/ml; p less than 0.05). |
| 266 | 1563587 | The insulin response during the oral glucose load was inversely correlated with the rate of glucose disposal measured during a euglycaemic hyperinsulinaemic clamp (r = -0.725; p less than 0.01), while no significant correlation was observed between the corresponding values for islet amyloid polypeptide and glucose disposal (r = -0.380; p = NS). |
| 267 | 1563587 | Hypersecretion of islet amyloid polypeptide is observed in glucose-intolerant first-degree relatives of patients with Type 2 diabetes. |
| 268 | 1563587 | Since these patients are characterized by insulin resistance and abnormal first-phase insulin secretion, the putative role of islet amyloid polypeptide in the development of these abnormalities remains to be established. |
| 269 | 1563587 | It is however, unlikely that islet amyloid polypeptide is involved in the development of insulin resistance as insulin-resistant relatives with normal glucose-tolerance showed normal islet amyloid polypeptide concentrations. |
| 270 | 1563587 | Islet amyloid polypeptide plasma concentrations in individuals at increased risk of developing type 2 (non-insulin-dependent) diabetes mellitus. |
| 271 | 1563587 | To study whether abnormal secretion of islet amyloid polypeptide is involved in the development of insulin resistance and impaired insulin secretion in Type 2 (non-insulin-dependent) diabetes mellitus, we measured islet amyloid polypeptide concentrations in 56 first-degree relatives of Type 2 diabetic subjects and in 10 healthy control subjects. |
| 272 | 1563587 | Fasting islet amyloid polypeptide concentrations were similar in control subjects, glucose-tolerant and glucose-intolerant relatives (8 +/- 1, 9 +/- 1 and 11 +/- 2 fmol/ml; p = NS). |
| 273 | 1563587 | The area under the islet amyloid polypeptide curve measured during an oral glucose load was larger in glucose-intolerant relatives (115 +/- 13 fmol/ml) compared to glucose tolerant relatives and control subjects (88 +/- 3 and 79 +/- 12 fmol/ml; p less than 0.05). |
| 274 | 1563587 | The insulin response during the oral glucose load was inversely correlated with the rate of glucose disposal measured during a euglycaemic hyperinsulinaemic clamp (r = -0.725; p less than 0.01), while no significant correlation was observed between the corresponding values for islet amyloid polypeptide and glucose disposal (r = -0.380; p = NS). |
| 275 | 1563587 | Hypersecretion of islet amyloid polypeptide is observed in glucose-intolerant first-degree relatives of patients with Type 2 diabetes. |
| 276 | 1563587 | Since these patients are characterized by insulin resistance and abnormal first-phase insulin secretion, the putative role of islet amyloid polypeptide in the development of these abnormalities remains to be established. |
| 277 | 1563587 | It is however, unlikely that islet amyloid polypeptide is involved in the development of insulin resistance as insulin-resistant relatives with normal glucose-tolerance showed normal islet amyloid polypeptide concentrations. |
| 278 | 1563587 | Islet amyloid polypeptide plasma concentrations in individuals at increased risk of developing type 2 (non-insulin-dependent) diabetes mellitus. |
| 279 | 1563587 | To study whether abnormal secretion of islet amyloid polypeptide is involved in the development of insulin resistance and impaired insulin secretion in Type 2 (non-insulin-dependent) diabetes mellitus, we measured islet amyloid polypeptide concentrations in 56 first-degree relatives of Type 2 diabetic subjects and in 10 healthy control subjects. |
| 280 | 1563587 | Fasting islet amyloid polypeptide concentrations were similar in control subjects, glucose-tolerant and glucose-intolerant relatives (8 +/- 1, 9 +/- 1 and 11 +/- 2 fmol/ml; p = NS). |
| 281 | 1563587 | The area under the islet amyloid polypeptide curve measured during an oral glucose load was larger in glucose-intolerant relatives (115 +/- 13 fmol/ml) compared to glucose tolerant relatives and control subjects (88 +/- 3 and 79 +/- 12 fmol/ml; p less than 0.05). |
| 282 | 1563587 | The insulin response during the oral glucose load was inversely correlated with the rate of glucose disposal measured during a euglycaemic hyperinsulinaemic clamp (r = -0.725; p less than 0.01), while no significant correlation was observed between the corresponding values for islet amyloid polypeptide and glucose disposal (r = -0.380; p = NS). |
| 283 | 1563587 | Hypersecretion of islet amyloid polypeptide is observed in glucose-intolerant first-degree relatives of patients with Type 2 diabetes. |
| 284 | 1563587 | Since these patients are characterized by insulin resistance and abnormal first-phase insulin secretion, the putative role of islet amyloid polypeptide in the development of these abnormalities remains to be established. |
| 285 | 1563587 | It is however, unlikely that islet amyloid polypeptide is involved in the development of insulin resistance as insulin-resistant relatives with normal glucose-tolerance showed normal islet amyloid polypeptide concentrations. |
| 286 | 1563587 | Islet amyloid polypeptide plasma concentrations in individuals at increased risk of developing type 2 (non-insulin-dependent) diabetes mellitus. |
| 287 | 1563587 | To study whether abnormal secretion of islet amyloid polypeptide is involved in the development of insulin resistance and impaired insulin secretion in Type 2 (non-insulin-dependent) diabetes mellitus, we measured islet amyloid polypeptide concentrations in 56 first-degree relatives of Type 2 diabetic subjects and in 10 healthy control subjects. |
| 288 | 1563587 | Fasting islet amyloid polypeptide concentrations were similar in control subjects, glucose-tolerant and glucose-intolerant relatives (8 +/- 1, 9 +/- 1 and 11 +/- 2 fmol/ml; p = NS). |
| 289 | 1563587 | The area under the islet amyloid polypeptide curve measured during an oral glucose load was larger in glucose-intolerant relatives (115 +/- 13 fmol/ml) compared to glucose tolerant relatives and control subjects (88 +/- 3 and 79 +/- 12 fmol/ml; p less than 0.05). |
| 290 | 1563587 | The insulin response during the oral glucose load was inversely correlated with the rate of glucose disposal measured during a euglycaemic hyperinsulinaemic clamp (r = -0.725; p less than 0.01), while no significant correlation was observed between the corresponding values for islet amyloid polypeptide and glucose disposal (r = -0.380; p = NS). |
| 291 | 1563587 | Hypersecretion of islet amyloid polypeptide is observed in glucose-intolerant first-degree relatives of patients with Type 2 diabetes. |
| 292 | 1563587 | Since these patients are characterized by insulin resistance and abnormal first-phase insulin secretion, the putative role of islet amyloid polypeptide in the development of these abnormalities remains to be established. |
| 293 | 1563587 | It is however, unlikely that islet amyloid polypeptide is involved in the development of insulin resistance as insulin-resistant relatives with normal glucose-tolerance showed normal islet amyloid polypeptide concentrations. |
| 294 | 1563587 | Islet amyloid polypeptide plasma concentrations in individuals at increased risk of developing type 2 (non-insulin-dependent) diabetes mellitus. |
| 295 | 1563587 | To study whether abnormal secretion of islet amyloid polypeptide is involved in the development of insulin resistance and impaired insulin secretion in Type 2 (non-insulin-dependent) diabetes mellitus, we measured islet amyloid polypeptide concentrations in 56 first-degree relatives of Type 2 diabetic subjects and in 10 healthy control subjects. |
| 296 | 1563587 | Fasting islet amyloid polypeptide concentrations were similar in control subjects, glucose-tolerant and glucose-intolerant relatives (8 +/- 1, 9 +/- 1 and 11 +/- 2 fmol/ml; p = NS). |
| 297 | 1563587 | The area under the islet amyloid polypeptide curve measured during an oral glucose load was larger in glucose-intolerant relatives (115 +/- 13 fmol/ml) compared to glucose tolerant relatives and control subjects (88 +/- 3 and 79 +/- 12 fmol/ml; p less than 0.05). |
| 298 | 1563587 | The insulin response during the oral glucose load was inversely correlated with the rate of glucose disposal measured during a euglycaemic hyperinsulinaemic clamp (r = -0.725; p less than 0.01), while no significant correlation was observed between the corresponding values for islet amyloid polypeptide and glucose disposal (r = -0.380; p = NS). |
| 299 | 1563587 | Hypersecretion of islet amyloid polypeptide is observed in glucose-intolerant first-degree relatives of patients with Type 2 diabetes. |
| 300 | 1563587 | Since these patients are characterized by insulin resistance and abnormal first-phase insulin secretion, the putative role of islet amyloid polypeptide in the development of these abnormalities remains to be established. |
| 301 | 1563587 | It is however, unlikely that islet amyloid polypeptide is involved in the development of insulin resistance as insulin-resistant relatives with normal glucose-tolerance showed normal islet amyloid polypeptide concentrations. |
| 302 | 1563587 | Islet amyloid polypeptide plasma concentrations in individuals at increased risk of developing type 2 (non-insulin-dependent) diabetes mellitus. |
| 303 | 1563587 | To study whether abnormal secretion of islet amyloid polypeptide is involved in the development of insulin resistance and impaired insulin secretion in Type 2 (non-insulin-dependent) diabetes mellitus, we measured islet amyloid polypeptide concentrations in 56 first-degree relatives of Type 2 diabetic subjects and in 10 healthy control subjects. |
| 304 | 1563587 | Fasting islet amyloid polypeptide concentrations were similar in control subjects, glucose-tolerant and glucose-intolerant relatives (8 +/- 1, 9 +/- 1 and 11 +/- 2 fmol/ml; p = NS). |
| 305 | 1563587 | The area under the islet amyloid polypeptide curve measured during an oral glucose load was larger in glucose-intolerant relatives (115 +/- 13 fmol/ml) compared to glucose tolerant relatives and control subjects (88 +/- 3 and 79 +/- 12 fmol/ml; p less than 0.05). |
| 306 | 1563587 | The insulin response during the oral glucose load was inversely correlated with the rate of glucose disposal measured during a euglycaemic hyperinsulinaemic clamp (r = -0.725; p less than 0.01), while no significant correlation was observed between the corresponding values for islet amyloid polypeptide and glucose disposal (r = -0.380; p = NS). |
| 307 | 1563587 | Hypersecretion of islet amyloid polypeptide is observed in glucose-intolerant first-degree relatives of patients with Type 2 diabetes. |
| 308 | 1563587 | Since these patients are characterized by insulin resistance and abnormal first-phase insulin secretion, the putative role of islet amyloid polypeptide in the development of these abnormalities remains to be established. |
| 309 | 1563587 | It is however, unlikely that islet amyloid polypeptide is involved in the development of insulin resistance as insulin-resistant relatives with normal glucose-tolerance showed normal islet amyloid polypeptide concentrations. |
| 310 | 1563587 | Islet amyloid polypeptide plasma concentrations in individuals at increased risk of developing type 2 (non-insulin-dependent) diabetes mellitus. |
| 311 | 1563587 | To study whether abnormal secretion of islet amyloid polypeptide is involved in the development of insulin resistance and impaired insulin secretion in Type 2 (non-insulin-dependent) diabetes mellitus, we measured islet amyloid polypeptide concentrations in 56 first-degree relatives of Type 2 diabetic subjects and in 10 healthy control subjects. |
| 312 | 1563587 | Fasting islet amyloid polypeptide concentrations were similar in control subjects, glucose-tolerant and glucose-intolerant relatives (8 +/- 1, 9 +/- 1 and 11 +/- 2 fmol/ml; p = NS). |
| 313 | 1563587 | The area under the islet amyloid polypeptide curve measured during an oral glucose load was larger in glucose-intolerant relatives (115 +/- 13 fmol/ml) compared to glucose tolerant relatives and control subjects (88 +/- 3 and 79 +/- 12 fmol/ml; p less than 0.05). |
| 314 | 1563587 | The insulin response during the oral glucose load was inversely correlated with the rate of glucose disposal measured during a euglycaemic hyperinsulinaemic clamp (r = -0.725; p less than 0.01), while no significant correlation was observed between the corresponding values for islet amyloid polypeptide and glucose disposal (r = -0.380; p = NS). |
| 315 | 1563587 | Hypersecretion of islet amyloid polypeptide is observed in glucose-intolerant first-degree relatives of patients with Type 2 diabetes. |
| 316 | 1563587 | Since these patients are characterized by insulin resistance and abnormal first-phase insulin secretion, the putative role of islet amyloid polypeptide in the development of these abnormalities remains to be established. |
| 317 | 1563587 | It is however, unlikely that islet amyloid polypeptide is involved in the development of insulin resistance as insulin-resistant relatives with normal glucose-tolerance showed normal islet amyloid polypeptide concentrations. |
| 318 | 1563587 | Islet amyloid polypeptide plasma concentrations in individuals at increased risk of developing type 2 (non-insulin-dependent) diabetes mellitus. |
| 319 | 1563587 | To study whether abnormal secretion of islet amyloid polypeptide is involved in the development of insulin resistance and impaired insulin secretion in Type 2 (non-insulin-dependent) diabetes mellitus, we measured islet amyloid polypeptide concentrations in 56 first-degree relatives of Type 2 diabetic subjects and in 10 healthy control subjects. |
| 320 | 1563587 | Fasting islet amyloid polypeptide concentrations were similar in control subjects, glucose-tolerant and glucose-intolerant relatives (8 +/- 1, 9 +/- 1 and 11 +/- 2 fmol/ml; p = NS). |
| 321 | 1563587 | The area under the islet amyloid polypeptide curve measured during an oral glucose load was larger in glucose-intolerant relatives (115 +/- 13 fmol/ml) compared to glucose tolerant relatives and control subjects (88 +/- 3 and 79 +/- 12 fmol/ml; p less than 0.05). |
| 322 | 1563587 | The insulin response during the oral glucose load was inversely correlated with the rate of glucose disposal measured during a euglycaemic hyperinsulinaemic clamp (r = -0.725; p less than 0.01), while no significant correlation was observed between the corresponding values for islet amyloid polypeptide and glucose disposal (r = -0.380; p = NS). |
| 323 | 1563587 | Hypersecretion of islet amyloid polypeptide is observed in glucose-intolerant first-degree relatives of patients with Type 2 diabetes. |
| 324 | 1563587 | Since these patients are characterized by insulin resistance and abnormal first-phase insulin secretion, the putative role of islet amyloid polypeptide in the development of these abnormalities remains to be established. |
| 325 | 1563587 | It is however, unlikely that islet amyloid polypeptide is involved in the development of insulin resistance as insulin-resistant relatives with normal glucose-tolerance showed normal islet amyloid polypeptide concentrations. |
| 326 | 1573849 | Islet amyloid polypeptide: mechanisms of amyloidogenesis in the pancreatic islets and potential roles in diabetes mellitus. |
| 327 | 1573849 | IAPP, a highly conserved and carboxy-terminally amidated 37 amino acid polypeptide with approximately 45% amino acid sequence identity to CGRP, is produced by islet beta cells and is cosecreted with insulin in response to glucose and other secretagogues. |
| 328 | 1609616 | The argyrophilic tumor cells with occasional mitoses and focal venous involvement predominantly showed immunoreactivity of cytokeratin, neuron-specific enolase, cystatin C, chromogranin A, calcitonin and neuropeptide Y (NPY). |
| 329 | 1609616 | Fewer cells were immunoreactive for calcitonin gene-related peptide (CGRP), the alpha-subunit of human chorionic gonadotropin, gastrin-releasing peptide, serotonin, methionine-enkephalin and gastrin. |
| 330 | 1609616 | Immunoreactive CGRP or NPY were co-localized in calcitonin-positive cells. |
| 331 | 1609616 | The amyloid substance was positively labeled only for CGRP. |
| 332 | 1609616 | Immunostaining for amylin, a polypeptide isolated from insular amyloid in type II diabetes mellitus or insulinoma showing a 50% homology with CGRP, was negative. |
| 333 | 1609616 | Immunoelectron microscopic studies disclosed peptide localization in neurosecretory-type granules and CGRP immunoreactivity in extracellular amyloid fibrils. |
| 334 | 1609616 | This is the first report describing CGRP as a component of amyloid of endocrine origin. |
| 335 | 1609616 | The argyrophilic tumor cells with occasional mitoses and focal venous involvement predominantly showed immunoreactivity of cytokeratin, neuron-specific enolase, cystatin C, chromogranin A, calcitonin and neuropeptide Y (NPY). |
| 336 | 1609616 | Fewer cells were immunoreactive for calcitonin gene-related peptide (CGRP), the alpha-subunit of human chorionic gonadotropin, gastrin-releasing peptide, serotonin, methionine-enkephalin and gastrin. |
| 337 | 1609616 | Immunoreactive CGRP or NPY were co-localized in calcitonin-positive cells. |
| 338 | 1609616 | The amyloid substance was positively labeled only for CGRP. |
| 339 | 1609616 | Immunostaining for amylin, a polypeptide isolated from insular amyloid in type II diabetes mellitus or insulinoma showing a 50% homology with CGRP, was negative. |
| 340 | 1609616 | Immunoelectron microscopic studies disclosed peptide localization in neurosecretory-type granules and CGRP immunoreactivity in extracellular amyloid fibrils. |
| 341 | 1609616 | This is the first report describing CGRP as a component of amyloid of endocrine origin. |
| 342 | 1609616 | The argyrophilic tumor cells with occasional mitoses and focal venous involvement predominantly showed immunoreactivity of cytokeratin, neuron-specific enolase, cystatin C, chromogranin A, calcitonin and neuropeptide Y (NPY). |
| 343 | 1609616 | Fewer cells were immunoreactive for calcitonin gene-related peptide (CGRP), the alpha-subunit of human chorionic gonadotropin, gastrin-releasing peptide, serotonin, methionine-enkephalin and gastrin. |
| 344 | 1609616 | Immunoreactive CGRP or NPY were co-localized in calcitonin-positive cells. |
| 345 | 1609616 | The amyloid substance was positively labeled only for CGRP. |
| 346 | 1609616 | Immunostaining for amylin, a polypeptide isolated from insular amyloid in type II diabetes mellitus or insulinoma showing a 50% homology with CGRP, was negative. |
| 347 | 1609616 | Immunoelectron microscopic studies disclosed peptide localization in neurosecretory-type granules and CGRP immunoreactivity in extracellular amyloid fibrils. |
| 348 | 1609616 | This is the first report describing CGRP as a component of amyloid of endocrine origin. |
| 349 | 1609616 | The argyrophilic tumor cells with occasional mitoses and focal venous involvement predominantly showed immunoreactivity of cytokeratin, neuron-specific enolase, cystatin C, chromogranin A, calcitonin and neuropeptide Y (NPY). |
| 350 | 1609616 | Fewer cells were immunoreactive for calcitonin gene-related peptide (CGRP), the alpha-subunit of human chorionic gonadotropin, gastrin-releasing peptide, serotonin, methionine-enkephalin and gastrin. |
| 351 | 1609616 | Immunoreactive CGRP or NPY were co-localized in calcitonin-positive cells. |
| 352 | 1609616 | The amyloid substance was positively labeled only for CGRP. |
| 353 | 1609616 | Immunostaining for amylin, a polypeptide isolated from insular amyloid in type II diabetes mellitus or insulinoma showing a 50% homology with CGRP, was negative. |
| 354 | 1609616 | Immunoelectron microscopic studies disclosed peptide localization in neurosecretory-type granules and CGRP immunoreactivity in extracellular amyloid fibrils. |
| 355 | 1609616 | This is the first report describing CGRP as a component of amyloid of endocrine origin. |
| 356 | 1628773 | Amylin, a peptide found in pancreatic amyloid deposits, may be involved in NIDDM. |
| 357 | 1637089 | The physiology of calcitonin gene-related peptide in the islet compared with that of islet amyloid polypeptide (amylin). |
| 358 | 1637089 | Another 37-amino acid peptide was recently isolated from islet amyloid deposits and found to have approximately 50% amino acid sequence homology with CGRP. |
| 359 | 1637089 | Islet amyloid polypeptide, or amylin, is co-localized with insulin to the beta-cell secretory granule and is synthesized and released in parallel with insulin in response to a range of physiological and pharmacological stimuli. |
| 360 | 1637089 | IAPP was subsequently shown, like CGRP, to inhibit the release of insulin pharmacologically. |
| 361 | 1637089 | The physiology of calcitonin gene-related peptide in the islet compared with that of islet amyloid polypeptide (amylin). |
| 362 | 1637089 | Another 37-amino acid peptide was recently isolated from islet amyloid deposits and found to have approximately 50% amino acid sequence homology with CGRP. |
| 363 | 1637089 | Islet amyloid polypeptide, or amylin, is co-localized with insulin to the beta-cell secretory granule and is synthesized and released in parallel with insulin in response to a range of physiological and pharmacological stimuli. |
| 364 | 1637089 | IAPP was subsequently shown, like CGRP, to inhibit the release of insulin pharmacologically. |
| 365 | 1637089 | The physiology of calcitonin gene-related peptide in the islet compared with that of islet amyloid polypeptide (amylin). |
| 366 | 1637089 | Another 37-amino acid peptide was recently isolated from islet amyloid deposits and found to have approximately 50% amino acid sequence homology with CGRP. |
| 367 | 1637089 | Islet amyloid polypeptide, or amylin, is co-localized with insulin to the beta-cell secretory granule and is synthesized and released in parallel with insulin in response to a range of physiological and pharmacological stimuli. |
| 368 | 1637089 | IAPP was subsequently shown, like CGRP, to inhibit the release of insulin pharmacologically. |
| 369 | 1641390 | Inhibitory effect of islet amyloid polypeptide of glucose-induced proinsulin biosynthesis in rat insulinoma cells. |
| 370 | 1641390 | Islet amyloid polypeptide (IAPP) has been recently identified as the principal constituent of amyloid deposits in pancreatic islets of patients with type 2 (non-insulin-dependent) diabetes mellitus and causes insulin resistance in some target cells. |
| 371 | 1641390 | Inhibitory effect of islet amyloid polypeptide of glucose-induced proinsulin biosynthesis in rat insulinoma cells. |
| 372 | 1641390 | Islet amyloid polypeptide (IAPP) has been recently identified as the principal constituent of amyloid deposits in pancreatic islets of patients with type 2 (non-insulin-dependent) diabetes mellitus and causes insulin resistance in some target cells. |
| 373 | 1676684 | Non-linkage of the islet amyloid polypeptide gene with type 2 (non-insulin-dependent) diabetes mellitus. |
| 374 | 1676684 | Type 2 (non-insulin-dependent) diabetes is associated with the deposition of islet amyloid. |
| 375 | 1676684 | The major formative peptide, islet amyloid polypeptide, has recently been characterised and an abnormality of the structure or expression of this gene is a possible candidate for the inherited component of Type 2 diabetes. |
| 376 | 1676684 | To study the relationship between the islet amyloid polypeptide gene and Type 2 diabetes, two distinct genetic approaches have been undertaken. |
| 377 | 1676684 | A mutation in or near the islet amyloid polypeptide gene is thus unlikely to be a common cause of Type 2 diabetes. |
| 378 | 1676684 | Non-linkage of the islet amyloid polypeptide gene with type 2 (non-insulin-dependent) diabetes mellitus. |
| 379 | 1676684 | Type 2 (non-insulin-dependent) diabetes is associated with the deposition of islet amyloid. |
| 380 | 1676684 | The major formative peptide, islet amyloid polypeptide, has recently been characterised and an abnormality of the structure or expression of this gene is a possible candidate for the inherited component of Type 2 diabetes. |
| 381 | 1676684 | To study the relationship between the islet amyloid polypeptide gene and Type 2 diabetes, two distinct genetic approaches have been undertaken. |
| 382 | 1676684 | A mutation in or near the islet amyloid polypeptide gene is thus unlikely to be a common cause of Type 2 diabetes. |
| 383 | 1676684 | Non-linkage of the islet amyloid polypeptide gene with type 2 (non-insulin-dependent) diabetes mellitus. |
| 384 | 1676684 | Type 2 (non-insulin-dependent) diabetes is associated with the deposition of islet amyloid. |
| 385 | 1676684 | The major formative peptide, islet amyloid polypeptide, has recently been characterised and an abnormality of the structure or expression of this gene is a possible candidate for the inherited component of Type 2 diabetes. |
| 386 | 1676684 | To study the relationship between the islet amyloid polypeptide gene and Type 2 diabetes, two distinct genetic approaches have been undertaken. |
| 387 | 1676684 | A mutation in or near the islet amyloid polypeptide gene is thus unlikely to be a common cause of Type 2 diabetes. |
| 388 | 1676684 | Non-linkage of the islet amyloid polypeptide gene with type 2 (non-insulin-dependent) diabetes mellitus. |
| 389 | 1676684 | Type 2 (non-insulin-dependent) diabetes is associated with the deposition of islet amyloid. |
| 390 | 1676684 | The major formative peptide, islet amyloid polypeptide, has recently been characterised and an abnormality of the structure or expression of this gene is a possible candidate for the inherited component of Type 2 diabetes. |
| 391 | 1676684 | To study the relationship between the islet amyloid polypeptide gene and Type 2 diabetes, two distinct genetic approaches have been undertaken. |
| 392 | 1676684 | A mutation in or near the islet amyloid polypeptide gene is thus unlikely to be a common cause of Type 2 diabetes. |
| 393 | 1676684 | Non-linkage of the islet amyloid polypeptide gene with type 2 (non-insulin-dependent) diabetes mellitus. |
| 394 | 1676684 | Type 2 (non-insulin-dependent) diabetes is associated with the deposition of islet amyloid. |
| 395 | 1676684 | The major formative peptide, islet amyloid polypeptide, has recently been characterised and an abnormality of the structure or expression of this gene is a possible candidate for the inherited component of Type 2 diabetes. |
| 396 | 1676684 | To study the relationship between the islet amyloid polypeptide gene and Type 2 diabetes, two distinct genetic approaches have been undertaken. |
| 397 | 1676684 | A mutation in or near the islet amyloid polypeptide gene is thus unlikely to be a common cause of Type 2 diabetes. |
| 398 | 1718805 | Sequences of islet amyloid polypeptide precursors of an Old World monkey, the pig-tailed macaque (Macaca nemestrina), and the dog (Canis familiaris). |
| 399 | 1718805 | The 37-amino acid islet amyloid polypeptide represents the major protein component present in islet amyloid deposits. |
| 400 | 1718805 | Although the presence of islet amyloid is a characteristic pathological feature of the islets of humans, monkeys and cats with Type 2 (non-insulin-dependent) diabetes mellitus, it is not found in the islets of diabetic rats, mice or dogs. |
| 401 | 1718805 | To further explore the molecular basis for these species differences in amyloid deposition we have used a polymerase chain reaction based method to clone cDNAs encoding the monkey (Macaca nemestrina) and dog (Canis familiaris) islet amyloid polypeptide precursors. |
| 402 | 1718805 | The predicted amino acid sequence of the monkey precursor is 96% identical to that of the human protein; differences include one replacement in the signal peptide and three in the islet amyloid polypeptide domain. |
| 403 | 1718805 | The sequence of the dog precursor is most closely related to that of the cat protein (85% identity); the sequences of dog and cat islet amyloid polypeptide differ only at two positions and are identical in the region of amino acids 20-29, the region thought to be primarily responsible for amyloidogenesis. |
| 404 | 1718805 | Thus, amino acid residues in addition to those at positions 20-29 may facilitate the aggregation of islet amyloid polypeptide. |
| 405 | 1718805 | The presence of amyloid deposits in some dog pancreatic endocrine tumours suggests that the dog protein can be amyloidogenic, perhaps due to elevated expression of islet amyloid polypeptide by the tumours relative to normal islets. |
| 406 | 1718805 | Sequences of islet amyloid polypeptide precursors of an Old World monkey, the pig-tailed macaque (Macaca nemestrina), and the dog (Canis familiaris). |
| 407 | 1718805 | The 37-amino acid islet amyloid polypeptide represents the major protein component present in islet amyloid deposits. |
| 408 | 1718805 | Although the presence of islet amyloid is a characteristic pathological feature of the islets of humans, monkeys and cats with Type 2 (non-insulin-dependent) diabetes mellitus, it is not found in the islets of diabetic rats, mice or dogs. |
| 409 | 1718805 | To further explore the molecular basis for these species differences in amyloid deposition we have used a polymerase chain reaction based method to clone cDNAs encoding the monkey (Macaca nemestrina) and dog (Canis familiaris) islet amyloid polypeptide precursors. |
| 410 | 1718805 | The predicted amino acid sequence of the monkey precursor is 96% identical to that of the human protein; differences include one replacement in the signal peptide and three in the islet amyloid polypeptide domain. |
| 411 | 1718805 | The sequence of the dog precursor is most closely related to that of the cat protein (85% identity); the sequences of dog and cat islet amyloid polypeptide differ only at two positions and are identical in the region of amino acids 20-29, the region thought to be primarily responsible for amyloidogenesis. |
| 412 | 1718805 | Thus, amino acid residues in addition to those at positions 20-29 may facilitate the aggregation of islet amyloid polypeptide. |
| 413 | 1718805 | The presence of amyloid deposits in some dog pancreatic endocrine tumours suggests that the dog protein can be amyloidogenic, perhaps due to elevated expression of islet amyloid polypeptide by the tumours relative to normal islets. |
| 414 | 1718805 | Sequences of islet amyloid polypeptide precursors of an Old World monkey, the pig-tailed macaque (Macaca nemestrina), and the dog (Canis familiaris). |
| 415 | 1718805 | The 37-amino acid islet amyloid polypeptide represents the major protein component present in islet amyloid deposits. |
| 416 | 1718805 | Although the presence of islet amyloid is a characteristic pathological feature of the islets of humans, monkeys and cats with Type 2 (non-insulin-dependent) diabetes mellitus, it is not found in the islets of diabetic rats, mice or dogs. |
| 417 | 1718805 | To further explore the molecular basis for these species differences in amyloid deposition we have used a polymerase chain reaction based method to clone cDNAs encoding the monkey (Macaca nemestrina) and dog (Canis familiaris) islet amyloid polypeptide precursors. |
| 418 | 1718805 | The predicted amino acid sequence of the monkey precursor is 96% identical to that of the human protein; differences include one replacement in the signal peptide and three in the islet amyloid polypeptide domain. |
| 419 | 1718805 | The sequence of the dog precursor is most closely related to that of the cat protein (85% identity); the sequences of dog and cat islet amyloid polypeptide differ only at two positions and are identical in the region of amino acids 20-29, the region thought to be primarily responsible for amyloidogenesis. |
| 420 | 1718805 | Thus, amino acid residues in addition to those at positions 20-29 may facilitate the aggregation of islet amyloid polypeptide. |
| 421 | 1718805 | The presence of amyloid deposits in some dog pancreatic endocrine tumours suggests that the dog protein can be amyloidogenic, perhaps due to elevated expression of islet amyloid polypeptide by the tumours relative to normal islets. |
| 422 | 1718805 | Sequences of islet amyloid polypeptide precursors of an Old World monkey, the pig-tailed macaque (Macaca nemestrina), and the dog (Canis familiaris). |
| 423 | 1718805 | The 37-amino acid islet amyloid polypeptide represents the major protein component present in islet amyloid deposits. |
| 424 | 1718805 | Although the presence of islet amyloid is a characteristic pathological feature of the islets of humans, monkeys and cats with Type 2 (non-insulin-dependent) diabetes mellitus, it is not found in the islets of diabetic rats, mice or dogs. |
| 425 | 1718805 | To further explore the molecular basis for these species differences in amyloid deposition we have used a polymerase chain reaction based method to clone cDNAs encoding the monkey (Macaca nemestrina) and dog (Canis familiaris) islet amyloid polypeptide precursors. |
| 426 | 1718805 | The predicted amino acid sequence of the monkey precursor is 96% identical to that of the human protein; differences include one replacement in the signal peptide and three in the islet amyloid polypeptide domain. |
| 427 | 1718805 | The sequence of the dog precursor is most closely related to that of the cat protein (85% identity); the sequences of dog and cat islet amyloid polypeptide differ only at two positions and are identical in the region of amino acids 20-29, the region thought to be primarily responsible for amyloidogenesis. |
| 428 | 1718805 | Thus, amino acid residues in addition to those at positions 20-29 may facilitate the aggregation of islet amyloid polypeptide. |
| 429 | 1718805 | The presence of amyloid deposits in some dog pancreatic endocrine tumours suggests that the dog protein can be amyloidogenic, perhaps due to elevated expression of islet amyloid polypeptide by the tumours relative to normal islets. |
| 430 | 1718805 | Sequences of islet amyloid polypeptide precursors of an Old World monkey, the pig-tailed macaque (Macaca nemestrina), and the dog (Canis familiaris). |
| 431 | 1718805 | The 37-amino acid islet amyloid polypeptide represents the major protein component present in islet amyloid deposits. |
| 432 | 1718805 | Although the presence of islet amyloid is a characteristic pathological feature of the islets of humans, monkeys and cats with Type 2 (non-insulin-dependent) diabetes mellitus, it is not found in the islets of diabetic rats, mice or dogs. |
| 433 | 1718805 | To further explore the molecular basis for these species differences in amyloid deposition we have used a polymerase chain reaction based method to clone cDNAs encoding the monkey (Macaca nemestrina) and dog (Canis familiaris) islet amyloid polypeptide precursors. |
| 434 | 1718805 | The predicted amino acid sequence of the monkey precursor is 96% identical to that of the human protein; differences include one replacement in the signal peptide and three in the islet amyloid polypeptide domain. |
| 435 | 1718805 | The sequence of the dog precursor is most closely related to that of the cat protein (85% identity); the sequences of dog and cat islet amyloid polypeptide differ only at two positions and are identical in the region of amino acids 20-29, the region thought to be primarily responsible for amyloidogenesis. |
| 436 | 1718805 | Thus, amino acid residues in addition to those at positions 20-29 may facilitate the aggregation of islet amyloid polypeptide. |
| 437 | 1718805 | The presence of amyloid deposits in some dog pancreatic endocrine tumours suggests that the dog protein can be amyloidogenic, perhaps due to elevated expression of islet amyloid polypeptide by the tumours relative to normal islets. |
| 438 | 1718805 | Sequences of islet amyloid polypeptide precursors of an Old World monkey, the pig-tailed macaque (Macaca nemestrina), and the dog (Canis familiaris). |
| 439 | 1718805 | The 37-amino acid islet amyloid polypeptide represents the major protein component present in islet amyloid deposits. |
| 440 | 1718805 | Although the presence of islet amyloid is a characteristic pathological feature of the islets of humans, monkeys and cats with Type 2 (non-insulin-dependent) diabetes mellitus, it is not found in the islets of diabetic rats, mice or dogs. |
| 441 | 1718805 | To further explore the molecular basis for these species differences in amyloid deposition we have used a polymerase chain reaction based method to clone cDNAs encoding the monkey (Macaca nemestrina) and dog (Canis familiaris) islet amyloid polypeptide precursors. |
| 442 | 1718805 | The predicted amino acid sequence of the monkey precursor is 96% identical to that of the human protein; differences include one replacement in the signal peptide and three in the islet amyloid polypeptide domain. |
| 443 | 1718805 | The sequence of the dog precursor is most closely related to that of the cat protein (85% identity); the sequences of dog and cat islet amyloid polypeptide differ only at two positions and are identical in the region of amino acids 20-29, the region thought to be primarily responsible for amyloidogenesis. |
| 444 | 1718805 | Thus, amino acid residues in addition to those at positions 20-29 may facilitate the aggregation of islet amyloid polypeptide. |
| 445 | 1718805 | The presence of amyloid deposits in some dog pancreatic endocrine tumours suggests that the dog protein can be amyloidogenic, perhaps due to elevated expression of islet amyloid polypeptide by the tumours relative to normal islets. |
| 446 | 1718805 | Sequences of islet amyloid polypeptide precursors of an Old World monkey, the pig-tailed macaque (Macaca nemestrina), and the dog (Canis familiaris). |
| 447 | 1718805 | The 37-amino acid islet amyloid polypeptide represents the major protein component present in islet amyloid deposits. |
| 448 | 1718805 | Although the presence of islet amyloid is a characteristic pathological feature of the islets of humans, monkeys and cats with Type 2 (non-insulin-dependent) diabetes mellitus, it is not found in the islets of diabetic rats, mice or dogs. |
| 449 | 1718805 | To further explore the molecular basis for these species differences in amyloid deposition we have used a polymerase chain reaction based method to clone cDNAs encoding the monkey (Macaca nemestrina) and dog (Canis familiaris) islet amyloid polypeptide precursors. |
| 450 | 1718805 | The predicted amino acid sequence of the monkey precursor is 96% identical to that of the human protein; differences include one replacement in the signal peptide and three in the islet amyloid polypeptide domain. |
| 451 | 1718805 | The sequence of the dog precursor is most closely related to that of the cat protein (85% identity); the sequences of dog and cat islet amyloid polypeptide differ only at two positions and are identical in the region of amino acids 20-29, the region thought to be primarily responsible for amyloidogenesis. |
| 452 | 1718805 | Thus, amino acid residues in addition to those at positions 20-29 may facilitate the aggregation of islet amyloid polypeptide. |
| 453 | 1718805 | The presence of amyloid deposits in some dog pancreatic endocrine tumours suggests that the dog protein can be amyloidogenic, perhaps due to elevated expression of islet amyloid polypeptide by the tumours relative to normal islets. |
| 454 | 1718805 | Sequences of islet amyloid polypeptide precursors of an Old World monkey, the pig-tailed macaque (Macaca nemestrina), and the dog (Canis familiaris). |
| 455 | 1718805 | The 37-amino acid islet amyloid polypeptide represents the major protein component present in islet amyloid deposits. |
| 456 | 1718805 | Although the presence of islet amyloid is a characteristic pathological feature of the islets of humans, monkeys and cats with Type 2 (non-insulin-dependent) diabetes mellitus, it is not found in the islets of diabetic rats, mice or dogs. |
| 457 | 1718805 | To further explore the molecular basis for these species differences in amyloid deposition we have used a polymerase chain reaction based method to clone cDNAs encoding the monkey (Macaca nemestrina) and dog (Canis familiaris) islet amyloid polypeptide precursors. |
| 458 | 1718805 | The predicted amino acid sequence of the monkey precursor is 96% identical to that of the human protein; differences include one replacement in the signal peptide and three in the islet amyloid polypeptide domain. |
| 459 | 1718805 | The sequence of the dog precursor is most closely related to that of the cat protein (85% identity); the sequences of dog and cat islet amyloid polypeptide differ only at two positions and are identical in the region of amino acids 20-29, the region thought to be primarily responsible for amyloidogenesis. |
| 460 | 1718805 | Thus, amino acid residues in addition to those at positions 20-29 may facilitate the aggregation of islet amyloid polypeptide. |
| 461 | 1718805 | The presence of amyloid deposits in some dog pancreatic endocrine tumours suggests that the dog protein can be amyloidogenic, perhaps due to elevated expression of islet amyloid polypeptide by the tumours relative to normal islets. |
| 462 | 1734887 | Presence of islet amyloid polypeptide in rat islet B and D cells determines parallelism and dissociation between rat pancreatic islet amyloid polypeptide and insulin content. |
| 463 | 1734887 | The islet amyloid polypeptide (IAPP) immunoreactivity of the adult rat pancreas is located in insulin-containing B cells as well as in somatostatin-containing D cells. |
| 464 | 1734887 | Presence of islet amyloid polypeptide in rat islet B and D cells determines parallelism and dissociation between rat pancreatic islet amyloid polypeptide and insulin content. |
| 465 | 1734887 | The islet amyloid polypeptide (IAPP) immunoreactivity of the adult rat pancreas is located in insulin-containing B cells as well as in somatostatin-containing D cells. |
| 466 | 1756902 | Amylin, a 37-amino acid polypeptide, has been identified as the major protein component of pancreatic amyloid deposits in patients with non-insulin-dependent (type II) diabetes mellitus. |
| 467 | 1756902 | Amylin is stored and released together with insulin and has been proposed to play a major role in the pathogenesis of type II diabetes. |
| 468 | 1756910 | Islet amyloid polypeptide and insulin secretion from isolated perfused pancreas of fed, fasted, glucose-treated, and dexamethasone-treated rats. |
| 469 | 1756910 | Rats from four experimental treatment groups, including fed controls, 24- to 30-h fasted, dexamethasone-treated, and intraperitoneal glucose-treated, were used to assess the effects of these treatments on the immunohistochemically detectable islet amyloid polypeptide (IAPP) content in the pancreatic islets. |
| 470 | 1756910 | Islet amyloid polypeptide and insulin secretion from isolated perfused pancreas of fed, fasted, glucose-treated, and dexamethasone-treated rats. |
| 471 | 1756910 | Rats from four experimental treatment groups, including fed controls, 24- to 30-h fasted, dexamethasone-treated, and intraperitoneal glucose-treated, were used to assess the effects of these treatments on the immunohistochemically detectable islet amyloid polypeptide (IAPP) content in the pancreatic islets. |
| 472 | 1833120 | Autoantibodies to islet amyloid polypeptide in diabetes. |
| 473 | 1833120 | Islet amyloid polypeptide (IAPP) is the constituent peptide of amyloid in pancreatic islets of Type 2 diabetic patients and in insulinomas. |
| 474 | 1833120 | Autoantibodies to islet amyloid polypeptide in diabetes. |
| 475 | 1833120 | Islet amyloid polypeptide (IAPP) is the constituent peptide of amyloid in pancreatic islets of Type 2 diabetic patients and in insulinomas. |
| 476 | 1854502 | Islet amyloid polypeptide (IAPP). |
| 477 | 1854502 | The islet amyloid polypeptide (IAPP) was originally identified by chemical analysis of the amyloid component in a human pancreatic islet cell tumor. |
| 478 | 1854502 | Islet amyloid polypeptide (IAPP). |
| 479 | 1854502 | The islet amyloid polypeptide (IAPP) was originally identified by chemical analysis of the amyloid component in a human pancreatic islet cell tumor. |
| 480 | 1860552 | Amylin is a 37-amino acid peptide isolated from the islet amyloid of patients with non-insulin-dependent diabetes mellitus. |
| 481 | 1860559 | Antagonistic effect of human alpha-calcitonin gene-related peptide (8-37) on regional hemodynamic actions of rat islet amyloid polypeptide in conscious Long-Evans rats. |
| 482 | 1860559 | Rat synthetic amidated islet amyloid polypeptide (IAPP) was infused into conscious Long-Evans rats chronically instrumented for the measurement of regional hemodynamics. |
| 483 | 1860559 | Antagonistic effect of human alpha-calcitonin gene-related peptide (8-37) on regional hemodynamic actions of rat islet amyloid polypeptide in conscious Long-Evans rats. |
| 484 | 1860559 | Rat synthetic amidated islet amyloid polypeptide (IAPP) was infused into conscious Long-Evans rats chronically instrumented for the measurement of regional hemodynamics. |
| 485 | 1860564 | Lack of effect of islet amyloid polypeptide in causing insulin resistance in conscious dogs during euglycemic clamp studies. |
| 486 | 1860564 | In this study, we administered constant intravenous infusions of human islet amyloid polypeptide (hIAPP) to conscious dogs during euglycemic glucose-clamp studies. |
| 487 | 1860564 | Lack of effect of islet amyloid polypeptide in causing insulin resistance in conscious dogs during euglycemic clamp studies. |
| 488 | 1860564 | In this study, we administered constant intravenous infusions of human islet amyloid polypeptide (hIAPP) to conscious dogs during euglycemic glucose-clamp studies. |
| 489 | 1876601 | Inhibitory action of islet amyloid polypeptide and calcitonin gene-related peptide on release of insulin from the isolated perfused rat pancreas. |
| 490 | 1876601 | The purpose of this study was to examine the effects of IAPP and CGRP on glucose- and carbachol-stimulated release of insulin and pancreatic polypeptide (PP) from the isolated perfused rat pancreas. |
| 491 | 1876601 | At the same concentration, however, IAPP significantly (p less than 0.05) inhibited carbachol-stimulated (10(-7) M) release of insulin by 30%, and CGRP significantly inhibited carbachol-stimulated release of insulin by 33% when compared with the control group. |
| 492 | 1876601 | IAPP and CGRP, at 10(-8) M, did not inhibit carbachol-stimulated release of insulin and PP. |
| 493 | 1880936 | However, the responsiveness of VLDL to LPL might be under the control of triglyceride (TG)/surface component ratios but not of the apoprotein ratios in ordinary circumstances judging from the results of the releases of fatty acids from VLDL by LPL in vitro. |
| 494 | 1880936 | Since high density lipoproteins (HDL) from patients in acute phases contain a large amount of serum amyloid A protein (SAA), the percentages of apo A proteins markedly decreased. |
| 495 | 1884903 | Localisation of islet amyloid polypeptide and its carboxy terminal flanking peptide in islets of diabetic man and monkey. |
| 496 | 1884903 | Islet amyloid polypeptide is a normal constituent of islet Beta cells and is derived from a larger precursor by removal of flanking peptides at the carboxy (C) and amino (N) terminals. |
| 497 | 1884903 | The role of these flanking peptides in the formation of amyloid in Type 2 (non-insulin-dependent) diabetes mellitus and in insulinomas is unknown. |
| 498 | 1884903 | The C-terminal flanking peptide of islet amyloid polypeptide was localised by immunocytochemistry in human and monkey pancreatic islets from Type 2 diabetic and non-diabetic individuals by use of specific polyclonal antisera. |
| 499 | 1884903 | Immunoreactivity for the C-terminal peptide was found in insulin-containing cells in both diabetic and non-diabetic tissue: no antibody binding was detected in islet amyloid of Type 2 diabetic man or of monkeys although a positive reaction occurred with antisera for islet amyloid polypeptide. |
| 500 | 1884903 | The C-terminal peptide was localised by immunogold electron microscopy in the insulin granules in both diabetic and non-diabetic individuals but, unlike islet amyloid polypeptide, was not detected in lysosomes. |
| 501 | 1884903 | The absence of immunoreactivity for the C-terminal peptide in amyloid suggests that incomplete cleavage of this flanking peptide from islet amyloid polypeptide is not a factor in the formation of islet amyloid. |
| 502 | 1884903 | Localisation of islet amyloid polypeptide and its carboxy terminal flanking peptide in islets of diabetic man and monkey. |
| 503 | 1884903 | Islet amyloid polypeptide is a normal constituent of islet Beta cells and is derived from a larger precursor by removal of flanking peptides at the carboxy (C) and amino (N) terminals. |
| 504 | 1884903 | The role of these flanking peptides in the formation of amyloid in Type 2 (non-insulin-dependent) diabetes mellitus and in insulinomas is unknown. |
| 505 | 1884903 | The C-terminal flanking peptide of islet amyloid polypeptide was localised by immunocytochemistry in human and monkey pancreatic islets from Type 2 diabetic and non-diabetic individuals by use of specific polyclonal antisera. |
| 506 | 1884903 | Immunoreactivity for the C-terminal peptide was found in insulin-containing cells in both diabetic and non-diabetic tissue: no antibody binding was detected in islet amyloid of Type 2 diabetic man or of monkeys although a positive reaction occurred with antisera for islet amyloid polypeptide. |
| 507 | 1884903 | The C-terminal peptide was localised by immunogold electron microscopy in the insulin granules in both diabetic and non-diabetic individuals but, unlike islet amyloid polypeptide, was not detected in lysosomes. |
| 508 | 1884903 | The absence of immunoreactivity for the C-terminal peptide in amyloid suggests that incomplete cleavage of this flanking peptide from islet amyloid polypeptide is not a factor in the formation of islet amyloid. |
| 509 | 1884903 | Localisation of islet amyloid polypeptide and its carboxy terminal flanking peptide in islets of diabetic man and monkey. |
| 510 | 1884903 | Islet amyloid polypeptide is a normal constituent of islet Beta cells and is derived from a larger precursor by removal of flanking peptides at the carboxy (C) and amino (N) terminals. |
| 511 | 1884903 | The role of these flanking peptides in the formation of amyloid in Type 2 (non-insulin-dependent) diabetes mellitus and in insulinomas is unknown. |
| 512 | 1884903 | The C-terminal flanking peptide of islet amyloid polypeptide was localised by immunocytochemistry in human and monkey pancreatic islets from Type 2 diabetic and non-diabetic individuals by use of specific polyclonal antisera. |
| 513 | 1884903 | Immunoreactivity for the C-terminal peptide was found in insulin-containing cells in both diabetic and non-diabetic tissue: no antibody binding was detected in islet amyloid of Type 2 diabetic man or of monkeys although a positive reaction occurred with antisera for islet amyloid polypeptide. |
| 514 | 1884903 | The C-terminal peptide was localised by immunogold electron microscopy in the insulin granules in both diabetic and non-diabetic individuals but, unlike islet amyloid polypeptide, was not detected in lysosomes. |
| 515 | 1884903 | The absence of immunoreactivity for the C-terminal peptide in amyloid suggests that incomplete cleavage of this flanking peptide from islet amyloid polypeptide is not a factor in the formation of islet amyloid. |
| 516 | 1884903 | Localisation of islet amyloid polypeptide and its carboxy terminal flanking peptide in islets of diabetic man and monkey. |
| 517 | 1884903 | Islet amyloid polypeptide is a normal constituent of islet Beta cells and is derived from a larger precursor by removal of flanking peptides at the carboxy (C) and amino (N) terminals. |
| 518 | 1884903 | The role of these flanking peptides in the formation of amyloid in Type 2 (non-insulin-dependent) diabetes mellitus and in insulinomas is unknown. |
| 519 | 1884903 | The C-terminal flanking peptide of islet amyloid polypeptide was localised by immunocytochemistry in human and monkey pancreatic islets from Type 2 diabetic and non-diabetic individuals by use of specific polyclonal antisera. |
| 520 | 1884903 | Immunoreactivity for the C-terminal peptide was found in insulin-containing cells in both diabetic and non-diabetic tissue: no antibody binding was detected in islet amyloid of Type 2 diabetic man or of monkeys although a positive reaction occurred with antisera for islet amyloid polypeptide. |
| 521 | 1884903 | The C-terminal peptide was localised by immunogold electron microscopy in the insulin granules in both diabetic and non-diabetic individuals but, unlike islet amyloid polypeptide, was not detected in lysosomes. |
| 522 | 1884903 | The absence of immunoreactivity for the C-terminal peptide in amyloid suggests that incomplete cleavage of this flanking peptide from islet amyloid polypeptide is not a factor in the formation of islet amyloid. |
| 523 | 1884903 | Localisation of islet amyloid polypeptide and its carboxy terminal flanking peptide in islets of diabetic man and monkey. |
| 524 | 1884903 | Islet amyloid polypeptide is a normal constituent of islet Beta cells and is derived from a larger precursor by removal of flanking peptides at the carboxy (C) and amino (N) terminals. |
| 525 | 1884903 | The role of these flanking peptides in the formation of amyloid in Type 2 (non-insulin-dependent) diabetes mellitus and in insulinomas is unknown. |
| 526 | 1884903 | The C-terminal flanking peptide of islet amyloid polypeptide was localised by immunocytochemistry in human and monkey pancreatic islets from Type 2 diabetic and non-diabetic individuals by use of specific polyclonal antisera. |
| 527 | 1884903 | Immunoreactivity for the C-terminal peptide was found in insulin-containing cells in both diabetic and non-diabetic tissue: no antibody binding was detected in islet amyloid of Type 2 diabetic man or of monkeys although a positive reaction occurred with antisera for islet amyloid polypeptide. |
| 528 | 1884903 | The C-terminal peptide was localised by immunogold electron microscopy in the insulin granules in both diabetic and non-diabetic individuals but, unlike islet amyloid polypeptide, was not detected in lysosomes. |
| 529 | 1884903 | The absence of immunoreactivity for the C-terminal peptide in amyloid suggests that incomplete cleavage of this flanking peptide from islet amyloid polypeptide is not a factor in the formation of islet amyloid. |
| 530 | 1884903 | Localisation of islet amyloid polypeptide and its carboxy terminal flanking peptide in islets of diabetic man and monkey. |
| 531 | 1884903 | Islet amyloid polypeptide is a normal constituent of islet Beta cells and is derived from a larger precursor by removal of flanking peptides at the carboxy (C) and amino (N) terminals. |
| 532 | 1884903 | The role of these flanking peptides in the formation of amyloid in Type 2 (non-insulin-dependent) diabetes mellitus and in insulinomas is unknown. |
| 533 | 1884903 | The C-terminal flanking peptide of islet amyloid polypeptide was localised by immunocytochemistry in human and monkey pancreatic islets from Type 2 diabetic and non-diabetic individuals by use of specific polyclonal antisera. |
| 534 | 1884903 | Immunoreactivity for the C-terminal peptide was found in insulin-containing cells in both diabetic and non-diabetic tissue: no antibody binding was detected in islet amyloid of Type 2 diabetic man or of monkeys although a positive reaction occurred with antisera for islet amyloid polypeptide. |
| 535 | 1884903 | The C-terminal peptide was localised by immunogold electron microscopy in the insulin granules in both diabetic and non-diabetic individuals but, unlike islet amyloid polypeptide, was not detected in lysosomes. |
| 536 | 1884903 | The absence of immunoreactivity for the C-terminal peptide in amyloid suggests that incomplete cleavage of this flanking peptide from islet amyloid polypeptide is not a factor in the formation of islet amyloid. |
| 537 | 1884903 | Localisation of islet amyloid polypeptide and its carboxy terminal flanking peptide in islets of diabetic man and monkey. |
| 538 | 1884903 | Islet amyloid polypeptide is a normal constituent of islet Beta cells and is derived from a larger precursor by removal of flanking peptides at the carboxy (C) and amino (N) terminals. |
| 539 | 1884903 | The role of these flanking peptides in the formation of amyloid in Type 2 (non-insulin-dependent) diabetes mellitus and in insulinomas is unknown. |
| 540 | 1884903 | The C-terminal flanking peptide of islet amyloid polypeptide was localised by immunocytochemistry in human and monkey pancreatic islets from Type 2 diabetic and non-diabetic individuals by use of specific polyclonal antisera. |
| 541 | 1884903 | Immunoreactivity for the C-terminal peptide was found in insulin-containing cells in both diabetic and non-diabetic tissue: no antibody binding was detected in islet amyloid of Type 2 diabetic man or of monkeys although a positive reaction occurred with antisera for islet amyloid polypeptide. |
| 542 | 1884903 | The C-terminal peptide was localised by immunogold electron microscopy in the insulin granules in both diabetic and non-diabetic individuals but, unlike islet amyloid polypeptide, was not detected in lysosomes. |
| 543 | 1884903 | The absence of immunoreactivity for the C-terminal peptide in amyloid suggests that incomplete cleavage of this flanking peptide from islet amyloid polypeptide is not a factor in the formation of islet amyloid. |
| 544 | 1891461 | Amylin is the major component of the amyloid found in the pancreases of noninsulin-dependent diabetics (type 2 diabetes). |
| 545 | 1924295 | Alz-50, a monoclonal antibody against abnormally phosphorylated tau proteins, stained neurons along the cortical needle track at 2 but not 7 days after injection of either amyloid or lipofuscin. |
| 546 | 1924295 | At 1 month, however, ubiquitin, Alz-50 antigen, and silver-positive structures were observed only in response to amyloid. |
| 547 | 1924295 | Alz-50, a monoclonal antibody against abnormally phosphorylated tau proteins, stained neurons along the cortical needle track at 2 but not 7 days after injection of either amyloid or lipofuscin. |
| 548 | 1924295 | At 1 month, however, ubiquitin, Alz-50 antigen, and silver-positive structures were observed only in response to amyloid. |
| 549 | 1950379 | Amylin, a peptide, which was isolated from the islet amyloid of type II diabetics, might play a potential role in the pathogenesis of type II diabetes mellitus. |
| 550 | 1970540 | Islet amyloid polypeptide response to glucose, insulin, and somatostatin analogue administration. |
| 551 | 1970540 | We determined islet amyloid polypeptide (IAPP) response in plasma to oral and intravenous glucose administration and intravenous insulin injection in nondiabetic subjects. |
| 552 | 1970540 | Islet amyloid polypeptide response to glucose, insulin, and somatostatin analogue administration. |
| 553 | 1970540 | We determined islet amyloid polypeptide (IAPP) response in plasma to oral and intravenous glucose administration and intravenous insulin injection in nondiabetic subjects. |
| 554 | 1990240 | Effects of ciglitazone on endogenous plasma islet amyloid polypeptide and insulin sensitivity in obese-diabetic viable yellow mice. |
| 555 | 1990240 | The role of islet amyloid polypeptide, also known as amylin, in insulin resistance and in the etiology of diabetes has been a subject of debate. |
| 556 | 1990240 | Effects of ciglitazone on endogenous plasma islet amyloid polypeptide and insulin sensitivity in obese-diabetic viable yellow mice. |
| 557 | 1990240 | The role of islet amyloid polypeptide, also known as amylin, in insulin resistance and in the etiology of diabetes has been a subject of debate. |
| 558 | 1991568 | The recent discovery of the islet amyloid polypeptide (IAPP) or amylin, which is the major constituent of islet amyloid deposits, is integrated into this hypothesis. |
| 559 | 1991568 | It is suggested that pro-IAPP and proinsulin processing and mature peptide secretion normally occur together and that abnormal processing, secondary to or in conjunction with defects in hormone secretion, lead to progressive accumulation of intracellular IAPP and pro-IAPP, which in cats, monkeys, and humans form intracellular fibrils and amyloid deposits with a loss of beta-cell mass. |
| 560 | 1991568 | The recent discovery of the islet amyloid polypeptide (IAPP) or amylin, which is the major constituent of islet amyloid deposits, is integrated into this hypothesis. |
| 561 | 1991568 | It is suggested that pro-IAPP and proinsulin processing and mature peptide secretion normally occur together and that abnormal processing, secondary to or in conjunction with defects in hormone secretion, lead to progressive accumulation of intracellular IAPP and pro-IAPP, which in cats, monkeys, and humans form intracellular fibrils and amyloid deposits with a loss of beta-cell mass. |
| 562 | 1999270 | Newly identified pancreatic protein islet amyloid polypeptide. |
| 563 | 1999270 | Islet amyloid polypeptide (IAPP) or amylin is a newly identified 37-amino acid COOH-terminal-amidated polypeptide that is the major protein constituent of amyloid deposits in insulinomas and amyloid deposits in pancreatic islets of non-insulin-dependent (type II) diabetic humans and adult diabetic cats. |
| 564 | 1999270 | Newly identified pancreatic protein islet amyloid polypeptide. |
| 565 | 1999270 | Islet amyloid polypeptide (IAPP) or amylin is a newly identified 37-amino acid COOH-terminal-amidated polypeptide that is the major protein constituent of amyloid deposits in insulinomas and amyloid deposits in pancreatic islets of non-insulin-dependent (type II) diabetic humans and adult diabetic cats. |
| 566 | 1999269 | Is islet amyloid polypeptide a significant factor in pathogenesis or pathophysiology of diabetes? |
| 567 | 1999269 | Islet amyloid polypeptide (IAPP) or amylin, a recently discovered minor secretory peptide of the beta-cell related to calcitonin gene-related peptide (CGRP), is a constituent of amyloid deposits in the islets of many non-insulin-dependent (type II) diabetic individuals and some elderly nondiabetic subjects. |
| 568 | 1999269 | Like CGRP, IAPP antagonizes the action of insulin mainly at the level of muscle glycogen synthesis, but the levels required for this effect seem to be considerably higher than reported circulating levels. |
| 569 | 1999269 | Is islet amyloid polypeptide a significant factor in pathogenesis or pathophysiology of diabetes? |
| 570 | 1999269 | Islet amyloid polypeptide (IAPP) or amylin, a recently discovered minor secretory peptide of the beta-cell related to calcitonin gene-related peptide (CGRP), is a constituent of amyloid deposits in the islets of many non-insulin-dependent (type II) diabetic individuals and some elderly nondiabetic subjects. |
| 571 | 1999269 | Like CGRP, IAPP antagonizes the action of insulin mainly at the level of muscle glycogen synthesis, but the levels required for this effect seem to be considerably higher than reported circulating levels. |
| 572 | 2000701 | Amyloid protein in somatostatinoma differs from human islet amyloid polypeptide. |
| 573 | 2000701 | To examine the characteristics of this amyloid, we compared amyloid deposits in a somatostatinoma to those found in pancreatic tissue in patients with Type II diabetes mellitus and in insulinomas, using immunohistochemical techniques and specific antibodies to islet amyloid polypeptide or other pancreatic hormones, as well as electron-microscopy. |
| 574 | 2000701 | Antibodies to islet amyloid polypeptide regions 8-17 or 25-37 were confirmed to be specific. |
| 575 | 2000701 | Amyloid deposits in patients with Type II diabetes mellitus and in insulinomas, but not those in the somatostatinoma strongly reacted with these antibodies, or to an antibody to amyloid P component. |
| 576 | 2000701 | As amyloid in somatostatinomas is unlike that consisting of islet amyloid polypeptide or other mature pancreatic hormones, it may be a novel type of local amyloid in pancreatic islets. |
| 577 | 2000701 | Amyloid protein in somatostatinoma differs from human islet amyloid polypeptide. |
| 578 | 2000701 | To examine the characteristics of this amyloid, we compared amyloid deposits in a somatostatinoma to those found in pancreatic tissue in patients with Type II diabetes mellitus and in insulinomas, using immunohistochemical techniques and specific antibodies to islet amyloid polypeptide or other pancreatic hormones, as well as electron-microscopy. |
| 579 | 2000701 | Antibodies to islet amyloid polypeptide regions 8-17 or 25-37 were confirmed to be specific. |
| 580 | 2000701 | Amyloid deposits in patients with Type II diabetes mellitus and in insulinomas, but not those in the somatostatinoma strongly reacted with these antibodies, or to an antibody to amyloid P component. |
| 581 | 2000701 | As amyloid in somatostatinomas is unlike that consisting of islet amyloid polypeptide or other mature pancreatic hormones, it may be a novel type of local amyloid in pancreatic islets. |
| 582 | 2000701 | Amyloid protein in somatostatinoma differs from human islet amyloid polypeptide. |
| 583 | 2000701 | To examine the characteristics of this amyloid, we compared amyloid deposits in a somatostatinoma to those found in pancreatic tissue in patients with Type II diabetes mellitus and in insulinomas, using immunohistochemical techniques and specific antibodies to islet amyloid polypeptide or other pancreatic hormones, as well as electron-microscopy. |
| 584 | 2000701 | Antibodies to islet amyloid polypeptide regions 8-17 or 25-37 were confirmed to be specific. |
| 585 | 2000701 | Amyloid deposits in patients with Type II diabetes mellitus and in insulinomas, but not those in the somatostatinoma strongly reacted with these antibodies, or to an antibody to amyloid P component. |
| 586 | 2000701 | As amyloid in somatostatinomas is unlike that consisting of islet amyloid polypeptide or other mature pancreatic hormones, it may be a novel type of local amyloid in pancreatic islets. |
| 587 | 2000701 | Amyloid protein in somatostatinoma differs from human islet amyloid polypeptide. |
| 588 | 2000701 | To examine the characteristics of this amyloid, we compared amyloid deposits in a somatostatinoma to those found in pancreatic tissue in patients with Type II diabetes mellitus and in insulinomas, using immunohistochemical techniques and specific antibodies to islet amyloid polypeptide or other pancreatic hormones, as well as electron-microscopy. |
| 589 | 2000701 | Antibodies to islet amyloid polypeptide regions 8-17 or 25-37 were confirmed to be specific. |
| 590 | 2000701 | Amyloid deposits in patients with Type II diabetes mellitus and in insulinomas, but not those in the somatostatinoma strongly reacted with these antibodies, or to an antibody to amyloid P component. |
| 591 | 2000701 | As amyloid in somatostatinomas is unlike that consisting of islet amyloid polypeptide or other mature pancreatic hormones, it may be a novel type of local amyloid in pancreatic islets. |
| 592 | 2000701 | Amyloid protein in somatostatinoma differs from human islet amyloid polypeptide. |
| 593 | 2000701 | To examine the characteristics of this amyloid, we compared amyloid deposits in a somatostatinoma to those found in pancreatic tissue in patients with Type II diabetes mellitus and in insulinomas, using immunohistochemical techniques and specific antibodies to islet amyloid polypeptide or other pancreatic hormones, as well as electron-microscopy. |
| 594 | 2000701 | Antibodies to islet amyloid polypeptide regions 8-17 or 25-37 were confirmed to be specific. |
| 595 | 2000701 | Amyloid deposits in patients with Type II diabetes mellitus and in insulinomas, but not those in the somatostatinoma strongly reacted with these antibodies, or to an antibody to amyloid P component. |
| 596 | 2000701 | As amyloid in somatostatinomas is unlike that consisting of islet amyloid polypeptide or other mature pancreatic hormones, it may be a novel type of local amyloid in pancreatic islets. |
| 597 | 2010042 | This protein, termed islet amyloid polypeptide, is related to two neuropeptides, calcitonin gene-related peptides 1 and 2, and represents a new beta-cell secretory product whose normal physiological function remains to be determined. |
| 598 | 2010042 | Characterization of the insulin-receptor gene in patients with extreme forms of insulin resistance has resulted in the identification of mutations that impair its function and lead to tissue resistance to the action of insulin. |
| 599 | 2015054 | Depletion of islet amyloid polypeptide in the spontaneously diabetic (BB) Wistar rat. |
| 600 | 2015054 | Islet amyloid polypeptide (IAPP) in the pancreas of the spontaneously diabetic (BB) Wistar rat was examined by radioimmunoassay, and IAPP mRNA levels were determined by Northern blotting. |
| 601 | 2015054 | Insulin mRNA was dramatically reduced to only 4% of the control group and, in contrast, somatostatin was relatively unaffected, with the diabetic group retaining 86% of signal compared with the controls. |
| 602 | 2015054 | Depletion of islet amyloid polypeptide in the spontaneously diabetic (BB) Wistar rat. |
| 603 | 2015054 | Islet amyloid polypeptide (IAPP) in the pancreas of the spontaneously diabetic (BB) Wistar rat was examined by radioimmunoassay, and IAPP mRNA levels were determined by Northern blotting. |
| 604 | 2015054 | Insulin mRNA was dramatically reduced to only 4% of the control group and, in contrast, somatostatin was relatively unaffected, with the diabetic group retaining 86% of signal compared with the controls. |
| 605 | 2028355 | This review discusses recent advances in understanding of the structure and function of the insulin receptor and insulin action, and how these relate to the clinical aspects of insulin resistance associated with non-insulin-dependent diabetes and other disorders. |
| 606 | 2028355 | Receptor-mediated insulin resistance may be a consequence of various factors including increased serine/threonine phosphorylation of the receptor with decreased tyrosine phosphorylation, receptor desensitization, auto-antibodies to the receptor and inherited structural defects in the insulin receptor. |
| 607 | 2028355 | Other circulating hormones, such as the newly characterised islet amyloid polypeptide (amylin), may also cause insulin resistance. |
| 608 | 2035254 | Islet amyloid polypeptide in insulinoma and in the islets of the pancreas of non-diabetic and diabetic subjects. |
| 609 | 2035254 | The present immunohistochemical study revealed that normal B-cells, insulinoma, and amyloid deposits in insulinoma and diabetic pancreatic islets were commonly immunoreactive with antiserum to C-terminal synthetic tetradecapeptide of human islet amyloid polypeptide (IAPP) (24-37). |
| 610 | 2035254 | Islet amyloid polypeptide in insulinoma and in the islets of the pancreas of non-diabetic and diabetic subjects. |
| 611 | 2035254 | The present immunohistochemical study revealed that normal B-cells, insulinoma, and amyloid deposits in insulinoma and diabetic pancreatic islets were commonly immunoreactive with antiserum to C-terminal synthetic tetradecapeptide of human islet amyloid polypeptide (IAPP) (24-37). |
| 612 | 2036958 | Hypersecretion of islet amyloid polypeptide from pancreatic islets of ventromedial hypothalamic-lesioned rats and obese Zucker rats. |
| 613 | 2036958 | To investigate the possible role of islet amyloid polypeptide (IAPP) in the development of type 2 diabetes mellitus, we examined the IAPP content and secretion in pancreatic islets isolated from ventromedial hypothalamic (VMH)-lesioned rats and genetically obese Zucker rats, using a specific RIA for IAPP. |
| 614 | 2036958 | Hypersecretion of islet amyloid polypeptide from pancreatic islets of ventromedial hypothalamic-lesioned rats and obese Zucker rats. |
| 615 | 2036958 | To investigate the possible role of islet amyloid polypeptide (IAPP) in the development of type 2 diabetes mellitus, we examined the IAPP content and secretion in pancreatic islets isolated from ventromedial hypothalamic (VMH)-lesioned rats and genetically obese Zucker rats, using a specific RIA for IAPP. |
| 616 | 2043439 | Musculoskeletal problems in chronic renal failure are common, but investigations into their pathogenesis are complicated by the coexistence of renal endocrine failure and beta 2-microglobulin-related amyloid deposition in long-term dialysis patients. |
| 617 | 2059220 | Amylin, an islet amyloid peptide secreted by the pancreatic beta cell, has been proposed as a humoral regulator of islet insulin secretion. |
| 618 | 2065848 | Plasma islet amyloid polypeptide (Amylin) levels and their responses to oral glucose in type 2 (non-insulin-dependent) diabetic patients. |
| 619 | 2065848 | Fasting plasma islet amyloid polypeptide concentrations and their responses to an oral glucose load were determined in non-diabetic control subjects and patients with abnormal glucose tolerance in relation to the responses of insulin or C-peptide. |
| 620 | 2065848 | Plasma islet amyloid polypeptide was measured by radioimmunoassay. |
| 621 | 2065848 | In the non-diabetic control subjects, fasting plasma islet amyloid polypeptide was 6.4 +/- 0.5 fmol/ml (mean +/- SEM) and was about 1/7 less in molar basis than in insulin. |
| 622 | 2065848 | The fasting islet amyloid polypeptide level rose in obese patients and fell in patients with Type 1 (insulin-dependent) diabetes mellitus. |
| 623 | 2065848 | In non-obese patients with impaired glucose tolerance and Type 2 (non-insulin-dependent) diabetic patients without insulin therapy, the level was equal to that of the control subjects, but a low concentration of islet amyloid polypeptide relative to insulin or C-peptide was observed in the non-obese Type 2 diabetic group. |
| 624 | 2065848 | The patterns of plasma islet amyloid polypeptide responses after oral glucose were similar to those of insulin or C-peptide. |
| 625 | 2065848 | However, compared to non-obese patients, a hyper-response of islet amyloid polypeptide relative to C-peptide was noted in obese patients who had a hyper-response of insulin relative to C-peptide. |
| 626 | 2065848 | This study suggests that basal hypo-secretion of islet amyloid polypeptide relative to insulin exists in non-obese Type 2 diabetes and that circulating islet amyloid polypeptide may act physiologically with insulin to modulate the glucose metabolism. |
| 627 | 2065848 | Plasma islet amyloid polypeptide (Amylin) levels and their responses to oral glucose in type 2 (non-insulin-dependent) diabetic patients. |
| 628 | 2065848 | Fasting plasma islet amyloid polypeptide concentrations and their responses to an oral glucose load were determined in non-diabetic control subjects and patients with abnormal glucose tolerance in relation to the responses of insulin or C-peptide. |
| 629 | 2065848 | Plasma islet amyloid polypeptide was measured by radioimmunoassay. |
| 630 | 2065848 | In the non-diabetic control subjects, fasting plasma islet amyloid polypeptide was 6.4 +/- 0.5 fmol/ml (mean +/- SEM) and was about 1/7 less in molar basis than in insulin. |
| 631 | 2065848 | The fasting islet amyloid polypeptide level rose in obese patients and fell in patients with Type 1 (insulin-dependent) diabetes mellitus. |
| 632 | 2065848 | In non-obese patients with impaired glucose tolerance and Type 2 (non-insulin-dependent) diabetic patients without insulin therapy, the level was equal to that of the control subjects, but a low concentration of islet amyloid polypeptide relative to insulin or C-peptide was observed in the non-obese Type 2 diabetic group. |
| 633 | 2065848 | The patterns of plasma islet amyloid polypeptide responses after oral glucose were similar to those of insulin or C-peptide. |
| 634 | 2065848 | However, compared to non-obese patients, a hyper-response of islet amyloid polypeptide relative to C-peptide was noted in obese patients who had a hyper-response of insulin relative to C-peptide. |
| 635 | 2065848 | This study suggests that basal hypo-secretion of islet amyloid polypeptide relative to insulin exists in non-obese Type 2 diabetes and that circulating islet amyloid polypeptide may act physiologically with insulin to modulate the glucose metabolism. |
| 636 | 2065848 | Plasma islet amyloid polypeptide (Amylin) levels and their responses to oral glucose in type 2 (non-insulin-dependent) diabetic patients. |
| 637 | 2065848 | Fasting plasma islet amyloid polypeptide concentrations and their responses to an oral glucose load were determined in non-diabetic control subjects and patients with abnormal glucose tolerance in relation to the responses of insulin or C-peptide. |
| 638 | 2065848 | Plasma islet amyloid polypeptide was measured by radioimmunoassay. |
| 639 | 2065848 | In the non-diabetic control subjects, fasting plasma islet amyloid polypeptide was 6.4 +/- 0.5 fmol/ml (mean +/- SEM) and was about 1/7 less in molar basis than in insulin. |
| 640 | 2065848 | The fasting islet amyloid polypeptide level rose in obese patients and fell in patients with Type 1 (insulin-dependent) diabetes mellitus. |
| 641 | 2065848 | In non-obese patients with impaired glucose tolerance and Type 2 (non-insulin-dependent) diabetic patients without insulin therapy, the level was equal to that of the control subjects, but a low concentration of islet amyloid polypeptide relative to insulin or C-peptide was observed in the non-obese Type 2 diabetic group. |
| 642 | 2065848 | The patterns of plasma islet amyloid polypeptide responses after oral glucose were similar to those of insulin or C-peptide. |
| 643 | 2065848 | However, compared to non-obese patients, a hyper-response of islet amyloid polypeptide relative to C-peptide was noted in obese patients who had a hyper-response of insulin relative to C-peptide. |
| 644 | 2065848 | This study suggests that basal hypo-secretion of islet amyloid polypeptide relative to insulin exists in non-obese Type 2 diabetes and that circulating islet amyloid polypeptide may act physiologically with insulin to modulate the glucose metabolism. |
| 645 | 2065848 | Plasma islet amyloid polypeptide (Amylin) levels and their responses to oral glucose in type 2 (non-insulin-dependent) diabetic patients. |
| 646 | 2065848 | Fasting plasma islet amyloid polypeptide concentrations and their responses to an oral glucose load were determined in non-diabetic control subjects and patients with abnormal glucose tolerance in relation to the responses of insulin or C-peptide. |
| 647 | 2065848 | Plasma islet amyloid polypeptide was measured by radioimmunoassay. |
| 648 | 2065848 | In the non-diabetic control subjects, fasting plasma islet amyloid polypeptide was 6.4 +/- 0.5 fmol/ml (mean +/- SEM) and was about 1/7 less in molar basis than in insulin. |
| 649 | 2065848 | The fasting islet amyloid polypeptide level rose in obese patients and fell in patients with Type 1 (insulin-dependent) diabetes mellitus. |
| 650 | 2065848 | In non-obese patients with impaired glucose tolerance and Type 2 (non-insulin-dependent) diabetic patients without insulin therapy, the level was equal to that of the control subjects, but a low concentration of islet amyloid polypeptide relative to insulin or C-peptide was observed in the non-obese Type 2 diabetic group. |
| 651 | 2065848 | The patterns of plasma islet amyloid polypeptide responses after oral glucose were similar to those of insulin or C-peptide. |
| 652 | 2065848 | However, compared to non-obese patients, a hyper-response of islet amyloid polypeptide relative to C-peptide was noted in obese patients who had a hyper-response of insulin relative to C-peptide. |
| 653 | 2065848 | This study suggests that basal hypo-secretion of islet amyloid polypeptide relative to insulin exists in non-obese Type 2 diabetes and that circulating islet amyloid polypeptide may act physiologically with insulin to modulate the glucose metabolism. |
| 654 | 2065848 | Plasma islet amyloid polypeptide (Amylin) levels and their responses to oral glucose in type 2 (non-insulin-dependent) diabetic patients. |
| 655 | 2065848 | Fasting plasma islet amyloid polypeptide concentrations and their responses to an oral glucose load were determined in non-diabetic control subjects and patients with abnormal glucose tolerance in relation to the responses of insulin or C-peptide. |
| 656 | 2065848 | Plasma islet amyloid polypeptide was measured by radioimmunoassay. |
| 657 | 2065848 | In the non-diabetic control subjects, fasting plasma islet amyloid polypeptide was 6.4 +/- 0.5 fmol/ml (mean +/- SEM) and was about 1/7 less in molar basis than in insulin. |
| 658 | 2065848 | The fasting islet amyloid polypeptide level rose in obese patients and fell in patients with Type 1 (insulin-dependent) diabetes mellitus. |
| 659 | 2065848 | In non-obese patients with impaired glucose tolerance and Type 2 (non-insulin-dependent) diabetic patients without insulin therapy, the level was equal to that of the control subjects, but a low concentration of islet amyloid polypeptide relative to insulin or C-peptide was observed in the non-obese Type 2 diabetic group. |
| 660 | 2065848 | The patterns of plasma islet amyloid polypeptide responses after oral glucose were similar to those of insulin or C-peptide. |
| 661 | 2065848 | However, compared to non-obese patients, a hyper-response of islet amyloid polypeptide relative to C-peptide was noted in obese patients who had a hyper-response of insulin relative to C-peptide. |
| 662 | 2065848 | This study suggests that basal hypo-secretion of islet amyloid polypeptide relative to insulin exists in non-obese Type 2 diabetes and that circulating islet amyloid polypeptide may act physiologically with insulin to modulate the glucose metabolism. |
| 663 | 2065848 | Plasma islet amyloid polypeptide (Amylin) levels and their responses to oral glucose in type 2 (non-insulin-dependent) diabetic patients. |
| 664 | 2065848 | Fasting plasma islet amyloid polypeptide concentrations and their responses to an oral glucose load were determined in non-diabetic control subjects and patients with abnormal glucose tolerance in relation to the responses of insulin or C-peptide. |
| 665 | 2065848 | Plasma islet amyloid polypeptide was measured by radioimmunoassay. |
| 666 | 2065848 | In the non-diabetic control subjects, fasting plasma islet amyloid polypeptide was 6.4 +/- 0.5 fmol/ml (mean +/- SEM) and was about 1/7 less in molar basis than in insulin. |
| 667 | 2065848 | The fasting islet amyloid polypeptide level rose in obese patients and fell in patients with Type 1 (insulin-dependent) diabetes mellitus. |
| 668 | 2065848 | In non-obese patients with impaired glucose tolerance and Type 2 (non-insulin-dependent) diabetic patients without insulin therapy, the level was equal to that of the control subjects, but a low concentration of islet amyloid polypeptide relative to insulin or C-peptide was observed in the non-obese Type 2 diabetic group. |
| 669 | 2065848 | The patterns of plasma islet amyloid polypeptide responses after oral glucose were similar to those of insulin or C-peptide. |
| 670 | 2065848 | However, compared to non-obese patients, a hyper-response of islet amyloid polypeptide relative to C-peptide was noted in obese patients who had a hyper-response of insulin relative to C-peptide. |
| 671 | 2065848 | This study suggests that basal hypo-secretion of islet amyloid polypeptide relative to insulin exists in non-obese Type 2 diabetes and that circulating islet amyloid polypeptide may act physiologically with insulin to modulate the glucose metabolism. |
| 672 | 2065848 | Plasma islet amyloid polypeptide (Amylin) levels and their responses to oral glucose in type 2 (non-insulin-dependent) diabetic patients. |
| 673 | 2065848 | Fasting plasma islet amyloid polypeptide concentrations and their responses to an oral glucose load were determined in non-diabetic control subjects and patients with abnormal glucose tolerance in relation to the responses of insulin or C-peptide. |
| 674 | 2065848 | Plasma islet amyloid polypeptide was measured by radioimmunoassay. |
| 675 | 2065848 | In the non-diabetic control subjects, fasting plasma islet amyloid polypeptide was 6.4 +/- 0.5 fmol/ml (mean +/- SEM) and was about 1/7 less in molar basis than in insulin. |
| 676 | 2065848 | The fasting islet amyloid polypeptide level rose in obese patients and fell in patients with Type 1 (insulin-dependent) diabetes mellitus. |
| 677 | 2065848 | In non-obese patients with impaired glucose tolerance and Type 2 (non-insulin-dependent) diabetic patients without insulin therapy, the level was equal to that of the control subjects, but a low concentration of islet amyloid polypeptide relative to insulin or C-peptide was observed in the non-obese Type 2 diabetic group. |
| 678 | 2065848 | The patterns of plasma islet amyloid polypeptide responses after oral glucose were similar to those of insulin or C-peptide. |
| 679 | 2065848 | However, compared to non-obese patients, a hyper-response of islet amyloid polypeptide relative to C-peptide was noted in obese patients who had a hyper-response of insulin relative to C-peptide. |
| 680 | 2065848 | This study suggests that basal hypo-secretion of islet amyloid polypeptide relative to insulin exists in non-obese Type 2 diabetes and that circulating islet amyloid polypeptide may act physiologically with insulin to modulate the glucose metabolism. |
| 681 | 2065848 | Plasma islet amyloid polypeptide (Amylin) levels and their responses to oral glucose in type 2 (non-insulin-dependent) diabetic patients. |
| 682 | 2065848 | Fasting plasma islet amyloid polypeptide concentrations and their responses to an oral glucose load were determined in non-diabetic control subjects and patients with abnormal glucose tolerance in relation to the responses of insulin or C-peptide. |
| 683 | 2065848 | Plasma islet amyloid polypeptide was measured by radioimmunoassay. |
| 684 | 2065848 | In the non-diabetic control subjects, fasting plasma islet amyloid polypeptide was 6.4 +/- 0.5 fmol/ml (mean +/- SEM) and was about 1/7 less in molar basis than in insulin. |
| 685 | 2065848 | The fasting islet amyloid polypeptide level rose in obese patients and fell in patients with Type 1 (insulin-dependent) diabetes mellitus. |
| 686 | 2065848 | In non-obese patients with impaired glucose tolerance and Type 2 (non-insulin-dependent) diabetic patients without insulin therapy, the level was equal to that of the control subjects, but a low concentration of islet amyloid polypeptide relative to insulin or C-peptide was observed in the non-obese Type 2 diabetic group. |
| 687 | 2065848 | The patterns of plasma islet amyloid polypeptide responses after oral glucose were similar to those of insulin or C-peptide. |
| 688 | 2065848 | However, compared to non-obese patients, a hyper-response of islet amyloid polypeptide relative to C-peptide was noted in obese patients who had a hyper-response of insulin relative to C-peptide. |
| 689 | 2065848 | This study suggests that basal hypo-secretion of islet amyloid polypeptide relative to insulin exists in non-obese Type 2 diabetes and that circulating islet amyloid polypeptide may act physiologically with insulin to modulate the glucose metabolism. |
| 690 | 2065848 | Plasma islet amyloid polypeptide (Amylin) levels and their responses to oral glucose in type 2 (non-insulin-dependent) diabetic patients. |
| 691 | 2065848 | Fasting plasma islet amyloid polypeptide concentrations and their responses to an oral glucose load were determined in non-diabetic control subjects and patients with abnormal glucose tolerance in relation to the responses of insulin or C-peptide. |
| 692 | 2065848 | Plasma islet amyloid polypeptide was measured by radioimmunoassay. |
| 693 | 2065848 | In the non-diabetic control subjects, fasting plasma islet amyloid polypeptide was 6.4 +/- 0.5 fmol/ml (mean +/- SEM) and was about 1/7 less in molar basis than in insulin. |
| 694 | 2065848 | The fasting islet amyloid polypeptide level rose in obese patients and fell in patients with Type 1 (insulin-dependent) diabetes mellitus. |
| 695 | 2065848 | In non-obese patients with impaired glucose tolerance and Type 2 (non-insulin-dependent) diabetic patients without insulin therapy, the level was equal to that of the control subjects, but a low concentration of islet amyloid polypeptide relative to insulin or C-peptide was observed in the non-obese Type 2 diabetic group. |
| 696 | 2065848 | The patterns of plasma islet amyloid polypeptide responses after oral glucose were similar to those of insulin or C-peptide. |
| 697 | 2065848 | However, compared to non-obese patients, a hyper-response of islet amyloid polypeptide relative to C-peptide was noted in obese patients who had a hyper-response of insulin relative to C-peptide. |
| 698 | 2065848 | This study suggests that basal hypo-secretion of islet amyloid polypeptide relative to insulin exists in non-obese Type 2 diabetes and that circulating islet amyloid polypeptide may act physiologically with insulin to modulate the glucose metabolism. |
| 699 | 2078850 | Islet amyloid polypeptide (IAPP) in the gastrointestinal tract and pancreas of man and rat. |
| 700 | 2078850 | An immunohistochemical study for islet amyloid polypeptide (IAPP) was made on the gastrointestinal (GI) tract and pancreas of man and rat, using antisera raised against a synthetic peptide of C-terminal human IAPP (24-37) and a synthetic peptide of rat IAPP (18-37). |
| 701 | 2078850 | An examination was made for evidence of colocalization of IAPP-immunoreactive material with material immunoreactive for gastrin, somatostatin, vasoactive intestinal polypeptide, pancreatic polypeptide, insulin, and glucagon, but none was found. |
| 702 | 2078850 | IAPP-immunoreactive cells were also found in the pancreas of non-diabetic and non-insulin-dependent diabetic patients, but they were completely absent from a patient with insulin-dependent diabetes mellitus despite the presence of IAPP in the plasma. |
| 703 | 2078850 | Islet amyloid polypeptide (IAPP) in the gastrointestinal tract and pancreas of man and rat. |
| 704 | 2078850 | An immunohistochemical study for islet amyloid polypeptide (IAPP) was made on the gastrointestinal (GI) tract and pancreas of man and rat, using antisera raised against a synthetic peptide of C-terminal human IAPP (24-37) and a synthetic peptide of rat IAPP (18-37). |
| 705 | 2078850 | An examination was made for evidence of colocalization of IAPP-immunoreactive material with material immunoreactive for gastrin, somatostatin, vasoactive intestinal polypeptide, pancreatic polypeptide, insulin, and glucagon, but none was found. |
| 706 | 2078850 | IAPP-immunoreactive cells were also found in the pancreas of non-diabetic and non-insulin-dependent diabetic patients, but they were completely absent from a patient with insulin-dependent diabetes mellitus despite the presence of IAPP in the plasma. |
| 707 | 2109283 | On electron-microscopy, collagen fibres were seen, while beta 2-M amyloid was consistently absent. |
| 708 | 2162304 | Activation of adenylate cyclase by islet amyloid polypeptide with COOH-terminal amide via calcitonin gene-related peptide receptors on rat liver plasma membranes. |
| 709 | 2162304 | Both human and rat islet amyloid polypeptide with COOH-terminal amide (IAPP-NH2) dose-dependently displaced the specific binding of 125I-labeled [Tyr0] rat alpha-calcitonin gene-related peptide (CGRP) to rat liver plasma membranes, whereas human IAPP (IAPP-COOH) had no effect. |
| 710 | 2162304 | Conversely, human or rat IAPP-NH2 but not human IAPP-COOH evoked dose-dependent activation of adenylate cyclase in the membranes, and these effects were significantly inhibited by the CGRP-receptor antagonist human CGRP-1(8-37). |
| 711 | 2162304 | Thus, IAPP-NH2 but not IAPP-COOH appears to induce adenylate cyclase activation via CGRP receptors on rat liver plasma membranes. |
| 712 | 2162304 | Activation of adenylate cyclase by islet amyloid polypeptide with COOH-terminal amide via calcitonin gene-related peptide receptors on rat liver plasma membranes. |
| 713 | 2162304 | Both human and rat islet amyloid polypeptide with COOH-terminal amide (IAPP-NH2) dose-dependently displaced the specific binding of 125I-labeled [Tyr0] rat alpha-calcitonin gene-related peptide (CGRP) to rat liver plasma membranes, whereas human IAPP (IAPP-COOH) had no effect. |
| 714 | 2162304 | Conversely, human or rat IAPP-NH2 but not human IAPP-COOH evoked dose-dependent activation of adenylate cyclase in the membranes, and these effects were significantly inhibited by the CGRP-receptor antagonist human CGRP-1(8-37). |
| 715 | 2162304 | Thus, IAPP-NH2 but not IAPP-COOH appears to induce adenylate cyclase activation via CGRP receptors on rat liver plasma membranes. |
| 716 | 2172004 | Aberrant expression of the islet amyloid polypeptide (IAPP) gene might be involved in the pathogenesis of non-insulin-dependent diabetes mellitus (NIDDM). |
| 717 | 2182015 | The putative hormone islet amyloid polypeptide (IAPP) induces impaired glucose tolerance in cats. |
| 718 | 2182015 | Islet amyloid polypeptide (IAPP) has been implicated by in vitro studies as an inhibitor of insulin-stimulated glucose utilization by skeletal muscle cells and also as an inhibitor of insulin-stimulated insulin secretion by beta cells. |
| 719 | 2182015 | The putative hormone islet amyloid polypeptide (IAPP) induces impaired glucose tolerance in cats. |
| 720 | 2182015 | Islet amyloid polypeptide (IAPP) has been implicated by in vitro studies as an inhibitor of insulin-stimulated glucose utilization by skeletal muscle cells and also as an inhibitor of insulin-stimulated insulin secretion by beta cells. |
| 721 | 2183542 | Failure of islet amyloid polypeptide to inhibit basal and glucose-stimulated insulin secretion in model experiments in mice and rats. |
| 722 | 2183542 | Islet amyloid polypeptide (IAPP), also known as amylin, has previously been demonstrated to occur in amyloid deposits in pancreatic islets in type 2 diabetics, and, therefore, the peptide has been suggested to be involved in the pathogenesis of diabetes. |
| 723 | 2183542 | The 37 amino acid peptide shows approximately 50% homology with the intrapancreatic neuropeptide calcitonin gene-related peptide (CGRP), a peptide that inhibits insulin secretion. |
| 724 | 2183542 | IAPP was given intravenously, at dose levels at which CGRP previously has been shown to inhibit insulin secretion. |
| 725 | 2183542 | Hence, in mice and rats, IAPP does not inhibit insulin secretion under experimental conditions identical to those previously used to demonstrate an inhibition by CGRP. |
| 726 | 2183542 | Therefore, we conclude (1) that the homologous amino acid sequence within IAPP and CGRP does not seem to be sufficient for inducing inhibition of insulin release in mice and rats and (2) that the possible involvement of IAPP in the pathogenesis of diabetes type 2 still remains speculative. |
| 727 | 2183542 | Failure of islet amyloid polypeptide to inhibit basal and glucose-stimulated insulin secretion in model experiments in mice and rats. |
| 728 | 2183542 | Islet amyloid polypeptide (IAPP), also known as amylin, has previously been demonstrated to occur in amyloid deposits in pancreatic islets in type 2 diabetics, and, therefore, the peptide has been suggested to be involved in the pathogenesis of diabetes. |
| 729 | 2183542 | The 37 amino acid peptide shows approximately 50% homology with the intrapancreatic neuropeptide calcitonin gene-related peptide (CGRP), a peptide that inhibits insulin secretion. |
| 730 | 2183542 | IAPP was given intravenously, at dose levels at which CGRP previously has been shown to inhibit insulin secretion. |
| 731 | 2183542 | Hence, in mice and rats, IAPP does not inhibit insulin secretion under experimental conditions identical to those previously used to demonstrate an inhibition by CGRP. |
| 732 | 2183542 | Therefore, we conclude (1) that the homologous amino acid sequence within IAPP and CGRP does not seem to be sufficient for inducing inhibition of insulin release in mice and rats and (2) that the possible involvement of IAPP in the pathogenesis of diabetes type 2 still remains speculative. |
| 733 | 2184060 | Islet amyloid polypeptide amide causes peripheral insulin resistance in vivo in dogs. |
| 734 | 2184060 | Islet amyloid polypeptide is a 37 amino acid hormone-like peptide which is the major protein component of islet amyloid deposits commonly found in patients with Type 2 (non-insulin-dependent) diabetes mellitus. |
| 735 | 2184060 | In order to clarify the possible in vivo actions of islet amyloid polypeptide, we have studied the effects of synthesized islet amyloid polypeptide-amide on peripheral glucose utilization by performing hyperinsulinaemic euglycaemic glucose clamp studies on dogs. |
| 736 | 2184060 | Exogenously administered islet amyloid polypeptide-amide (an infusion from 1.0 to 100 micrograms.kg-1.h-1, over 2 h) inhibited the insulin-stimulated glucose disposal rate in a dose dependent manner. |
| 737 | 2184060 | Twenty-five micrograms.kg-1.h-1 of islet amyloid polypeptide-amide infused via a peripheral vein significantly lowered the glucose disposal rate by 20% (from 17.4 +/- 1.7 to 14.4 +/- 1.7 mg.kg-1.min-1, n = 5, p less than 0.01). |
| 738 | 2184060 | These findings suggest that islet amyloid polypeptide-amide causes peripheral insulin resistance in vivo. |
| 739 | 2184060 | Islet amyloid polypeptide amide causes peripheral insulin resistance in vivo in dogs. |
| 740 | 2184060 | Islet amyloid polypeptide is a 37 amino acid hormone-like peptide which is the major protein component of islet amyloid deposits commonly found in patients with Type 2 (non-insulin-dependent) diabetes mellitus. |
| 741 | 2184060 | In order to clarify the possible in vivo actions of islet amyloid polypeptide, we have studied the effects of synthesized islet amyloid polypeptide-amide on peripheral glucose utilization by performing hyperinsulinaemic euglycaemic glucose clamp studies on dogs. |
| 742 | 2184060 | Exogenously administered islet amyloid polypeptide-amide (an infusion from 1.0 to 100 micrograms.kg-1.h-1, over 2 h) inhibited the insulin-stimulated glucose disposal rate in a dose dependent manner. |
| 743 | 2184060 | Twenty-five micrograms.kg-1.h-1 of islet amyloid polypeptide-amide infused via a peripheral vein significantly lowered the glucose disposal rate by 20% (from 17.4 +/- 1.7 to 14.4 +/- 1.7 mg.kg-1.min-1, n = 5, p less than 0.01). |
| 744 | 2184060 | These findings suggest that islet amyloid polypeptide-amide causes peripheral insulin resistance in vivo. |
| 745 | 2184060 | Islet amyloid polypeptide amide causes peripheral insulin resistance in vivo in dogs. |
| 746 | 2184060 | Islet amyloid polypeptide is a 37 amino acid hormone-like peptide which is the major protein component of islet amyloid deposits commonly found in patients with Type 2 (non-insulin-dependent) diabetes mellitus. |
| 747 | 2184060 | In order to clarify the possible in vivo actions of islet amyloid polypeptide, we have studied the effects of synthesized islet amyloid polypeptide-amide on peripheral glucose utilization by performing hyperinsulinaemic euglycaemic glucose clamp studies on dogs. |
| 748 | 2184060 | Exogenously administered islet amyloid polypeptide-amide (an infusion from 1.0 to 100 micrograms.kg-1.h-1, over 2 h) inhibited the insulin-stimulated glucose disposal rate in a dose dependent manner. |
| 749 | 2184060 | Twenty-five micrograms.kg-1.h-1 of islet amyloid polypeptide-amide infused via a peripheral vein significantly lowered the glucose disposal rate by 20% (from 17.4 +/- 1.7 to 14.4 +/- 1.7 mg.kg-1.min-1, n = 5, p less than 0.01). |
| 750 | 2184060 | These findings suggest that islet amyloid polypeptide-amide causes peripheral insulin resistance in vivo. |
| 751 | 2184060 | Islet amyloid polypeptide amide causes peripheral insulin resistance in vivo in dogs. |
| 752 | 2184060 | Islet amyloid polypeptide is a 37 amino acid hormone-like peptide which is the major protein component of islet amyloid deposits commonly found in patients with Type 2 (non-insulin-dependent) diabetes mellitus. |
| 753 | 2184060 | In order to clarify the possible in vivo actions of islet amyloid polypeptide, we have studied the effects of synthesized islet amyloid polypeptide-amide on peripheral glucose utilization by performing hyperinsulinaemic euglycaemic glucose clamp studies on dogs. |
| 754 | 2184060 | Exogenously administered islet amyloid polypeptide-amide (an infusion from 1.0 to 100 micrograms.kg-1.h-1, over 2 h) inhibited the insulin-stimulated glucose disposal rate in a dose dependent manner. |
| 755 | 2184060 | Twenty-five micrograms.kg-1.h-1 of islet amyloid polypeptide-amide infused via a peripheral vein significantly lowered the glucose disposal rate by 20% (from 17.4 +/- 1.7 to 14.4 +/- 1.7 mg.kg-1.min-1, n = 5, p less than 0.01). |
| 756 | 2184060 | These findings suggest that islet amyloid polypeptide-amide causes peripheral insulin resistance in vivo. |
| 757 | 2184060 | Islet amyloid polypeptide amide causes peripheral insulin resistance in vivo in dogs. |
| 758 | 2184060 | Islet amyloid polypeptide is a 37 amino acid hormone-like peptide which is the major protein component of islet amyloid deposits commonly found in patients with Type 2 (non-insulin-dependent) diabetes mellitus. |
| 759 | 2184060 | In order to clarify the possible in vivo actions of islet amyloid polypeptide, we have studied the effects of synthesized islet amyloid polypeptide-amide on peripheral glucose utilization by performing hyperinsulinaemic euglycaemic glucose clamp studies on dogs. |
| 760 | 2184060 | Exogenously administered islet amyloid polypeptide-amide (an infusion from 1.0 to 100 micrograms.kg-1.h-1, over 2 h) inhibited the insulin-stimulated glucose disposal rate in a dose dependent manner. |
| 761 | 2184060 | Twenty-five micrograms.kg-1.h-1 of islet amyloid polypeptide-amide infused via a peripheral vein significantly lowered the glucose disposal rate by 20% (from 17.4 +/- 1.7 to 14.4 +/- 1.7 mg.kg-1.min-1, n = 5, p less than 0.01). |
| 762 | 2184060 | These findings suggest that islet amyloid polypeptide-amide causes peripheral insulin resistance in vivo. |
| 763 | 2184060 | Islet amyloid polypeptide amide causes peripheral insulin resistance in vivo in dogs. |
| 764 | 2184060 | Islet amyloid polypeptide is a 37 amino acid hormone-like peptide which is the major protein component of islet amyloid deposits commonly found in patients with Type 2 (non-insulin-dependent) diabetes mellitus. |
| 765 | 2184060 | In order to clarify the possible in vivo actions of islet amyloid polypeptide, we have studied the effects of synthesized islet amyloid polypeptide-amide on peripheral glucose utilization by performing hyperinsulinaemic euglycaemic glucose clamp studies on dogs. |
| 766 | 2184060 | Exogenously administered islet amyloid polypeptide-amide (an infusion from 1.0 to 100 micrograms.kg-1.h-1, over 2 h) inhibited the insulin-stimulated glucose disposal rate in a dose dependent manner. |
| 767 | 2184060 | Twenty-five micrograms.kg-1.h-1 of islet amyloid polypeptide-amide infused via a peripheral vein significantly lowered the glucose disposal rate by 20% (from 17.4 +/- 1.7 to 14.4 +/- 1.7 mg.kg-1.min-1, n = 5, p less than 0.01). |
| 768 | 2184060 | These findings suggest that islet amyloid polypeptide-amide causes peripheral insulin resistance in vivo. |
| 769 | 2185112 | Evidence of cosecretion of islet amyloid polypeptide and insulin by beta-cells. |
| 770 | 2185112 | Islet amyloid polypeptide (IAPP) has been identified as the major constituent of the pancreatic amyloid of non-insulin-dependent diabetes mellitus (NIDDM) and is also present in normal beta-cell secretory granules. |
| 771 | 2185112 | Evidence of cosecretion of islet amyloid polypeptide and insulin by beta-cells. |
| 772 | 2185112 | Islet amyloid polypeptide (IAPP) has been identified as the major constituent of the pancreatic amyloid of non-insulin-dependent diabetes mellitus (NIDDM) and is also present in normal beta-cell secretory granules. |
| 773 | 2191889 | Lack of islet amyloid polypeptide regulation of insulin biosynthesis or secretion in normal rat islets. |
| 774 | 2191889 | We examined the effects of rat islet amyloid polypeptide (IAPP) on insulin biosynthesis and secretion by isolated rat islets of Langerhans. |
| 775 | 2191889 | Lack of islet amyloid polypeptide regulation of insulin biosynthesis or secretion in normal rat islets. |
| 776 | 2191889 | We examined the effects of rat islet amyloid polypeptide (IAPP) on insulin biosynthesis and secretion by isolated rat islets of Langerhans. |
| 777 | 2192709 | Islet amyloid polypeptide (IAPP) is a recently discovered pancreatic islet hormone which is stored with insulin in beta cell granules. |
| 778 | 2192709 | IAPP may have a significant role in the development of Type 2 diabetes mellitus due to its propensity to form islet cell-disrupting amyloid deposits, and by opposing the action of insulin in peripheral tissues. |
| 779 | 2192709 | Islet amyloid polypeptide (IAPP) is a recently discovered pancreatic islet hormone which is stored with insulin in beta cell granules. |
| 780 | 2192709 | IAPP may have a significant role in the development of Type 2 diabetes mellitus due to its propensity to form islet cell-disrupting amyloid deposits, and by opposing the action of insulin in peripheral tissues. |
| 781 | 2195544 | Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation. |
| 782 | 2195544 | Islet amyloid polypeptide (IAPP), a putative polypeptide hormone, is a product of pancreatic beta-cells and the major constituent of the amyloid deposits seen mainly in islets of type 2 diabetic humans and diabetic cats. |
| 783 | 2195544 | Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation. |
| 784 | 2195544 | Islet amyloid polypeptide (IAPP), a putative polypeptide hormone, is a product of pancreatic beta-cells and the major constituent of the amyloid deposits seen mainly in islets of type 2 diabetic humans and diabetic cats. |
| 785 | 2198187 | Islet amyloid polypeptide in diabetic and non-diabetic Pima Indians. |
| 786 | 2198187 | Islet amyloid may have a pathological role in the development of Type 2 (non-insulin-dependent) diabetes mellitus. |
| 787 | 2198187 | Islets were examined for amyloid deposits and for cellular immunoreactivity to pancreatic hormones and islet amyloid polypeptide, the constituent peptide of islet amyloid. |
| 788 | 2198187 | Islet amyloid in diabetic Pima Indians may indicate a primary Beta-cell defect which interacts with insulin resistance to produce diabetes, or may develop as a result of Beta-cell dysfunction induced by insulin resistance and hyperglycaemia. |
| 789 | 2198187 | Islet amyloid polypeptide in diabetic and non-diabetic Pima Indians. |
| 790 | 2198187 | Islet amyloid may have a pathological role in the development of Type 2 (non-insulin-dependent) diabetes mellitus. |
| 791 | 2198187 | Islets were examined for amyloid deposits and for cellular immunoreactivity to pancreatic hormones and islet amyloid polypeptide, the constituent peptide of islet amyloid. |
| 792 | 2198187 | Islet amyloid in diabetic Pima Indians may indicate a primary Beta-cell defect which interacts with insulin resistance to produce diabetes, or may develop as a result of Beta-cell dysfunction induced by insulin resistance and hyperglycaemia. |
| 793 | 2198187 | Islet amyloid polypeptide in diabetic and non-diabetic Pima Indians. |
| 794 | 2198187 | Islet amyloid may have a pathological role in the development of Type 2 (non-insulin-dependent) diabetes mellitus. |
| 795 | 2198187 | Islets were examined for amyloid deposits and for cellular immunoreactivity to pancreatic hormones and islet amyloid polypeptide, the constituent peptide of islet amyloid. |
| 796 | 2198187 | Islet amyloid in diabetic Pima Indians may indicate a primary Beta-cell defect which interacts with insulin resistance to produce diabetes, or may develop as a result of Beta-cell dysfunction induced by insulin resistance and hyperglycaemia. |
| 797 | 2198187 | Islet amyloid polypeptide in diabetic and non-diabetic Pima Indians. |
| 798 | 2198187 | Islet amyloid may have a pathological role in the development of Type 2 (non-insulin-dependent) diabetes mellitus. |
| 799 | 2198187 | Islets were examined for amyloid deposits and for cellular immunoreactivity to pancreatic hormones and islet amyloid polypeptide, the constituent peptide of islet amyloid. |
| 800 | 2198187 | Islet amyloid in diabetic Pima Indians may indicate a primary Beta-cell defect which interacts with insulin resistance to produce diabetes, or may develop as a result of Beta-cell dysfunction induced by insulin resistance and hyperglycaemia. |
| 801 | 2202297 | Islet amyloid polypeptide (IAPP) does not inhibit glucose-stimulated insulin secretion from isolated perfused rat pancreas. |
| 802 | 2202297 | Islet amyloid polypeptide (IAPP) is a recently discovered pancreatic islet hormone which is stored with insulin in the secretory vesicles of beta cells. |
| 803 | 2202297 | Islet amyloid polypeptide (IAPP) does not inhibit glucose-stimulated insulin secretion from isolated perfused rat pancreas. |
| 804 | 2202297 | Islet amyloid polypeptide (IAPP) is a recently discovered pancreatic islet hormone which is stored with insulin in the secretory vesicles of beta cells. |
| 805 | 2210054 | Structure of cat islet amyloid polypeptide and identification of amino acid residues of potential significance for islet amyloid formation. |
| 806 | 2210054 | Cats and humans, unlike most rodent species, develop amyloid in the islets of Langerhans in conjunction with non-insulin-dependent diabetes mellitus. |
| 807 | 2210054 | The amyloid consists of a 37-amino acid polypeptide referred to as islet amyloid polypeptide (IAPP). |
| 808 | 2210054 | Structure of cat islet amyloid polypeptide and identification of amino acid residues of potential significance for islet amyloid formation. |
| 809 | 2210054 | Cats and humans, unlike most rodent species, develop amyloid in the islets of Langerhans in conjunction with non-insulin-dependent diabetes mellitus. |
| 810 | 2210054 | The amyloid consists of a 37-amino acid polypeptide referred to as islet amyloid polypeptide (IAPP). |
| 811 | 2210054 | Structure of cat islet amyloid polypeptide and identification of amino acid residues of potential significance for islet amyloid formation. |
| 812 | 2210054 | Cats and humans, unlike most rodent species, develop amyloid in the islets of Langerhans in conjunction with non-insulin-dependent diabetes mellitus. |
| 813 | 2210054 | The amyloid consists of a 37-amino acid polypeptide referred to as islet amyloid polypeptide (IAPP). |
| 814 | 2212934 | Islet amyloid polypeptide-like immunoreactivity (amylin) in rats treated with dexamethasone and streptozotocin. |
| 815 | 2212934 | Islet amyloid polypeptide (IAPP) is a 37 amino acid peptide present in pancreatic beta-cells. |
| 816 | 2212934 | Islet amyloid polypeptide-like immunoreactivity (amylin) in rats treated with dexamethasone and streptozotocin. |
| 817 | 2212934 | Islet amyloid polypeptide (IAPP) is a 37 amino acid peptide present in pancreatic beta-cells. |
| 818 | 2223885 | Islet amyloid polypeptide: structure and upstream sequences of the IAPP gene in rat and man. |
| 819 | 2223885 | Islet amyloid polypeptide (IAPP) or amylin is a pancreatic islet hormone which was first found in amyloid in insulinomas and in pancreases of patients with type 2 diabetes. |
| 820 | 2223885 | Islet amyloid polypeptide: structure and upstream sequences of the IAPP gene in rat and man. |
| 821 | 2223885 | Islet amyloid polypeptide (IAPP) or amylin is a pancreatic islet hormone which was first found in amyloid in insulinomas and in pancreases of patients with type 2 diabetes. |
| 822 | 2226108 | Lowering fasting blood glucose to normal with a basal insulin supplement reduces endogenous insulin production, and this may be advantageous if accompanying production of islet amyloid polypeptide and islet amyloid formation are also reduced. |
| 823 | 2226190 | [Amylin, islet amyloid and diabetes mellitus type II]. |
| 824 | 2227135 | During hyperinsulinemic glucose-clamp studies, intravenous infusion of calcitonin gene-related peptide (CGRP) in rats antagonized the ability of insulin to stimulate peripheral glucose disposal by 52% (196 +/- 7.2 vs. 105 +/- 10.5 mumol.kg-1.min-1, P less than 0.05) and to inhibit hepatic glucose output by 54% (P less than 0.01). |
| 825 | 2227135 | CGRP also inhibited the in vitro effects of insulin to stimulate hexose uptake in cultured BC3H1 myocytes at all insulin concentrations studied. |
| 826 | 2227135 | Amylin is a peptide isolated from amyloid deposits in pancreatic islets of type II (non-insulin-dependent) diabetic subjects, is present in normal beta-cells, and bears a striking homology to CGRP. |
| 827 | 2227135 | Therefore, amylin and CGRP can cause insulin resistance in vivo and may be implicated in insulin-resistant states such as type II diabetes mellitus. |
| 828 | 2251644 | Islet amyloid and type 2 (non-insulin-dependent) diabetes. |
| 829 | 2258001 | Islet amyloid polypeptide (amylin): no evidence of an abnormal precursor sequence in 25 type 2 (non-insulin-dependent) diabetic patients. |
| 830 | 2258001 | Islet amyloid polypeptide is the major protein component of the islet amyloid of patients with Type 2 (non-insulin-dependent) diabetes mellitus. |
| 831 | 2258001 | Since the synthesis of a structurally abnormal or mutant protein may contribute to the formation of amyloid deposits, we have examined the possibility that a mutant form of islet amyloid polypeptide or its precursor contributes to the formation of islet amyloid in Type 2 diabetic patients. |
| 832 | 2258001 | We have sequenced the islet amyloid polypeptide precursor coding regions of the gene of 25 patients with Type 2 diabetes. |
| 833 | 2258001 | Genomic DNA fragments corresponding to exon 2 and 3 of the islet amyloid polypeptide gene were amplified from patients' peripheral blood leucocyte DNAs using the polymerase chain reaction and specific oligonucleotide primer sets, and then directly sequenced. |
| 834 | 2258001 | The nucleotide sequences of the amplified regions of both alleles of the islet amyloid polypeptide gene of these 25 patients were identical to one another and to the sequence of an islet amyloid polypeptide allele isolated from a human fetal liver genomic library. |
| 835 | 2258001 | These findings suggest that a primary structural abnormality of islet amyloid polypeptide or its precursor is unlikely to play a significant role in the formation of islet amyloid in Type 2 diabetic patients. |
| 836 | 2258001 | Islet amyloid polypeptide (amylin): no evidence of an abnormal precursor sequence in 25 type 2 (non-insulin-dependent) diabetic patients. |
| 837 | 2258001 | Islet amyloid polypeptide is the major protein component of the islet amyloid of patients with Type 2 (non-insulin-dependent) diabetes mellitus. |
| 838 | 2258001 | Since the synthesis of a structurally abnormal or mutant protein may contribute to the formation of amyloid deposits, we have examined the possibility that a mutant form of islet amyloid polypeptide or its precursor contributes to the formation of islet amyloid in Type 2 diabetic patients. |
| 839 | 2258001 | We have sequenced the islet amyloid polypeptide precursor coding regions of the gene of 25 patients with Type 2 diabetes. |
| 840 | 2258001 | Genomic DNA fragments corresponding to exon 2 and 3 of the islet amyloid polypeptide gene were amplified from patients' peripheral blood leucocyte DNAs using the polymerase chain reaction and specific oligonucleotide primer sets, and then directly sequenced. |
| 841 | 2258001 | The nucleotide sequences of the amplified regions of both alleles of the islet amyloid polypeptide gene of these 25 patients were identical to one another and to the sequence of an islet amyloid polypeptide allele isolated from a human fetal liver genomic library. |
| 842 | 2258001 | These findings suggest that a primary structural abnormality of islet amyloid polypeptide or its precursor is unlikely to play a significant role in the formation of islet amyloid in Type 2 diabetic patients. |
| 843 | 2258001 | Islet amyloid polypeptide (amylin): no evidence of an abnormal precursor sequence in 25 type 2 (non-insulin-dependent) diabetic patients. |
| 844 | 2258001 | Islet amyloid polypeptide is the major protein component of the islet amyloid of patients with Type 2 (non-insulin-dependent) diabetes mellitus. |
| 845 | 2258001 | Since the synthesis of a structurally abnormal or mutant protein may contribute to the formation of amyloid deposits, we have examined the possibility that a mutant form of islet amyloid polypeptide or its precursor contributes to the formation of islet amyloid in Type 2 diabetic patients. |
| 846 | 2258001 | We have sequenced the islet amyloid polypeptide precursor coding regions of the gene of 25 patients with Type 2 diabetes. |
| 847 | 2258001 | Genomic DNA fragments corresponding to exon 2 and 3 of the islet amyloid polypeptide gene were amplified from patients' peripheral blood leucocyte DNAs using the polymerase chain reaction and specific oligonucleotide primer sets, and then directly sequenced. |
| 848 | 2258001 | The nucleotide sequences of the amplified regions of both alleles of the islet amyloid polypeptide gene of these 25 patients were identical to one another and to the sequence of an islet amyloid polypeptide allele isolated from a human fetal liver genomic library. |
| 849 | 2258001 | These findings suggest that a primary structural abnormality of islet amyloid polypeptide or its precursor is unlikely to play a significant role in the formation of islet amyloid in Type 2 diabetic patients. |
| 850 | 2258001 | Islet amyloid polypeptide (amylin): no evidence of an abnormal precursor sequence in 25 type 2 (non-insulin-dependent) diabetic patients. |
| 851 | 2258001 | Islet amyloid polypeptide is the major protein component of the islet amyloid of patients with Type 2 (non-insulin-dependent) diabetes mellitus. |
| 852 | 2258001 | Since the synthesis of a structurally abnormal or mutant protein may contribute to the formation of amyloid deposits, we have examined the possibility that a mutant form of islet amyloid polypeptide or its precursor contributes to the formation of islet amyloid in Type 2 diabetic patients. |
| 853 | 2258001 | We have sequenced the islet amyloid polypeptide precursor coding regions of the gene of 25 patients with Type 2 diabetes. |
| 854 | 2258001 | Genomic DNA fragments corresponding to exon 2 and 3 of the islet amyloid polypeptide gene were amplified from patients' peripheral blood leucocyte DNAs using the polymerase chain reaction and specific oligonucleotide primer sets, and then directly sequenced. |
| 855 | 2258001 | The nucleotide sequences of the amplified regions of both alleles of the islet amyloid polypeptide gene of these 25 patients were identical to one another and to the sequence of an islet amyloid polypeptide allele isolated from a human fetal liver genomic library. |
| 856 | 2258001 | These findings suggest that a primary structural abnormality of islet amyloid polypeptide or its precursor is unlikely to play a significant role in the formation of islet amyloid in Type 2 diabetic patients. |
| 857 | 2258001 | Islet amyloid polypeptide (amylin): no evidence of an abnormal precursor sequence in 25 type 2 (non-insulin-dependent) diabetic patients. |
| 858 | 2258001 | Islet amyloid polypeptide is the major protein component of the islet amyloid of patients with Type 2 (non-insulin-dependent) diabetes mellitus. |
| 859 | 2258001 | Since the synthesis of a structurally abnormal or mutant protein may contribute to the formation of amyloid deposits, we have examined the possibility that a mutant form of islet amyloid polypeptide or its precursor contributes to the formation of islet amyloid in Type 2 diabetic patients. |
| 860 | 2258001 | We have sequenced the islet amyloid polypeptide precursor coding regions of the gene of 25 patients with Type 2 diabetes. |
| 861 | 2258001 | Genomic DNA fragments corresponding to exon 2 and 3 of the islet amyloid polypeptide gene were amplified from patients' peripheral blood leucocyte DNAs using the polymerase chain reaction and specific oligonucleotide primer sets, and then directly sequenced. |
| 862 | 2258001 | The nucleotide sequences of the amplified regions of both alleles of the islet amyloid polypeptide gene of these 25 patients were identical to one another and to the sequence of an islet amyloid polypeptide allele isolated from a human fetal liver genomic library. |
| 863 | 2258001 | These findings suggest that a primary structural abnormality of islet amyloid polypeptide or its precursor is unlikely to play a significant role in the formation of islet amyloid in Type 2 diabetic patients. |
| 864 | 2258001 | Islet amyloid polypeptide (amylin): no evidence of an abnormal precursor sequence in 25 type 2 (non-insulin-dependent) diabetic patients. |
| 865 | 2258001 | Islet amyloid polypeptide is the major protein component of the islet amyloid of patients with Type 2 (non-insulin-dependent) diabetes mellitus. |
| 866 | 2258001 | Since the synthesis of a structurally abnormal or mutant protein may contribute to the formation of amyloid deposits, we have examined the possibility that a mutant form of islet amyloid polypeptide or its precursor contributes to the formation of islet amyloid in Type 2 diabetic patients. |
| 867 | 2258001 | We have sequenced the islet amyloid polypeptide precursor coding regions of the gene of 25 patients with Type 2 diabetes. |
| 868 | 2258001 | Genomic DNA fragments corresponding to exon 2 and 3 of the islet amyloid polypeptide gene were amplified from patients' peripheral blood leucocyte DNAs using the polymerase chain reaction and specific oligonucleotide primer sets, and then directly sequenced. |
| 869 | 2258001 | The nucleotide sequences of the amplified regions of both alleles of the islet amyloid polypeptide gene of these 25 patients were identical to one another and to the sequence of an islet amyloid polypeptide allele isolated from a human fetal liver genomic library. |
| 870 | 2258001 | These findings suggest that a primary structural abnormality of islet amyloid polypeptide or its precursor is unlikely to play a significant role in the formation of islet amyloid in Type 2 diabetic patients. |
| 871 | 2258001 | Islet amyloid polypeptide (amylin): no evidence of an abnormal precursor sequence in 25 type 2 (non-insulin-dependent) diabetic patients. |
| 872 | 2258001 | Islet amyloid polypeptide is the major protein component of the islet amyloid of patients with Type 2 (non-insulin-dependent) diabetes mellitus. |
| 873 | 2258001 | Since the synthesis of a structurally abnormal or mutant protein may contribute to the formation of amyloid deposits, we have examined the possibility that a mutant form of islet amyloid polypeptide or its precursor contributes to the formation of islet amyloid in Type 2 diabetic patients. |
| 874 | 2258001 | We have sequenced the islet amyloid polypeptide precursor coding regions of the gene of 25 patients with Type 2 diabetes. |
| 875 | 2258001 | Genomic DNA fragments corresponding to exon 2 and 3 of the islet amyloid polypeptide gene were amplified from patients' peripheral blood leucocyte DNAs using the polymerase chain reaction and specific oligonucleotide primer sets, and then directly sequenced. |
| 876 | 2258001 | The nucleotide sequences of the amplified regions of both alleles of the islet amyloid polypeptide gene of these 25 patients were identical to one another and to the sequence of an islet amyloid polypeptide allele isolated from a human fetal liver genomic library. |
| 877 | 2258001 | These findings suggest that a primary structural abnormality of islet amyloid polypeptide or its precursor is unlikely to play a significant role in the formation of islet amyloid in Type 2 diabetic patients. |
| 878 | 2261856 | Amylin, or islet amyloid polypeptide, is a 37-amino acid peptide isolated from pancreatic islet amyloid of patients with non-insulin-dependent diabetes mellitus (NIDDM). |
| 879 | 2293024 | Cloning of complementary DNAs encoding islet amyloid polypeptide, insulin, and glucagon precursors from a New World rodent, the degu, Octodon degus. |
| 880 | 2293024 | To help clarify these problems we have cloned cDNAs encoding islet amyloid polypeptide (IAPP), insulin, and glucagon precursors from this species. |
| 881 | 2293024 | Cloning of complementary DNAs encoding islet amyloid polypeptide, insulin, and glucagon precursors from a New World rodent, the degu, Octodon degus. |
| 882 | 2293024 | To help clarify these problems we have cloned cDNAs encoding islet amyloid polypeptide (IAPP), insulin, and glucagon precursors from this species. |
| 883 | 2316620 | Amylin amide, a 37-amino acid peptide that is a major component of amyloid deposits in the diabetic pancreas, possesses vasodilator activity. |
| 884 | 2328845 | Failure to establish islet amyloid polypeptide (amylin) as a circulating beta cell inhibiting hormone in man. |
| 885 | 2328845 | The presence of islet amyloid polypeptide in amyloid within pancreatic islet cells in Type 2 (non-insulin-dependent) diabetes, and its reported inhibition of glucose uptake by skeletal muscle in vitro, has prompted speculation concerning its role in the pathogenesis of diabetes. |
| 886 | 2328845 | We investigated the effect of infused synthetic amidated human islet amyloid polypeptide (mol. wt. 3904, confirmed by mass spectroscopy) on intravenous glucose tolerance. |
| 887 | 2328845 | Seven healthy, non-obese volunteers (age +/- SD, 27 +/- 4 years) were infused over 50 min with normal (0.9%) saline or islet amyloid polypeptide at 50 pmol.kg-1.min-1. |
| 888 | 2328845 | Circulating concentrations of islet amyloid polypeptide reached at steady state were 1130 +/- 90 pmol/l. |
| 889 | 2328845 | However, islet amyloid polypeptide was found to have no effect on the peak value reached, or the total area under the curve for plasma glucose, insulin or glucagon following intravenous glucose. |
| 890 | 2328845 | This study suggests circulating islet amyloid polypeptide may not be an important influence on intravenous glucose tolerance in man. |
| 891 | 2328845 | Failure to establish islet amyloid polypeptide (amylin) as a circulating beta cell inhibiting hormone in man. |
| 892 | 2328845 | The presence of islet amyloid polypeptide in amyloid within pancreatic islet cells in Type 2 (non-insulin-dependent) diabetes, and its reported inhibition of glucose uptake by skeletal muscle in vitro, has prompted speculation concerning its role in the pathogenesis of diabetes. |
| 893 | 2328845 | We investigated the effect of infused synthetic amidated human islet amyloid polypeptide (mol. wt. 3904, confirmed by mass spectroscopy) on intravenous glucose tolerance. |
| 894 | 2328845 | Seven healthy, non-obese volunteers (age +/- SD, 27 +/- 4 years) were infused over 50 min with normal (0.9%) saline or islet amyloid polypeptide at 50 pmol.kg-1.min-1. |
| 895 | 2328845 | Circulating concentrations of islet amyloid polypeptide reached at steady state were 1130 +/- 90 pmol/l. |
| 896 | 2328845 | However, islet amyloid polypeptide was found to have no effect on the peak value reached, or the total area under the curve for plasma glucose, insulin or glucagon following intravenous glucose. |
| 897 | 2328845 | This study suggests circulating islet amyloid polypeptide may not be an important influence on intravenous glucose tolerance in man. |
| 898 | 2328845 | Failure to establish islet amyloid polypeptide (amylin) as a circulating beta cell inhibiting hormone in man. |
| 899 | 2328845 | The presence of islet amyloid polypeptide in amyloid within pancreatic islet cells in Type 2 (non-insulin-dependent) diabetes, and its reported inhibition of glucose uptake by skeletal muscle in vitro, has prompted speculation concerning its role in the pathogenesis of diabetes. |
| 900 | 2328845 | We investigated the effect of infused synthetic amidated human islet amyloid polypeptide (mol. wt. 3904, confirmed by mass spectroscopy) on intravenous glucose tolerance. |
| 901 | 2328845 | Seven healthy, non-obese volunteers (age +/- SD, 27 +/- 4 years) were infused over 50 min with normal (0.9%) saline or islet amyloid polypeptide at 50 pmol.kg-1.min-1. |
| 902 | 2328845 | Circulating concentrations of islet amyloid polypeptide reached at steady state were 1130 +/- 90 pmol/l. |
| 903 | 2328845 | However, islet amyloid polypeptide was found to have no effect on the peak value reached, or the total area under the curve for plasma glucose, insulin or glucagon following intravenous glucose. |
| 904 | 2328845 | This study suggests circulating islet amyloid polypeptide may not be an important influence on intravenous glucose tolerance in man. |
| 905 | 2328845 | Failure to establish islet amyloid polypeptide (amylin) as a circulating beta cell inhibiting hormone in man. |
| 906 | 2328845 | The presence of islet amyloid polypeptide in amyloid within pancreatic islet cells in Type 2 (non-insulin-dependent) diabetes, and its reported inhibition of glucose uptake by skeletal muscle in vitro, has prompted speculation concerning its role in the pathogenesis of diabetes. |
| 907 | 2328845 | We investigated the effect of infused synthetic amidated human islet amyloid polypeptide (mol. wt. 3904, confirmed by mass spectroscopy) on intravenous glucose tolerance. |
| 908 | 2328845 | Seven healthy, non-obese volunteers (age +/- SD, 27 +/- 4 years) were infused over 50 min with normal (0.9%) saline or islet amyloid polypeptide at 50 pmol.kg-1.min-1. |
| 909 | 2328845 | Circulating concentrations of islet amyloid polypeptide reached at steady state were 1130 +/- 90 pmol/l. |
| 910 | 2328845 | However, islet amyloid polypeptide was found to have no effect on the peak value reached, or the total area under the curve for plasma glucose, insulin or glucagon following intravenous glucose. |
| 911 | 2328845 | This study suggests circulating islet amyloid polypeptide may not be an important influence on intravenous glucose tolerance in man. |
| 912 | 2328845 | Failure to establish islet amyloid polypeptide (amylin) as a circulating beta cell inhibiting hormone in man. |
| 913 | 2328845 | The presence of islet amyloid polypeptide in amyloid within pancreatic islet cells in Type 2 (non-insulin-dependent) diabetes, and its reported inhibition of glucose uptake by skeletal muscle in vitro, has prompted speculation concerning its role in the pathogenesis of diabetes. |
| 914 | 2328845 | We investigated the effect of infused synthetic amidated human islet amyloid polypeptide (mol. wt. 3904, confirmed by mass spectroscopy) on intravenous glucose tolerance. |
| 915 | 2328845 | Seven healthy, non-obese volunteers (age +/- SD, 27 +/- 4 years) were infused over 50 min with normal (0.9%) saline or islet amyloid polypeptide at 50 pmol.kg-1.min-1. |
| 916 | 2328845 | Circulating concentrations of islet amyloid polypeptide reached at steady state were 1130 +/- 90 pmol/l. |
| 917 | 2328845 | However, islet amyloid polypeptide was found to have no effect on the peak value reached, or the total area under the curve for plasma glucose, insulin or glucagon following intravenous glucose. |
| 918 | 2328845 | This study suggests circulating islet amyloid polypeptide may not be an important influence on intravenous glucose tolerance in man. |
| 919 | 2328845 | Failure to establish islet amyloid polypeptide (amylin) as a circulating beta cell inhibiting hormone in man. |
| 920 | 2328845 | The presence of islet amyloid polypeptide in amyloid within pancreatic islet cells in Type 2 (non-insulin-dependent) diabetes, and its reported inhibition of glucose uptake by skeletal muscle in vitro, has prompted speculation concerning its role in the pathogenesis of diabetes. |
| 921 | 2328845 | We investigated the effect of infused synthetic amidated human islet amyloid polypeptide (mol. wt. 3904, confirmed by mass spectroscopy) on intravenous glucose tolerance. |
| 922 | 2328845 | Seven healthy, non-obese volunteers (age +/- SD, 27 +/- 4 years) were infused over 50 min with normal (0.9%) saline or islet amyloid polypeptide at 50 pmol.kg-1.min-1. |
| 923 | 2328845 | Circulating concentrations of islet amyloid polypeptide reached at steady state were 1130 +/- 90 pmol/l. |
| 924 | 2328845 | However, islet amyloid polypeptide was found to have no effect on the peak value reached, or the total area under the curve for plasma glucose, insulin or glucagon following intravenous glucose. |
| 925 | 2328845 | This study suggests circulating islet amyloid polypeptide may not be an important influence on intravenous glucose tolerance in man. |
| 926 | 2328845 | Failure to establish islet amyloid polypeptide (amylin) as a circulating beta cell inhibiting hormone in man. |
| 927 | 2328845 | The presence of islet amyloid polypeptide in amyloid within pancreatic islet cells in Type 2 (non-insulin-dependent) diabetes, and its reported inhibition of glucose uptake by skeletal muscle in vitro, has prompted speculation concerning its role in the pathogenesis of diabetes. |
| 928 | 2328845 | We investigated the effect of infused synthetic amidated human islet amyloid polypeptide (mol. wt. 3904, confirmed by mass spectroscopy) on intravenous glucose tolerance. |
| 929 | 2328845 | Seven healthy, non-obese volunteers (age +/- SD, 27 +/- 4 years) were infused over 50 min with normal (0.9%) saline or islet amyloid polypeptide at 50 pmol.kg-1.min-1. |
| 930 | 2328845 | Circulating concentrations of islet amyloid polypeptide reached at steady state were 1130 +/- 90 pmol/l. |
| 931 | 2328845 | However, islet amyloid polypeptide was found to have no effect on the peak value reached, or the total area under the curve for plasma glucose, insulin or glucagon following intravenous glucose. |
| 932 | 2328845 | This study suggests circulating islet amyloid polypeptide may not be an important influence on intravenous glucose tolerance in man. |
| 933 | 2409805 | Ganglioneuronal amyloid had staining characteristics identical to those previously reported for islet amyloid, including 1) congophilia, 2) resistance to oxidation by KMnO4, 3) immunoreactivity (PAP technique) with antiserum to a B-chain-rich insulin fraction, and 4) no reactivity with antisera to insulin, glucagon, or somatostatin. |
| 934 | 2409805 | Nonneuronal cells with insulin, glucagon, and somatostatin immunoreactivity were seen in many pancreatic ganglia and nerves; and in a few instances, B cells were found near ganglioneuronal amyloid deposits. |
| 935 | 2409805 | The premise that these ganglioneuronal amyloid deposits (like islet amyloid) are insulin-related is supported by their immunoreactivity with antiserum to B-chain-rich insulin and the demonstration of B cells in pancreatic ganglia and nerves. |
| 936 | 2409805 | Ganglioneuronal amyloid had staining characteristics identical to those previously reported for islet amyloid, including 1) congophilia, 2) resistance to oxidation by KMnO4, 3) immunoreactivity (PAP technique) with antiserum to a B-chain-rich insulin fraction, and 4) no reactivity with antisera to insulin, glucagon, or somatostatin. |
| 937 | 2409805 | Nonneuronal cells with insulin, glucagon, and somatostatin immunoreactivity were seen in many pancreatic ganglia and nerves; and in a few instances, B cells were found near ganglioneuronal amyloid deposits. |
| 938 | 2409805 | The premise that these ganglioneuronal amyloid deposits (like islet amyloid) are insulin-related is supported by their immunoreactivity with antiserum to B-chain-rich insulin and the demonstration of B cells in pancreatic ganglia and nerves. |
| 939 | 2409805 | Ganglioneuronal amyloid had staining characteristics identical to those previously reported for islet amyloid, including 1) congophilia, 2) resistance to oxidation by KMnO4, 3) immunoreactivity (PAP technique) with antiserum to a B-chain-rich insulin fraction, and 4) no reactivity with antisera to insulin, glucagon, or somatostatin. |
| 940 | 2409805 | Nonneuronal cells with insulin, glucagon, and somatostatin immunoreactivity were seen in many pancreatic ganglia and nerves; and in a few instances, B cells were found near ganglioneuronal amyloid deposits. |
| 941 | 2409805 | The premise that these ganglioneuronal amyloid deposits (like islet amyloid) are insulin-related is supported by their immunoreactivity with antiserum to B-chain-rich insulin and the demonstration of B cells in pancreatic ganglia and nerves. |
| 942 | 2441214 | A novel peptide, 37 aminoacids long, termed diabetes-associated peptide (DAP), has been identified in amyloid-containing pancreatic extracts from 3 type-2 diabetic patients but not in extracts from 6 non-diabetic subjects. |
| 943 | 2441214 | DAP has major homology with calcitonin-gene related peptide (CGRP) and the islet amyloid of all 22 diabetics showed CGRP immunoreactivity. |
| 944 | 2441214 | The immunoreactivity was inhibited by preabsorption of three different CGRP antisera either with CGRP carboxyterminal peptide 28-37 or with extracted DAP. |
| 945 | 2441214 | Both diabetic and non-diabetic subjects had CGRP/DAP immunoreactivity in islet B-cells. |
| 946 | 2441214 | These results suggest that islet amyloid contains DAP, which may originate from B-cells. |
| 947 | 2441214 | A novel peptide, 37 aminoacids long, termed diabetes-associated peptide (DAP), has been identified in amyloid-containing pancreatic extracts from 3 type-2 diabetic patients but not in extracts from 6 non-diabetic subjects. |
| 948 | 2441214 | DAP has major homology with calcitonin-gene related peptide (CGRP) and the islet amyloid of all 22 diabetics showed CGRP immunoreactivity. |
| 949 | 2441214 | The immunoreactivity was inhibited by preabsorption of three different CGRP antisera either with CGRP carboxyterminal peptide 28-37 or with extracted DAP. |
| 950 | 2441214 | Both diabetic and non-diabetic subjects had CGRP/DAP immunoreactivity in islet B-cells. |
| 951 | 2441214 | These results suggest that islet amyloid contains DAP, which may originate from B-cells. |
| 952 | 2441214 | A novel peptide, 37 aminoacids long, termed diabetes-associated peptide (DAP), has been identified in amyloid-containing pancreatic extracts from 3 type-2 diabetic patients but not in extracts from 6 non-diabetic subjects. |
| 953 | 2441214 | DAP has major homology with calcitonin-gene related peptide (CGRP) and the islet amyloid of all 22 diabetics showed CGRP immunoreactivity. |
| 954 | 2441214 | The immunoreactivity was inhibited by preabsorption of three different CGRP antisera either with CGRP carboxyterminal peptide 28-37 or with extracted DAP. |
| 955 | 2441214 | Both diabetic and non-diabetic subjects had CGRP/DAP immunoreactivity in islet B-cells. |
| 956 | 2441214 | These results suggest that islet amyloid contains DAP, which may originate from B-cells. |
| 957 | 2458216 | Serum levels of six acute phase proteins (APP)--C-reactive protein (CRP), serum amyloid A (SAA), alpha 1-antitrypsin, haptoglobin and complement fractions C3 and C4--were serially studied in 24 patients with poorly controlled diabetes mellitus, ten of whom had unequivocal evidence of an underlying infection. |
| 958 | 2458216 | No correlation between the presence of infection, and fever, leukocytosis, a raised erythrocyte sedimentation rate, or serum levels of alpha 1-antitrypsin, haptoglobin or complement was apparent in these patients. |
| 959 | 2458216 | However, serum CRP and SAA were initially increased 10-100 times above normal in diabetic patients with an underlying infection (P less than 0.01); during the following week circulating levels of CRP and SAA decreased steadily in response to the infection being brought under control. |
| 960 | 2458216 | We conclude that serial measurement of CRP and/or SAA is a sensitive, albeit non-specific, parameter to detect and monitor the activity of infection in patients with diabetes. |
| 961 | 2612759 | Altered islet amyloid polypeptide (amylin) gene expression in rat models of diabetes. |
| 962 | 2612759 | The response of the islet amyloid polypeptide gene to chronic dexamethasone treatment in adult rats was investigated. |
| 963 | 2612759 | When pancreatic mRNA was analysed, a 16-fold elevation in islet amyloid polypeptide mRNA was observed with only a four-fold increase in insulin mRNA levels. |
| 964 | 2612759 | Pancreatic islet amyloid polypeptide and insulin mRNA levels were also determined 12 days after streptozotocin treatment. |
| 965 | 2612759 | In these rats, which were not severely diabetic, the reduction in islet amyloid polypeptide mRNA levels was sixfold less than the reduction in insulin mRNA levels. |
| 966 | 2612759 | In both these models of diabetes the ratio of islet amyloid polypeptide to insulin mRNA levels was raised. |
| 967 | 2612759 | This would not be expected if the physiological role of islet amyloid polypeptide is as a simple hyperglycaemic agent opposing insulin action or release. |
| 968 | 2612759 | Altered islet amyloid polypeptide (amylin) gene expression in rat models of diabetes. |
| 969 | 2612759 | The response of the islet amyloid polypeptide gene to chronic dexamethasone treatment in adult rats was investigated. |
| 970 | 2612759 | When pancreatic mRNA was analysed, a 16-fold elevation in islet amyloid polypeptide mRNA was observed with only a four-fold increase in insulin mRNA levels. |
| 971 | 2612759 | Pancreatic islet amyloid polypeptide and insulin mRNA levels were also determined 12 days after streptozotocin treatment. |
| 972 | 2612759 | In these rats, which were not severely diabetic, the reduction in islet amyloid polypeptide mRNA levels was sixfold less than the reduction in insulin mRNA levels. |
| 973 | 2612759 | In both these models of diabetes the ratio of islet amyloid polypeptide to insulin mRNA levels was raised. |
| 974 | 2612759 | This would not be expected if the physiological role of islet amyloid polypeptide is as a simple hyperglycaemic agent opposing insulin action or release. |
| 975 | 2612759 | Altered islet amyloid polypeptide (amylin) gene expression in rat models of diabetes. |
| 976 | 2612759 | The response of the islet amyloid polypeptide gene to chronic dexamethasone treatment in adult rats was investigated. |
| 977 | 2612759 | When pancreatic mRNA was analysed, a 16-fold elevation in islet amyloid polypeptide mRNA was observed with only a four-fold increase in insulin mRNA levels. |
| 978 | 2612759 | Pancreatic islet amyloid polypeptide and insulin mRNA levels were also determined 12 days after streptozotocin treatment. |
| 979 | 2612759 | In these rats, which were not severely diabetic, the reduction in islet amyloid polypeptide mRNA levels was sixfold less than the reduction in insulin mRNA levels. |
| 980 | 2612759 | In both these models of diabetes the ratio of islet amyloid polypeptide to insulin mRNA levels was raised. |
| 981 | 2612759 | This would not be expected if the physiological role of islet amyloid polypeptide is as a simple hyperglycaemic agent opposing insulin action or release. |
| 982 | 2612759 | Altered islet amyloid polypeptide (amylin) gene expression in rat models of diabetes. |
| 983 | 2612759 | The response of the islet amyloid polypeptide gene to chronic dexamethasone treatment in adult rats was investigated. |
| 984 | 2612759 | When pancreatic mRNA was analysed, a 16-fold elevation in islet amyloid polypeptide mRNA was observed with only a four-fold increase in insulin mRNA levels. |
| 985 | 2612759 | Pancreatic islet amyloid polypeptide and insulin mRNA levels were also determined 12 days after streptozotocin treatment. |
| 986 | 2612759 | In these rats, which were not severely diabetic, the reduction in islet amyloid polypeptide mRNA levels was sixfold less than the reduction in insulin mRNA levels. |
| 987 | 2612759 | In both these models of diabetes the ratio of islet amyloid polypeptide to insulin mRNA levels was raised. |
| 988 | 2612759 | This would not be expected if the physiological role of islet amyloid polypeptide is as a simple hyperglycaemic agent opposing insulin action or release. |
| 989 | 2612759 | Altered islet amyloid polypeptide (amylin) gene expression in rat models of diabetes. |
| 990 | 2612759 | The response of the islet amyloid polypeptide gene to chronic dexamethasone treatment in adult rats was investigated. |
| 991 | 2612759 | When pancreatic mRNA was analysed, a 16-fold elevation in islet amyloid polypeptide mRNA was observed with only a four-fold increase in insulin mRNA levels. |
| 992 | 2612759 | Pancreatic islet amyloid polypeptide and insulin mRNA levels were also determined 12 days after streptozotocin treatment. |
| 993 | 2612759 | In these rats, which were not severely diabetic, the reduction in islet amyloid polypeptide mRNA levels was sixfold less than the reduction in insulin mRNA levels. |
| 994 | 2612759 | In both these models of diabetes the ratio of islet amyloid polypeptide to insulin mRNA levels was raised. |
| 995 | 2612759 | This would not be expected if the physiological role of islet amyloid polypeptide is as a simple hyperglycaemic agent opposing insulin action or release. |
| 996 | 2612759 | Altered islet amyloid polypeptide (amylin) gene expression in rat models of diabetes. |
| 997 | 2612759 | The response of the islet amyloid polypeptide gene to chronic dexamethasone treatment in adult rats was investigated. |
| 998 | 2612759 | When pancreatic mRNA was analysed, a 16-fold elevation in islet amyloid polypeptide mRNA was observed with only a four-fold increase in insulin mRNA levels. |
| 999 | 2612759 | Pancreatic islet amyloid polypeptide and insulin mRNA levels were also determined 12 days after streptozotocin treatment. |
| 1000 | 2612759 | In these rats, which were not severely diabetic, the reduction in islet amyloid polypeptide mRNA levels was sixfold less than the reduction in insulin mRNA levels. |
| 1001 | 2612759 | In both these models of diabetes the ratio of islet amyloid polypeptide to insulin mRNA levels was raised. |
| 1002 | 2612759 | This would not be expected if the physiological role of islet amyloid polypeptide is as a simple hyperglycaemic agent opposing insulin action or release. |
| 1003 | 2612759 | Altered islet amyloid polypeptide (amylin) gene expression in rat models of diabetes. |
| 1004 | 2612759 | The response of the islet amyloid polypeptide gene to chronic dexamethasone treatment in adult rats was investigated. |
| 1005 | 2612759 | When pancreatic mRNA was analysed, a 16-fold elevation in islet amyloid polypeptide mRNA was observed with only a four-fold increase in insulin mRNA levels. |
| 1006 | 2612759 | Pancreatic islet amyloid polypeptide and insulin mRNA levels were also determined 12 days after streptozotocin treatment. |
| 1007 | 2612759 | In these rats, which were not severely diabetic, the reduction in islet amyloid polypeptide mRNA levels was sixfold less than the reduction in insulin mRNA levels. |
| 1008 | 2612759 | In both these models of diabetes the ratio of islet amyloid polypeptide to insulin mRNA levels was raised. |
| 1009 | 2612759 | This would not be expected if the physiological role of islet amyloid polypeptide is as a simple hyperglycaemic agent opposing insulin action or release. |
| 1010 | 2639135 | Recently, islet- or insulinoma-amyloid polypeptide (IAPP) was isolated as a major constituent of amyloid present in human insulinoma and in pancreatic islet amyloid in noninsulin-dependent diabetes mellitus. |
| 1011 | 2639135 | IAPP shows 46% amino acid sequence homology with human CGRP-II. |
| 1012 | 2649092 | Antibodies specific for the pancreatic islet amyloid polypeptide associated with type 2 diabetes mellitus. |
| 1013 | 2649092 | Antibodies raised to a lysine solubilized peptide composed of residues 20-29 of the pancreatic islet amyloid polypeptide react selectively and specifically with this polypeptide and with islet amyloid deposits in Type 2 diabetes mellitus. |
| 1014 | 2649092 | These antibodies may prove useful in studies employing radioimmunoassay of body fluids and islet cell cultures in order to define if a pathogenic relationship exists between the islet amyloid polypeptide and Type 2 diabetes mellitus. |
| 1015 | 2649092 | Antibodies specific for the pancreatic islet amyloid polypeptide associated with type 2 diabetes mellitus. |
| 1016 | 2649092 | Antibodies raised to a lysine solubilized peptide composed of residues 20-29 of the pancreatic islet amyloid polypeptide react selectively and specifically with this polypeptide and with islet amyloid deposits in Type 2 diabetes mellitus. |
| 1017 | 2649092 | These antibodies may prove useful in studies employing radioimmunoassay of body fluids and islet cell cultures in order to define if a pathogenic relationship exists between the islet amyloid polypeptide and Type 2 diabetes mellitus. |
| 1018 | 2649092 | Antibodies specific for the pancreatic islet amyloid polypeptide associated with type 2 diabetes mellitus. |
| 1019 | 2649092 | Antibodies raised to a lysine solubilized peptide composed of residues 20-29 of the pancreatic islet amyloid polypeptide react selectively and specifically with this polypeptide and with islet amyloid deposits in Type 2 diabetes mellitus. |
| 1020 | 2649092 | These antibodies may prove useful in studies employing radioimmunoassay of body fluids and islet cell cultures in order to define if a pathogenic relationship exists between the islet amyloid polypeptide and Type 2 diabetes mellitus. |
| 1021 | 2655598 | Islet amyloid polypeptide inhibits glucose-stimulated insulin secretion from isolated rat pancreatic islets. |
| 1022 | 2655598 | Islet amyloid polypeptide has 37 amino acids and is a major component of amyloid deposition in pancreatic islets of patients with type 2 diabetes mellitus. |
| 1023 | 2655598 | To determine whether the peptide is involved in the impaired insulin secretion in this type of diabetes mellitus, we synthesized islet amyloid polypeptide and its fragments and examined its effect on insulin secretion. |
| 1024 | 2655598 | Islet amyloid polypeptide inhibited the glucose-stimulated insulin secretion from isolated rat pancreatic islets, as calcitonin gene-related peptide did, but the fragments failed to inhibit the secretion. |
| 1025 | 2655598 | Thus, we propose that amyloid deposition may be an important factor in the impairment of insulin secretion in type 2 diabetes mellitus. |
| 1026 | 2655598 | Islet amyloid polypeptide inhibits glucose-stimulated insulin secretion from isolated rat pancreatic islets. |
| 1027 | 2655598 | Islet amyloid polypeptide has 37 amino acids and is a major component of amyloid deposition in pancreatic islets of patients with type 2 diabetes mellitus. |
| 1028 | 2655598 | To determine whether the peptide is involved in the impaired insulin secretion in this type of diabetes mellitus, we synthesized islet amyloid polypeptide and its fragments and examined its effect on insulin secretion. |
| 1029 | 2655598 | Islet amyloid polypeptide inhibited the glucose-stimulated insulin secretion from isolated rat pancreatic islets, as calcitonin gene-related peptide did, but the fragments failed to inhibit the secretion. |
| 1030 | 2655598 | Thus, we propose that amyloid deposition may be an important factor in the impairment of insulin secretion in type 2 diabetes mellitus. |
| 1031 | 2655598 | Islet amyloid polypeptide inhibits glucose-stimulated insulin secretion from isolated rat pancreatic islets. |
| 1032 | 2655598 | Islet amyloid polypeptide has 37 amino acids and is a major component of amyloid deposition in pancreatic islets of patients with type 2 diabetes mellitus. |
| 1033 | 2655598 | To determine whether the peptide is involved in the impaired insulin secretion in this type of diabetes mellitus, we synthesized islet amyloid polypeptide and its fragments and examined its effect on insulin secretion. |
| 1034 | 2655598 | Islet amyloid polypeptide inhibited the glucose-stimulated insulin secretion from isolated rat pancreatic islets, as calcitonin gene-related peptide did, but the fragments failed to inhibit the secretion. |
| 1035 | 2655598 | Thus, we propose that amyloid deposition may be an important factor in the impairment of insulin secretion in type 2 diabetes mellitus. |
| 1036 | 2655598 | Islet amyloid polypeptide inhibits glucose-stimulated insulin secretion from isolated rat pancreatic islets. |
| 1037 | 2655598 | Islet amyloid polypeptide has 37 amino acids and is a major component of amyloid deposition in pancreatic islets of patients with type 2 diabetes mellitus. |
| 1038 | 2655598 | To determine whether the peptide is involved in the impaired insulin secretion in this type of diabetes mellitus, we synthesized islet amyloid polypeptide and its fragments and examined its effect on insulin secretion. |
| 1039 | 2655598 | Islet amyloid polypeptide inhibited the glucose-stimulated insulin secretion from isolated rat pancreatic islets, as calcitonin gene-related peptide did, but the fragments failed to inhibit the secretion. |
| 1040 | 2655598 | Thus, we propose that amyloid deposition may be an important factor in the impairment of insulin secretion in type 2 diabetes mellitus. |
| 1041 | 2655598 | Islet amyloid polypeptide inhibits glucose-stimulated insulin secretion from isolated rat pancreatic islets. |
| 1042 | 2655598 | Islet amyloid polypeptide has 37 amino acids and is a major component of amyloid deposition in pancreatic islets of patients with type 2 diabetes mellitus. |
| 1043 | 2655598 | To determine whether the peptide is involved in the impaired insulin secretion in this type of diabetes mellitus, we synthesized islet amyloid polypeptide and its fragments and examined its effect on insulin secretion. |
| 1044 | 2655598 | Islet amyloid polypeptide inhibited the glucose-stimulated insulin secretion from isolated rat pancreatic islets, as calcitonin gene-related peptide did, but the fragments failed to inhibit the secretion. |
| 1045 | 2655598 | Thus, we propose that amyloid deposition may be an important factor in the impairment of insulin secretion in type 2 diabetes mellitus. |
| 1046 | 2659052 | In the eight years that have elapsed since the first implantation of an insulin pump in a human subject, insulin delivered by implantable pump has been shown to improve metabolic control while reducing total and LDL cholesterol, serum amyloid A, and serum anti-insulin antibody titres. |
| 1047 | 2666169 | Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species. |
| 1048 | 2666169 | Amyloid deposits in the islets of Langerhans occur in association with type 2 diabetes mellitus (DM) in humans and cats and consist of a 37-amino-acid polypeptide known as islet amyloid polypeptide (IAPP). |
| 1049 | 2666169 | Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species. |
| 1050 | 2666169 | Amyloid deposits in the islets of Langerhans occur in association with type 2 diabetes mellitus (DM) in humans and cats and consist of a 37-amino-acid polypeptide known as islet amyloid polypeptide (IAPP). |
| 1051 | 2668761 | Islet amyloid, islet-amyloid polypeptide, and diabetes mellitus. |
| 1052 | 2668761 | Although the physiologic function of IAPP and its role in the pathogenesis of Type II diabetes mellitus are just beginning to be unraveled, IAPP may play an important part in the development of this most common form of diabetes mellitus by opposing the action of insulin in peripheral tissues. |
| 1053 | 2668761 | Substantial evidence indicates that the propensity of IAPP to polymerize and form extracellular amyloid deposits in only certain species (e.g., humans, cats, and raccoons) is directly associated with an intrinsically amyloidogenic part of the molecule--i.e., positions 20 through 29 of IAPP. |
| 1054 | 2668761 | Although increased production of IAPP may initially cause insulin resistance, prolonged overproduction of IAPP may ultimately impair insulin secretion by leading to the progressive deposition of insoluble islet amyloid, a finding apparent in most subjects with overt diabetes. |
| 1055 | 2668761 | Islet amyloid, islet-amyloid polypeptide, and diabetes mellitus. |
| 1056 | 2668761 | Although the physiologic function of IAPP and its role in the pathogenesis of Type II diabetes mellitus are just beginning to be unraveled, IAPP may play an important part in the development of this most common form of diabetes mellitus by opposing the action of insulin in peripheral tissues. |
| 1057 | 2668761 | Substantial evidence indicates that the propensity of IAPP to polymerize and form extracellular amyloid deposits in only certain species (e.g., humans, cats, and raccoons) is directly associated with an intrinsically amyloidogenic part of the molecule--i.e., positions 20 through 29 of IAPP. |
| 1058 | 2668761 | Although increased production of IAPP may initially cause insulin resistance, prolonged overproduction of IAPP may ultimately impair insulin secretion by leading to the progressive deposition of insoluble islet amyloid, a finding apparent in most subjects with overt diabetes. |
| 1059 | 2668761 | Islet amyloid, islet-amyloid polypeptide, and diabetes mellitus. |
| 1060 | 2668761 | Although the physiologic function of IAPP and its role in the pathogenesis of Type II diabetes mellitus are just beginning to be unraveled, IAPP may play an important part in the development of this most common form of diabetes mellitus by opposing the action of insulin in peripheral tissues. |
| 1061 | 2668761 | Substantial evidence indicates that the propensity of IAPP to polymerize and form extracellular amyloid deposits in only certain species (e.g., humans, cats, and raccoons) is directly associated with an intrinsically amyloidogenic part of the molecule--i.e., positions 20 through 29 of IAPP. |
| 1062 | 2668761 | Although increased production of IAPP may initially cause insulin resistance, prolonged overproduction of IAPP may ultimately impair insulin secretion by leading to the progressive deposition of insoluble islet amyloid, a finding apparent in most subjects with overt diabetes. |
| 1063 | 2670595 | Islet amyloid polypeptide (IAPP):cDNA cloning and identification of an amyloidogenic region associated with the species-specific occurrence of age-related diabetes mellitus. |
| 1064 | 2670595 | We have cloned and sequenced a human islet amyloid polypeptide (IAPP) cDNA. |
| 1065 | 2670595 | Evolutionary conserved proteolytic processing sites indicate that similar proteases are involved in the maturation of IAPP and CGRP and that the IAPP amyloid polypeptide is identical to the normal proteolytic product of the IAPP precursor. |
| 1066 | 2670595 | Islet amyloid polypeptide (IAPP):cDNA cloning and identification of an amyloidogenic region associated with the species-specific occurrence of age-related diabetes mellitus. |
| 1067 | 2670595 | We have cloned and sequenced a human islet amyloid polypeptide (IAPP) cDNA. |
| 1068 | 2670595 | Evolutionary conserved proteolytic processing sites indicate that similar proteases are involved in the maturation of IAPP and CGRP and that the IAPP amyloid polypeptide is identical to the normal proteolytic product of the IAPP precursor. |
| 1069 | 2670595 | Islet amyloid polypeptide (IAPP):cDNA cloning and identification of an amyloidogenic region associated with the species-specific occurrence of age-related diabetes mellitus. |
| 1070 | 2670595 | We have cloned and sequenced a human islet amyloid polypeptide (IAPP) cDNA. |
| 1071 | 2670595 | Evolutionary conserved proteolytic processing sites indicate that similar proteases are involved in the maturation of IAPP and CGRP and that the IAPP amyloid polypeptide is identical to the normal proteolytic product of the IAPP precursor. |
| 1072 | 2675614 | Impaired glucose tolerance is associated with increased islet amyloid polypeptide (IAPP) immunoreactivity in pancreatic beta cells. |
| 1073 | 2675614 | Adult cats determined by clinical laboratory evaluations to be normal, impaired glucose tolerant, or overtly diabetic were used to explore prospectively the relationships among pancreatic beta cell islet amyloid polypeptide (IAPP) immunoreactivity, islet amyloid (IA) deposition, and diabetogenesis. |
| 1074 | 2675614 | Impaired glucose tolerance is associated with increased islet amyloid polypeptide (IAPP) immunoreactivity in pancreatic beta cells. |
| 1075 | 2675614 | Adult cats determined by clinical laboratory evaluations to be normal, impaired glucose tolerant, or overtly diabetic were used to explore prospectively the relationships among pancreatic beta cell islet amyloid polypeptide (IAPP) immunoreactivity, islet amyloid (IA) deposition, and diabetogenesis. |
| 1076 | 2679554 | Establishment of radioimmunoassay for human islet amyloid polypeptide and its tissue content and plasma concentration. |
| 1077 | 2679554 | Using a synthetic C- terminal tetradecapeptide of human islet amyloid polypeptide (IAPP), we prepared an antiserum for human IAPP [24-37] and established a highly sensitive radioimmunoassay (RIA) for human IAPP. |
| 1078 | 2679554 | Establishment of radioimmunoassay for human islet amyloid polypeptide and its tissue content and plasma concentration. |
| 1079 | 2679554 | Using a synthetic C- terminal tetradecapeptide of human islet amyloid polypeptide (IAPP), we prepared an antiserum for human IAPP [24-37] and established a highly sensitive radioimmunoassay (RIA) for human IAPP. |
| 1080 | 2689229 | Secretion of islet amyloid polypeptide in response to glucose. |
| 1081 | 2689229 | The content of islet amyloid polypeptide (IAPP) in isolated rat pancreatic islets was determined by a radioimmunoassay. |
| 1082 | 2689229 | Secretion of islet amyloid polypeptide in response to glucose. |
| 1083 | 2689229 | The content of islet amyloid polypeptide (IAPP) in isolated rat pancreatic islets was determined by a radioimmunoassay. |
| 1084 | 2690958 | Amylin and the amylin gene: structure, function and relationship to islet amyloid and to diabetes mellitus. |
| 1085 | 2690958 | Amylin, the major peptide component of the islet amyloid commonly found in the pancreases of patients with type 2 (non-insulin-dependent) diabetes mellitus (NIDDM), is a recently discovered islet polypeptide. |
| 1086 | 2690958 | Amylin is probably generated by proteolytic processing similar to that for proinsulin and other islet prohormones. |
| 1087 | 2690958 | Amylin is a potent modulator of glycogen synthesis and glucose uptake in skeletal muscle, and is capable of inducing an insulin-resistant state in this tissue in vitro, and perhaps also in the liver in vivo. |
| 1088 | 2690958 | Following the beta-cell destruction which occurs in type 1 (insulin-dependent) diabetes mellitus (IDDM), it is probable that amylin secretion disappears in addition to that of insulin. |
| 1089 | 2690958 | As patients with insulin-treated IDDM frequently experience problems with hypoglycaemia, and as amylin acts to modulate the action of insulin in various tissues, it is possible that amylin deficiency may contribute to morbidity in insulin-treated IDDM, perhaps through the loss of a natural damping mechanism which guards against hypoglycaemia under conditions of normal physiology. |
| 1090 | 2690958 | Amylin and the amylin gene: structure, function and relationship to islet amyloid and to diabetes mellitus. |
| 1091 | 2690958 | Amylin, the major peptide component of the islet amyloid commonly found in the pancreases of patients with type 2 (non-insulin-dependent) diabetes mellitus (NIDDM), is a recently discovered islet polypeptide. |
| 1092 | 2690958 | Amylin is probably generated by proteolytic processing similar to that for proinsulin and other islet prohormones. |
| 1093 | 2690958 | Amylin is a potent modulator of glycogen synthesis and glucose uptake in skeletal muscle, and is capable of inducing an insulin-resistant state in this tissue in vitro, and perhaps also in the liver in vivo. |
| 1094 | 2690958 | Following the beta-cell destruction which occurs in type 1 (insulin-dependent) diabetes mellitus (IDDM), it is probable that amylin secretion disappears in addition to that of insulin. |
| 1095 | 2690958 | As patients with insulin-treated IDDM frequently experience problems with hypoglycaemia, and as amylin acts to modulate the action of insulin in various tissues, it is possible that amylin deficiency may contribute to morbidity in insulin-treated IDDM, perhaps through the loss of a natural damping mechanism which guards against hypoglycaemia under conditions of normal physiology. |
| 1096 | 2691219 | Islet amyloid polypeptide (IAPP) and pro-IAPP immunoreactivity in human islets of Langerhans. |
| 1097 | 2691219 | Islet amyloid polypeptide (IAPP) is a 37-amino-acid putative hormone which is expressed by islet B-cells and most probably is co-released with insulin. |
| 1098 | 2691219 | Islet amyloid polypeptide (IAPP) and pro-IAPP immunoreactivity in human islets of Langerhans. |
| 1099 | 2691219 | Islet amyloid polypeptide (IAPP) is a 37-amino-acid putative hormone which is expressed by islet B-cells and most probably is co-released with insulin. |
| 1100 | 2695369 | This peptide, named islet amyloid polypeptide or amylin, is also present in normal islets. |
| 1101 | 2695369 | Because of its association with two apparently dissimilar disease states, we propose a hypothesis that encompasses the observations related to proinsulin and islet amyloid polypeptide and suggest they are manifestations of the same abnormality. |
| 1102 | 2695369 | We also suggest that in the presence of defective proinsulin processing and insulin release, as occurs in NIDDM, hyperglycemia stimulates amylin biosynthesis so that this peptide is deposited in increased quantities in the islet as amyloid. |
| 1103 | 2695369 | This peptide, named islet amyloid polypeptide or amylin, is also present in normal islets. |
| 1104 | 2695369 | Because of its association with two apparently dissimilar disease states, we propose a hypothesis that encompasses the observations related to proinsulin and islet amyloid polypeptide and suggest they are manifestations of the same abnormality. |
| 1105 | 2695369 | We also suggest that in the presence of defective proinsulin processing and insulin release, as occurs in NIDDM, hyperglycemia stimulates amylin biosynthesis so that this peptide is deposited in increased quantities in the islet as amyloid. |
| 1106 | 2695369 | This peptide, named islet amyloid polypeptide or amylin, is also present in normal islets. |
| 1107 | 2695369 | Because of its association with two apparently dissimilar disease states, we propose a hypothesis that encompasses the observations related to proinsulin and islet amyloid polypeptide and suggest they are manifestations of the same abnormality. |
| 1108 | 2695369 | We also suggest that in the presence of defective proinsulin processing and insulin release, as occurs in NIDDM, hyperglycemia stimulates amylin biosynthesis so that this peptide is deposited in increased quantities in the islet as amyloid. |
| 1109 | 2884060 | Pancreatic islet amyloid and elevated proinsulin secretion in familial maturity-onset diabetes. |
| 1110 | 2884060 | Elevated proinsulin levels in a patient with islet-amyloid is consistent with the hypothesis that amyloid may be derived from abnormal beta-cell secretion. |
| 1111 | 2884060 | Pancreatic islet amyloid and elevated proinsulin secretion in familial maturity-onset diabetes. |
| 1112 | 2884060 | Elevated proinsulin levels in a patient with islet-amyloid is consistent with the hypothesis that amyloid may be derived from abnormal beta-cell secretion. |
| 1113 | 2887903 | Islet amyloid polypeptide. |
| 1114 | 3035556 | We have purified a major protein--insulinoma or islet amyloid polypeptide (IAPP)--from human and cat islet amyloid and from amyloid of a human insulinoma. |
| 1115 | 3050530 | Amylin is a 37-amino-acid peptide which is a major component of islet amyloid and has structural similarity to human calcitonin gene-related peptide-2 (CGRP-2; ref. 8). |
| 1116 | 3050530 | We now report that human pancreatic amylin and rat CGRP-1 are potent inhibitors of both basal and insulin-stimulated rates of glycogen synthesis in stripped rat soleus muscle in vitro. |
| 1117 | 3051005 | Amylin found in amyloid deposits in human type 2 diabetes mellitus may be a hormone that regulates glycogen metabolism in skeletal muscle. |
| 1118 | 3051005 | Diabetes-associated peptide has recently been isolated and characterized from the amyloid of the islets of Langerhans in type 2 (non-insulin-dependent) diabetics, and immunoreactivity with antibodies to the peptide has been demonstrated in islet B cells of both normal and type 2 diabetic subjects. |
| 1119 | 3051005 | Therefore, amylin may be a factor in the etiology of the insulin resistance in type 2 diabetes mellitus, as both deposition of the peptide in islet amyloid and decreased rates of glucose uptake and glycogen synthesis in skeletal muscle are characteristic of this condition. |
| 1120 | 3051005 | Amylin found in amyloid deposits in human type 2 diabetes mellitus may be a hormone that regulates glycogen metabolism in skeletal muscle. |
| 1121 | 3051005 | Diabetes-associated peptide has recently been isolated and characterized from the amyloid of the islets of Langerhans in type 2 (non-insulin-dependent) diabetics, and immunoreactivity with antibodies to the peptide has been demonstrated in islet B cells of both normal and type 2 diabetic subjects. |
| 1122 | 3051005 | Therefore, amylin may be a factor in the etiology of the insulin resistance in type 2 diabetes mellitus, as both deposition of the peptide in islet amyloid and decreased rates of glucose uptake and glycogen synthesis in skeletal muscle are characteristic of this condition. |
| 1123 | 3051005 | Amylin found in amyloid deposits in human type 2 diabetes mellitus may be a hormone that regulates glycogen metabolism in skeletal muscle. |
| 1124 | 3051005 | Diabetes-associated peptide has recently been isolated and characterized from the amyloid of the islets of Langerhans in type 2 (non-insulin-dependent) diabetics, and immunoreactivity with antibodies to the peptide has been demonstrated in islet B cells of both normal and type 2 diabetic subjects. |
| 1125 | 3051005 | Therefore, amylin may be a factor in the etiology of the insulin resistance in type 2 diabetes mellitus, as both deposition of the peptide in islet amyloid and decreased rates of glucose uptake and glycogen synthesis in skeletal muscle are characteristic of this condition. |
| 1126 | 3053705 | We have identified three cDNA clones encoding islet amyloid polypeptide (IAPP) or diabetes-associated peptide (DAP) by oligonucleotide screening of a lambda gt10 human insulinoma cDNA library. |
| 1127 | 3053705 | These data indicate that this amyloid peptide is generated by proteolytic processing similar to that for proinsulin and other islet prohormones and also that the peptide may be carboxyamidated. |
| 1128 | 3053705 | We have identified three cDNA clones encoding islet amyloid polypeptide (IAPP) or diabetes-associated peptide (DAP) by oligonucleotide screening of a lambda gt10 human insulinoma cDNA library. |
| 1129 | 3053705 | These data indicate that this amyloid peptide is generated by proteolytic processing similar to that for proinsulin and other islet prohormones and also that the peptide may be carboxyamidated. |
| 1130 | 3063263 | The pathogenesis of maturity-onset diabetes mellitus: is there a link to islet amyloid polypeptide? |
| 1131 | 3069282 | Serum concentrations of amyloid A (SAA) and C-reactive protein (CRP) were measured in 122 diabetic patients treated by continuous insulin infusion, 40 patients receiving conventional injection therapy and in 28 healthy controls. |
| 1132 | 3069282 | SAA and CRP-values did not significantly differ between the diabetics, irrespective of the method of insulin substitution used, and the healthy controls. |
| 1133 | 3069282 | Elevated SAA-levels were either associated with raised CRP, indicating a non-specific acute phase reaction, or were markedly diminished or normalized in a six-month follow-up, in spite ongoing pump therapy. |
| 1134 | 3069282 | Increased SAA-concentrations did not correlate with sex or age of patients, diabetes duration, diabetes type, duration of pump treatment, route of insulin, insulin preparation, catheter material and pump model, indicating that pump treatment does not stimulate a specific amyloidogenic reaction. |
| 1135 | 3073901 | The impaired insulin secretion in Type 2 diabetes may be due to a decrease in B-cells and to disruption of the islet structure by amyloid. |
| 1136 | 3276206 | Immunolocalization of islet amyloid polypeptide (IAPP) in pancreatic beta cells by means of peroxidase-antiperoxidase (PAP) and protein A-gold techniques. |
| 1137 | 3276206 | A novel putative polypeptide hormone identified as islet amyloid polypeptide (IAPP) was recently purified from islet amyloid (IA) of diabetic humans and cats, and also from amyloid of a human insulinoma. |
| 1138 | 3276206 | In the present investigation, the authors utilized antisera to insulin, glucagon, somatostatin, pancreatic polypeptide, synthetic human CGRP, and a synthetic human IAPP (7-17) undecapeptide to immunohistochemically (PAP technique) document the presence of IAPP immunoreactive cells in the islets of the cat, dog, mouse, and rat, but not in the islets of the horse or calf. |
| 1139 | 3276206 | Immunolocalization of islet amyloid polypeptide (IAPP) in pancreatic beta cells by means of peroxidase-antiperoxidase (PAP) and protein A-gold techniques. |
| 1140 | 3276206 | A novel putative polypeptide hormone identified as islet amyloid polypeptide (IAPP) was recently purified from islet amyloid (IA) of diabetic humans and cats, and also from amyloid of a human insulinoma. |
| 1141 | 3276206 | In the present investigation, the authors utilized antisera to insulin, glucagon, somatostatin, pancreatic polypeptide, synthetic human CGRP, and a synthetic human IAPP (7-17) undecapeptide to immunohistochemically (PAP technique) document the presence of IAPP immunoreactive cells in the islets of the cat, dog, mouse, and rat, but not in the islets of the horse or calf. |
| 1142 | 3286343 | A major amyloid fibril protein was extracted and, by means of its amino acid composition and amino acid sequence, it was shown to contain intact insulin molecules. |
| 1143 | 3286343 | Porcine insulin is the tenth protein and the first foreign protein to be chemically identified in human amyloid fibrils. |
| 1144 | 3286343 | A major amyloid fibril protein was extracted and, by means of its amino acid composition and amino acid sequence, it was shown to contain intact insulin molecules. |
| 1145 | 3286343 | Porcine insulin is the tenth protein and the first foreign protein to be chemically identified in human amyloid fibrils. |
| 1146 | 3296768 | It was shown recently that amyloid purified from an insulinoma was composed mainly of a novel polypeptide (insulinoma amyloid polypeptide, IAPP), which had partial identity with the neuropeptide calcitonin gene-related peptide (CGRP). |
| 1147 | 3328723 | Islet amyloid polypeptide-like immunoreactivity in the islet B cells of type 2 (non-insulin-dependent) diabetic and non-diabetic individuals. |
| 1148 | 3328723 | A novel peptide, islet amyloid polypeptide (IAPP), with structural resemblance to calcitonin gene-related peptide has recently been purified from amyloid deposits in an insulinoma and from islets of Langerhans. |
| 1149 | 3328723 | Islet amyloid polypeptide-like immunoreactivity in the islet B cells of type 2 (non-insulin-dependent) diabetic and non-diabetic individuals. |
| 1150 | 3328723 | A novel peptide, islet amyloid polypeptide (IAPP), with structural resemblance to calcitonin gene-related peptide has recently been purified from amyloid deposits in an insulinoma and from islets of Langerhans. |
| 1151 | 3512207 | C-reactive protein (CRP), the classical acute-phase reactant, and serum amyloid A protein (SAA), the putative precursor of AA-type amyloid fibrils, were measured in 62 diabetic patients. |
| 1152 | 3512207 | CRP and SAA levels were similar in 18 patients on continuous subcutaneous insulin infusion (CSII), 27 patients treated by conventional insulin therapy (CIT), nine treated by diet only, and eight treated by diet and oral hypoglycemic agents, and were almost entirely within the normal range. |
| 1153 | 3522329 | As nondiabetic monkeys with 0 to 3% islet amyloid progressed up to 20 to 40% amyloid, the insulin secretion and glucose clearance were both decreased (p less than or equal to 0.01), and the glucose and glucagon levels increased (p = 0.05). |
| 1154 | 3535798 | Deposition of amyloid is the most constantly present alteration in the islets of Langerhans in type 2 diabetes mellitus and is also quite common in insulin-producing tumors of the pancreas and it is very likely that these two amyloids are identical. |
| 1155 | 3535798 | We have isolated amyloid fibrils from an insulin-secreting human tumour and purified the fibrillar protein. |
| 1156 | 3535798 | Deposition of amyloid is the most constantly present alteration in the islets of Langerhans in type 2 diabetes mellitus and is also quite common in insulin-producing tumors of the pancreas and it is very likely that these two amyloids are identical. |
| 1157 | 3535798 | We have isolated amyloid fibrils from an insulin-secreting human tumour and purified the fibrillar protein. |
| 1158 | 3890345 | The high dose intravenous glucose tolerance test and concurrent immunoreactive serum insulin and glucagon levels were measured and the results related to the presence or absence of pancreatic insular amyloid in 16 cats, seven of which were known to be diabetic. |
| 1159 | 3890345 | Three diabetic cats with marked insular amyloid deposits had glucose disappearance T1/2 and K (coefficient) values, serum insulin levels, serum glucagon levels, and insulin/glucose ratios which were not significantly different from the other three diabetic cats with slight to moderate insular amyloidosis. |
| 1160 | 3890345 | The high dose intravenous glucose tolerance test and concurrent immunoreactive serum insulin and glucagon levels were measured and the results related to the presence or absence of pancreatic insular amyloid in 16 cats, seven of which were known to be diabetic. |
| 1161 | 3890345 | Three diabetic cats with marked insular amyloid deposits had glucose disappearance T1/2 and K (coefficient) values, serum insulin levels, serum glucagon levels, and insulin/glucose ratios which were not significantly different from the other three diabetic cats with slight to moderate insular amyloidosis. |
| 1162 | 3901495 | Feline insular amyloid: immunohistochemical and immunochemical evidence that the amyloid is insulin-related. |
| 1163 | 3901495 | Utilizing islet amyloid-laden pancreatic tissues from six diabetic cats, we demonstrated substantial immunoreactivity (peroxidase-antiperoxidase technique) of the islet amyloid with antiserum to a B chain-rich insulin fraction, but no reactivity with antisera to insulin, glucagon, or somatostatin. |
| 1164 | 3901495 | These results provide important additional evidence that an insulin-related protein is involved in the formation of islet amyloid. |
| 1165 | 3901495 | Feline insular amyloid: immunohistochemical and immunochemical evidence that the amyloid is insulin-related. |
| 1166 | 3901495 | Utilizing islet amyloid-laden pancreatic tissues from six diabetic cats, we demonstrated substantial immunoreactivity (peroxidase-antiperoxidase technique) of the islet amyloid with antiserum to a B chain-rich insulin fraction, but no reactivity with antisera to insulin, glucagon, or somatostatin. |
| 1167 | 3901495 | These results provide important additional evidence that an insulin-related protein is involved in the formation of islet amyloid. |
| 1168 | 3901495 | Feline insular amyloid: immunohistochemical and immunochemical evidence that the amyloid is insulin-related. |
| 1169 | 3901495 | Utilizing islet amyloid-laden pancreatic tissues from six diabetic cats, we demonstrated substantial immunoreactivity (peroxidase-antiperoxidase technique) of the islet amyloid with antiserum to a B chain-rich insulin fraction, but no reactivity with antisera to insulin, glucagon, or somatostatin. |
| 1170 | 3901495 | These results provide important additional evidence that an insulin-related protein is involved in the formation of islet amyloid. |
| 1171 | 3979691 | Continuous subcutaneous insulin infusion does not induce a significant acute phase response of serum amyloid A protein. |
| 1172 | 3979691 | In a study of 23 matched pairs of Type 1 (insulin-dependent) diabetic patients receiving continuous subcutaneous insulin infusion or conventional insulin injection therapy respectively, there were no significant differences in serum levels of the acute phase proteins, serum amyloid A and C-reactive protein. |
| 1173 | 3979691 | These results do not support the suggestion that continuous subcutaneous insulin infusion stimulates serum amyloid A production or that it carries a risk of inducing reactive systemic amyloidosis. |
| 1174 | 3979691 | Continuous subcutaneous insulin infusion does not induce a significant acute phase response of serum amyloid A protein. |
| 1175 | 3979691 | In a study of 23 matched pairs of Type 1 (insulin-dependent) diabetic patients receiving continuous subcutaneous insulin infusion or conventional insulin injection therapy respectively, there were no significant differences in serum levels of the acute phase proteins, serum amyloid A and C-reactive protein. |
| 1176 | 3979691 | These results do not support the suggestion that continuous subcutaneous insulin infusion stimulates serum amyloid A production or that it carries a risk of inducing reactive systemic amyloidosis. |
| 1177 | 3979691 | Continuous subcutaneous insulin infusion does not induce a significant acute phase response of serum amyloid A protein. |
| 1178 | 3979691 | In a study of 23 matched pairs of Type 1 (insulin-dependent) diabetic patients receiving continuous subcutaneous insulin infusion or conventional insulin injection therapy respectively, there were no significant differences in serum levels of the acute phase proteins, serum amyloid A and C-reactive protein. |
| 1179 | 3979691 | These results do not support the suggestion that continuous subcutaneous insulin infusion stimulates serum amyloid A production or that it carries a risk of inducing reactive systemic amyloidosis. |
| 1180 | 6142148 | Association of insulin pump therapy with raised serum amyloid A in type I diabetes mellitus. |
| 1181 | 6142148 | Serum concentrations of serum amyloid A protein, the high-density-lipoprotein-associated tissue amyloid A precursor, were determined in 29 diabetic patients receiving insulin by subcutaneous injection and in 50 receiving subcutaneous infusion pump therapy. |
| 1182 | 6142148 | Insulin delivered by continuous subcutaneous pumps stimulated serum amyloid A production to levels nearly six times those in normal subjects, nearly twice as much as insulin given by subcutaneous injection. 85% of patients with serum amyloid A levels greater than or equal to 10(4) ng/ml were being treated with insulin pump therapy. |
| 1183 | 6142148 | The relation between insulin aggregation and amyloid A in diabetes was evaluated in 1 patient; treatment with syringe-aggregated insulin resulted in a nearly 300% increase in serum amyloid A levels. |
| 1184 | 6142148 | Association of insulin pump therapy with raised serum amyloid A in type I diabetes mellitus. |
| 1185 | 6142148 | Serum concentrations of serum amyloid A protein, the high-density-lipoprotein-associated tissue amyloid A precursor, were determined in 29 diabetic patients receiving insulin by subcutaneous injection and in 50 receiving subcutaneous infusion pump therapy. |
| 1186 | 6142148 | Insulin delivered by continuous subcutaneous pumps stimulated serum amyloid A production to levels nearly six times those in normal subjects, nearly twice as much as insulin given by subcutaneous injection. 85% of patients with serum amyloid A levels greater than or equal to 10(4) ng/ml were being treated with insulin pump therapy. |
| 1187 | 6142148 | The relation between insulin aggregation and amyloid A in diabetes was evaluated in 1 patient; treatment with syringe-aggregated insulin resulted in a nearly 300% increase in serum amyloid A levels. |
| 1188 | 6142148 | Association of insulin pump therapy with raised serum amyloid A in type I diabetes mellitus. |
| 1189 | 6142148 | Serum concentrations of serum amyloid A protein, the high-density-lipoprotein-associated tissue amyloid A precursor, were determined in 29 diabetic patients receiving insulin by subcutaneous injection and in 50 receiving subcutaneous infusion pump therapy. |
| 1190 | 6142148 | Insulin delivered by continuous subcutaneous pumps stimulated serum amyloid A production to levels nearly six times those in normal subjects, nearly twice as much as insulin given by subcutaneous injection. 85% of patients with serum amyloid A levels greater than or equal to 10(4) ng/ml were being treated with insulin pump therapy. |
| 1191 | 6142148 | The relation between insulin aggregation and amyloid A in diabetes was evaluated in 1 patient; treatment with syringe-aggregated insulin resulted in a nearly 300% increase in serum amyloid A levels. |
| 1192 | 6142148 | Association of insulin pump therapy with raised serum amyloid A in type I diabetes mellitus. |
| 1193 | 6142148 | Serum concentrations of serum amyloid A protein, the high-density-lipoprotein-associated tissue amyloid A precursor, were determined in 29 diabetic patients receiving insulin by subcutaneous injection and in 50 receiving subcutaneous infusion pump therapy. |
| 1194 | 6142148 | Insulin delivered by continuous subcutaneous pumps stimulated serum amyloid A production to levels nearly six times those in normal subjects, nearly twice as much as insulin given by subcutaneous injection. 85% of patients with serum amyloid A levels greater than or equal to 10(4) ng/ml were being treated with insulin pump therapy. |
| 1195 | 6142148 | The relation between insulin aggregation and amyloid A in diabetes was evaluated in 1 patient; treatment with syringe-aggregated insulin resulted in a nearly 300% increase in serum amyloid A levels. |
| 1196 | 6143168 | Insulin pump therapy and serum amyloid A. |
| 1197 | 6159507 | Serum amyloid P-component (SAP) is a normal plasma protein and is a constituent of normal human glomerular basement membrane. |
| 1198 | 6347781 | Islet amyloid in Type 2 (non-insulin-dependent) diabetes is related to insulin. |
| 1199 | 6347781 | In the present study we show by immunohistochemistry that the amyloid reacts with an antiserum against insulin B chain. |
| 1200 | 6347781 | The results indicate that islet amyloid contains insulin B chain and that the amyloid is a product of the islet B cells. |
| 1201 | 6347781 | Islet amyloid in Type 2 (non-insulin-dependent) diabetes is related to insulin. |
| 1202 | 6347781 | In the present study we show by immunohistochemistry that the amyloid reacts with an antiserum against insulin B chain. |
| 1203 | 6347781 | The results indicate that islet amyloid contains insulin B chain and that the amyloid is a product of the islet B cells. |
| 1204 | 6347781 | Islet amyloid in Type 2 (non-insulin-dependent) diabetes is related to insulin. |
| 1205 | 6347781 | In the present study we show by immunohistochemistry that the amyloid reacts with an antiserum against insulin B chain. |
| 1206 | 6347781 | The results indicate that islet amyloid contains insulin B chain and that the amyloid is a product of the islet B cells. |
| 1207 | 6360758 | Massive deposits of amyloid were observed in animals receiving as little as 17 mg of insulin over a time span of 52 days. |
| 1208 | 6360758 | In those animals with hepatic amyloid, marked hepatomegaly was present (i.e., 1200 +/- 250, X +/- SD, versus 300 +/- 25 g for normal animals) and preterminal serum alkaline phosphatase levels were markedly elevated (434 +/- 285 versus 30 +/- 14 IU/L for animals without hepatic amyloid). |
| 1209 | 6360758 | The magnitude of the hepatic amyloid deposits precludes the possibility that they represent insulin aggregates or insulin-derived products per se. |
| 1210 | 6360758 | No evidence of amyloid was present in any of the tissue biopsy specimens obtained prior to insulin infusion. |
| 1211 | 6360758 | It is of particular interest that the affinity of the amyloid deposits for Congo red stain was totally abolished by prior permanganate treatment, suggesting that the amyloid was derived from serum amyloid A protein rather than from immunoglobulin light chains or insulin aggregates per se. |
| 1212 | 6360758 | Massive deposits of amyloid were observed in animals receiving as little as 17 mg of insulin over a time span of 52 days. |
| 1213 | 6360758 | In those animals with hepatic amyloid, marked hepatomegaly was present (i.e., 1200 +/- 250, X +/- SD, versus 300 +/- 25 g for normal animals) and preterminal serum alkaline phosphatase levels were markedly elevated (434 +/- 285 versus 30 +/- 14 IU/L for animals without hepatic amyloid). |
| 1214 | 6360758 | The magnitude of the hepatic amyloid deposits precludes the possibility that they represent insulin aggregates or insulin-derived products per se. |
| 1215 | 6360758 | No evidence of amyloid was present in any of the tissue biopsy specimens obtained prior to insulin infusion. |
| 1216 | 6360758 | It is of particular interest that the affinity of the amyloid deposits for Congo red stain was totally abolished by prior permanganate treatment, suggesting that the amyloid was derived from serum amyloid A protein rather than from immunoglobulin light chains or insulin aggregates per se. |
| 1217 | 6360758 | Massive deposits of amyloid were observed in animals receiving as little as 17 mg of insulin over a time span of 52 days. |
| 1218 | 6360758 | In those animals with hepatic amyloid, marked hepatomegaly was present (i.e., 1200 +/- 250, X +/- SD, versus 300 +/- 25 g for normal animals) and preterminal serum alkaline phosphatase levels were markedly elevated (434 +/- 285 versus 30 +/- 14 IU/L for animals without hepatic amyloid). |
| 1219 | 6360758 | The magnitude of the hepatic amyloid deposits precludes the possibility that they represent insulin aggregates or insulin-derived products per se. |
| 1220 | 6360758 | No evidence of amyloid was present in any of the tissue biopsy specimens obtained prior to insulin infusion. |
| 1221 | 6360758 | It is of particular interest that the affinity of the amyloid deposits for Congo red stain was totally abolished by prior permanganate treatment, suggesting that the amyloid was derived from serum amyloid A protein rather than from immunoglobulin light chains or insulin aggregates per se. |
| 1222 | 6360758 | Massive deposits of amyloid were observed in animals receiving as little as 17 mg of insulin over a time span of 52 days. |
| 1223 | 6360758 | In those animals with hepatic amyloid, marked hepatomegaly was present (i.e., 1200 +/- 250, X +/- SD, versus 300 +/- 25 g for normal animals) and preterminal serum alkaline phosphatase levels were markedly elevated (434 +/- 285 versus 30 +/- 14 IU/L for animals without hepatic amyloid). |
| 1224 | 6360758 | The magnitude of the hepatic amyloid deposits precludes the possibility that they represent insulin aggregates or insulin-derived products per se. |
| 1225 | 6360758 | No evidence of amyloid was present in any of the tissue biopsy specimens obtained prior to insulin infusion. |
| 1226 | 6360758 | It is of particular interest that the affinity of the amyloid deposits for Congo red stain was totally abolished by prior permanganate treatment, suggesting that the amyloid was derived from serum amyloid A protein rather than from immunoglobulin light chains or insulin aggregates per se. |
| 1227 | 6360758 | Massive deposits of amyloid were observed in animals receiving as little as 17 mg of insulin over a time span of 52 days. |
| 1228 | 6360758 | In those animals with hepatic amyloid, marked hepatomegaly was present (i.e., 1200 +/- 250, X +/- SD, versus 300 +/- 25 g for normal animals) and preterminal serum alkaline phosphatase levels were markedly elevated (434 +/- 285 versus 30 +/- 14 IU/L for animals without hepatic amyloid). |
| 1229 | 6360758 | The magnitude of the hepatic amyloid deposits precludes the possibility that they represent insulin aggregates or insulin-derived products per se. |
| 1230 | 6360758 | No evidence of amyloid was present in any of the tissue biopsy specimens obtained prior to insulin infusion. |
| 1231 | 6360758 | It is of particular interest that the affinity of the amyloid deposits for Congo red stain was totally abolished by prior permanganate treatment, suggesting that the amyloid was derived from serum amyloid A protein rather than from immunoglobulin light chains or insulin aggregates per se. |
| 1232 | 6365738 | The pancreases of 17 patients who had cystic fibrosis with and without diabetes mellitus were evaluated at autopsy by routine staining and immunohistochemical methods for insulin, glucagon, somatostatin, and pancreatic polypeptide. |
| 1233 | 6365738 | Young adult diabetic patients with cystic fibrosis have total loss of exocrine pancreas with fat replacement, lack of nesidioblastosis, a qualitative decrease in the number of islets, fibrosis of and amyloid deposits in islets, decreased numbers of insulin-containing cells in each islet, and atrophy of islet cells, probably resulting from progressive ischemia. |
| 1234 | 6375393 | Other plasma proteins of low isoelectric point were detected in basement membranes: albumin (pI 4.9), alpha-1-acid glycoprotein (pI 2.7), amyloid P (pI 3.9-4.8), and alpha-1-antitrypsin (pI 4.5). |
| 1235 | 6391995 | Quantitative morphometry of the pancreases of five 'maturity-onset' diabetic subjects has demonstrated more amyloid in islets of the head, body and tail (where it was found in a mean 29% of the islets occupying a mean 11% islet area) than in islets of the 'pancreatic-polypeptide-rich' lobule of the head (where amyloid was found in a mean of 3% of the islets occupying a mean of 0.7% islet area, both p less than 0.005). |
| 1236 | 6391995 | The non-uniform amyloid distribution may relate to the hormone content of the islet; the head and tail contained significantly more A, B and D-cells than the pancreatic-polypeptide-rich lobule in both non-diabetic subjects (n = 8) and diabetic patients (n = 5; p less than 0.005). |
| 1237 | 6391995 | This result is compatible with the previous suggestion that amyloid may be derived from insulin or its precursors. |
| 1238 | 6391995 | Quantitative morphometry of the pancreases of five 'maturity-onset' diabetic subjects has demonstrated more amyloid in islets of the head, body and tail (where it was found in a mean 29% of the islets occupying a mean 11% islet area) than in islets of the 'pancreatic-polypeptide-rich' lobule of the head (where amyloid was found in a mean of 3% of the islets occupying a mean of 0.7% islet area, both p less than 0.005). |
| 1239 | 6391995 | The non-uniform amyloid distribution may relate to the hormone content of the islet; the head and tail contained significantly more A, B and D-cells than the pancreatic-polypeptide-rich lobule in both non-diabetic subjects (n = 8) and diabetic patients (n = 5; p less than 0.005). |
| 1240 | 6391995 | This result is compatible with the previous suggestion that amyloid may be derived from insulin or its precursors. |
| 1241 | 6391995 | Quantitative morphometry of the pancreases of five 'maturity-onset' diabetic subjects has demonstrated more amyloid in islets of the head, body and tail (where it was found in a mean 29% of the islets occupying a mean 11% islet area) than in islets of the 'pancreatic-polypeptide-rich' lobule of the head (where amyloid was found in a mean of 3% of the islets occupying a mean of 0.7% islet area, both p less than 0.005). |
| 1242 | 6391995 | The non-uniform amyloid distribution may relate to the hormone content of the islet; the head and tail contained significantly more A, B and D-cells than the pancreatic-polypeptide-rich lobule in both non-diabetic subjects (n = 8) and diabetic patients (n = 5; p less than 0.005). |
| 1243 | 6391995 | This result is compatible with the previous suggestion that amyloid may be derived from insulin or its precursors. |
| 1244 | 6395671 | With gradual deterioration of cells and replacement by amyloid, secretion of insulin is impaired and concentrations of glucagon increase. |
| 1245 | 6395671 | Nondiabetic humans with sufficient beta cells to sustain adequate secretion of insulin, but with moderate amyloid infiltration, probably would be in a category equivalent to BD monkeys; since these people are not overtly hyperglycemic, they are not clinically recognizable as diabetic and would be classified retrospectively as nondiabetic. |
| 1246 | 6395671 | With gradual deterioration of cells and replacement by amyloid, secretion of insulin is impaired and concentrations of glucagon increase. |
| 1247 | 6395671 | Nondiabetic humans with sufficient beta cells to sustain adequate secretion of insulin, but with moderate amyloid infiltration, probably would be in a category equivalent to BD monkeys; since these people are not overtly hyperglycemic, they are not clinically recognizable as diabetic and would be classified retrospectively as nondiabetic. |
| 1248 | 6745737 | The stromal layer contained several irregular cells which were characterized by cytoplasmic vacuolization and collagen fiber separation by an amyloid-like, intercellular ground substance. |
| 1249 | 6848400 | Since elevated levels of serum amyloid A protein (SAA) and diminished amyloid fibril degrading activity (AFDA) are associated with amyloidosis, we measured SAA and AFDA in ten type I diabetics treated with continuous subcutaneous insulin infusion and in five conventionally treated patients. |
| 1250 | 7028600 | The low prevalence of amyloid seen in nondiabetics and the fact that all adult onset, insulin treated diabetics had islet amyloid indicate that a reaction to endogenous insulin may be the basis for the deposition of islet amyloid. |
| 1251 | 7033114 | Antiserum specific for human prealbumin (HPA) was studied by indirect immunofluorescence on tissue sections of cardiac ventricles containing senile cardiac amyloid. |
| 1252 | 7033114 | THe reaction of anti-HPA was completely blocked by purified human prealbumin but was not influenced by absorption with purified human albumin or proteins extracted from any amyloid types tested. |
| 1253 | 7033114 | These studies suggest that senile cardiac amyloid of the ASc1 type contains prealbumin or a protein antigenically closely related to this molecule. |
| 1254 | 7033114 | Antiserum specific for human prealbumin (HPA) was studied by indirect immunofluorescence on tissue sections of cardiac ventricles containing senile cardiac amyloid. |
| 1255 | 7033114 | THe reaction of anti-HPA was completely blocked by purified human prealbumin but was not influenced by absorption with purified human albumin or proteins extracted from any amyloid types tested. |
| 1256 | 7033114 | These studies suggest that senile cardiac amyloid of the ASc1 type contains prealbumin or a protein antigenically closely related to this molecule. |
| 1257 | 7033114 | Antiserum specific for human prealbumin (HPA) was studied by indirect immunofluorescence on tissue sections of cardiac ventricles containing senile cardiac amyloid. |
| 1258 | 7033114 | THe reaction of anti-HPA was completely blocked by purified human prealbumin but was not influenced by absorption with purified human albumin or proteins extracted from any amyloid types tested. |
| 1259 | 7033114 | These studies suggest that senile cardiac amyloid of the ASc1 type contains prealbumin or a protein antigenically closely related to this molecule. |
| 1260 | 7472513 | Islet amyloid polypeptide (amylin) is expressed in sensory neurons. |
| 1261 | 7472513 | Islet amyloid polypeptide (IAPP) or amylin is a hormone candidate predominantly expressed in insulin cells. |
| 1262 | 7472513 | In addition, IAPP-like immunoreactivity occurred in nerve cell bodies storing substance P and pituitary adenylate cyclase-activating polypeptide. |
| 1263 | 7472513 | Islet amyloid polypeptide (amylin) is expressed in sensory neurons. |
| 1264 | 7472513 | Islet amyloid polypeptide (IAPP) or amylin is a hormone candidate predominantly expressed in insulin cells. |
| 1265 | 7472513 | In addition, IAPP-like immunoreactivity occurred in nerve cell bodies storing substance P and pituitary adenylate cyclase-activating polypeptide. |
| 1266 | 7487407 | In statistical analysis, only two of the 25 diseases recorded were associated with interstitial amyloid: chronic obstructive pulmonary disease and non-insulin-dependent diabetes mellitus. |
| 1267 | 7487407 | In addition, non-insulin-dependent diabetes mellitus was accompanied with higher amounts of interstitial amyloid than with all other disorders (Wilcoxon; P < .03). |
| 1268 | 7487407 | In statistical analysis, only two of the 25 diseases recorded were associated with interstitial amyloid: chronic obstructive pulmonary disease and non-insulin-dependent diabetes mellitus. |
| 1269 | 7487407 | In addition, non-insulin-dependent diabetes mellitus was accompanied with higher amounts of interstitial amyloid than with all other disorders (Wilcoxon; P < .03). |
| 1270 | 7489583 | Spongiform encephalopathies are related to mutation and/or polymorphisms of the PRNP amyloid gene. |
| 1271 | 7504270 | Giant multilevel cation channels formed by Alzheimer disease amyloid beta-protein [A beta P-(1-40)] in bilayer membranes. |
| 1272 | 7504270 | We have recently shown that the Alzheimer disease 40-residue amyloid beta-protein [A beta P-(1-40)] can form cation-selective channels when incorporated into planar lipid bilayers by fusion of liposomes containing the peptide. |
| 1273 | 7504270 | Giant multilevel cation channels formed by Alzheimer disease amyloid beta-protein [A beta P-(1-40)] in bilayer membranes. |
| 1274 | 7504270 | We have recently shown that the Alzheimer disease 40-residue amyloid beta-protein [A beta P-(1-40)] can form cation-selective channels when incorporated into planar lipid bilayers by fusion of liposomes containing the peptide. |
| 1275 | 7533336 | We investigated the association of amyloid beta-protein precursor (APP) and platelet derived microparticles in 20 normal controls and 91 patients with various diseases causing a thrombotic tendency. |
| 1276 | 7535207 | Serum amyloid A protein in patients with non-insulin-dependent diabetes mellitus. |
| 1277 | 7535207 | We determined the serum amyloid A protein (SAA) levels in patients with non-insulin-dependent diabetes mellitus (NIDDM), and investigated the possible association between SAA and the complications of NIDDM. |
| 1278 | 7535207 | However, SAA levels in patients with NIDDM increased significantly, with increase of urinary albumin excretion (p = 0.027). |
| 1279 | 7535207 | Serum amyloid A protein in patients with non-insulin-dependent diabetes mellitus. |
| 1280 | 7535207 | We determined the serum amyloid A protein (SAA) levels in patients with non-insulin-dependent diabetes mellitus (NIDDM), and investigated the possible association between SAA and the complications of NIDDM. |
| 1281 | 7535207 | However, SAA levels in patients with NIDDM increased significantly, with increase of urinary albumin excretion (p = 0.027). |
| 1282 | 7535678 | Islet amyloid polypeptide and its N-terminal and C-terminal flanking peptides' immunoreactivity in islet amyloid of diabetic patients. |
| 1283 | 7535678 | We determined immunohistochemically whether the islet amyloid polypeptide (IAPP)/amylin precursor is one component of islet amyloid, using polyclonal antibodies specific for human IAPP8-17 and amino (N)-terminal and carboxy (C)-terminal flanking peptides. |
| 1284 | 7535678 | In six type 2 diabetic subjects and a subject with type A insulin resistance, islet amyloid deposits were reactive to anti-IAPP8-17 antibody, but not to anti-N-terminal and C-terminal flanking peptide antibodies. |
| 1285 | 7535678 | Islet amyloid polypeptide and its N-terminal and C-terminal flanking peptides' immunoreactivity in islet amyloid of diabetic patients. |
| 1286 | 7535678 | We determined immunohistochemically whether the islet amyloid polypeptide (IAPP)/amylin precursor is one component of islet amyloid, using polyclonal antibodies specific for human IAPP8-17 and amino (N)-terminal and carboxy (C)-terminal flanking peptides. |
| 1287 | 7535678 | In six type 2 diabetic subjects and a subject with type A insulin resistance, islet amyloid deposits were reactive to anti-IAPP8-17 antibody, but not to anti-N-terminal and C-terminal flanking peptide antibodies. |
| 1288 | 7535678 | Islet amyloid polypeptide and its N-terminal and C-terminal flanking peptides' immunoreactivity in islet amyloid of diabetic patients. |
| 1289 | 7535678 | We determined immunohistochemically whether the islet amyloid polypeptide (IAPP)/amylin precursor is one component of islet amyloid, using polyclonal antibodies specific for human IAPP8-17 and amino (N)-terminal and carboxy (C)-terminal flanking peptides. |
| 1290 | 7535678 | In six type 2 diabetic subjects and a subject with type A insulin resistance, islet amyloid deposits were reactive to anti-IAPP8-17 antibody, but not to anti-N-terminal and C-terminal flanking peptide antibodies. |
| 1291 | 7578065 | Effect of pH and insulin on fibrillogenesis of islet amyloid polypeptide in vitro. |
| 1292 | 7594773 | Islet amyloid polypeptide (IAPP or amylin) is the main component of pancreatic islet amyloid found in the vast majority of patients with noninsulin-dependent (Type-2) diabetes mellitus (NIDDM). |
| 1293 | 7660530 | Amylin has been postulated to be involved in the pathogenesis of feline diabetes mellitus both through its metabolic effects, which include inhibition of insulin secretion and induction of insulin resistance, and via progressive amyloid deposition and beta cell degeneration. |
| 1294 | 7660530 | The gastrointestinal hormone glucagon-like peptide-1 may also prove useful in treating diabetic cats, because of its stimulatory effect on insulin secretion and synthesis, and the absence of significant hypoglycemic effect. |
| 1295 | 7665954 | [Biochemical studies of amyloidogenesis in two different types of amyloidoses--amyloid transthyretin variant in familial amyloidotic polyneuropathy and islet amyloid polypeptide in non-insulin-dependent diabetes mellitus]. |
| 1296 | 7677175 | Human islet amyloid polypeptide expression in COS-1 cells. |
| 1297 | 7677175 | Non-insulin-dependent diabetes mellitus is characterized by concurrent loss of beta-cells and deposition of islet amyloid derived from islet amyloid polypeptide (IAPP). |
| 1298 | 7677175 | We have previously demonstrated that IAPP-derived amyloid forms intracellularly in humans with chronic excess insulin expression (eg, insulinoma and insulin receptor antibody-induced insulin resistance). |
| 1299 | 7677175 | Thus, overexpression of human IAPP can result in intracellular amyloid formation that is associated with cell death, suggesting that intracellular amyloid may play a role in beta-cell loss in non-insulin-dependent diabetes mellitus. |
| 1300 | 7677175 | Human islet amyloid polypeptide expression in COS-1 cells. |
| 1301 | 7677175 | Non-insulin-dependent diabetes mellitus is characterized by concurrent loss of beta-cells and deposition of islet amyloid derived from islet amyloid polypeptide (IAPP). |
| 1302 | 7677175 | We have previously demonstrated that IAPP-derived amyloid forms intracellularly in humans with chronic excess insulin expression (eg, insulinoma and insulin receptor antibody-induced insulin resistance). |
| 1303 | 7677175 | Thus, overexpression of human IAPP can result in intracellular amyloid formation that is associated with cell death, suggesting that intracellular amyloid may play a role in beta-cell loss in non-insulin-dependent diabetes mellitus. |
| 1304 | 7677175 | Human islet amyloid polypeptide expression in COS-1 cells. |
| 1305 | 7677175 | Non-insulin-dependent diabetes mellitus is characterized by concurrent loss of beta-cells and deposition of islet amyloid derived from islet amyloid polypeptide (IAPP). |
| 1306 | 7677175 | We have previously demonstrated that IAPP-derived amyloid forms intracellularly in humans with chronic excess insulin expression (eg, insulinoma and insulin receptor antibody-induced insulin resistance). |
| 1307 | 7677175 | Thus, overexpression of human IAPP can result in intracellular amyloid formation that is associated with cell death, suggesting that intracellular amyloid may play a role in beta-cell loss in non-insulin-dependent diabetes mellitus. |
| 1308 | 7677175 | Human islet amyloid polypeptide expression in COS-1 cells. |
| 1309 | 7677175 | Non-insulin-dependent diabetes mellitus is characterized by concurrent loss of beta-cells and deposition of islet amyloid derived from islet amyloid polypeptide (IAPP). |
| 1310 | 7677175 | We have previously demonstrated that IAPP-derived amyloid forms intracellularly in humans with chronic excess insulin expression (eg, insulinoma and insulin receptor antibody-induced insulin resistance). |
| 1311 | 7677175 | Thus, overexpression of human IAPP can result in intracellular amyloid formation that is associated with cell death, suggesting that intracellular amyloid may play a role in beta-cell loss in non-insulin-dependent diabetes mellitus. |
| 1312 | 7705017 | Islet amyloid polypeptide: does it play a pathophysiological role in the development of diabetes? |
| 1313 | 7705017 | The potential exists for the development of amylin antagonists as pharmacological agents to enhance insulin secretion in NIDDM but antagonism of systematic CGRP would need to be avoided. |
| 1314 | 7711888 | Formation of islet amyloid fibrils in beta-secretory granules of transgenic mice expressing human islet amyloid polypeptide/amylin. |
| 1315 | 7711888 | To investigate the relationship between human islet amyloid polypeptide (IAPP)/amylin expression and islet amyloid deposits in the pathogenesis of human non-insulin-dependent diabetes mellitus (NIDDM), we developed transgenic mice using a human IAPP cDNA connected to an insulin promoter. |
| 1316 | 7711888 | Formation of islet amyloid fibrils in beta-secretory granules of transgenic mice expressing human islet amyloid polypeptide/amylin. |
| 1317 | 7711888 | To investigate the relationship between human islet amyloid polypeptide (IAPP)/amylin expression and islet amyloid deposits in the pathogenesis of human non-insulin-dependent diabetes mellitus (NIDDM), we developed transgenic mice using a human IAPP cDNA connected to an insulin promoter. |
| 1318 | 7738722 | Islet amyloid polypeptide (IAPP) is the main proteinaceous component of pancreatic islet amyloid, which is a characteristic feature of type 2 diabetes. |
| 1319 | 7753801 | Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosis. |
| 1320 | 7753801 | Serum amyloid P component (SAP) binds to all types of amyloid fibrils and is a universal constituent of amyloid deposits, including the plaques, amorphous amyloid beta protein deposits and neurofibrillary tangles of Alzheimer disease [Coria, F., Castano, E., Prelli, F., Larrondo-Lillo, M., van Duinen, S., Shelanski, M. |
| 1321 | 7753801 | Here we show that SAP prevents proteolysis of the amyloid fibrils of Alzheimer disease, of systemic amyloid A amyloidosis and of systemic monoclonal light chain amyloidosis and may thereby contribute to their persistence in vivo. |
| 1322 | 7753801 | Interference with binding of SAP to amyloid fibrils in vivo is thus an attractive therapeutic objective, achievement of which should promote regression of the deposits. |
| 1323 | 7753801 | Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosis. |
| 1324 | 7753801 | Serum amyloid P component (SAP) binds to all types of amyloid fibrils and is a universal constituent of amyloid deposits, including the plaques, amorphous amyloid beta protein deposits and neurofibrillary tangles of Alzheimer disease [Coria, F., Castano, E., Prelli, F., Larrondo-Lillo, M., van Duinen, S., Shelanski, M. |
| 1325 | 7753801 | Here we show that SAP prevents proteolysis of the amyloid fibrils of Alzheimer disease, of systemic amyloid A amyloidosis and of systemic monoclonal light chain amyloidosis and may thereby contribute to their persistence in vivo. |
| 1326 | 7753801 | Interference with binding of SAP to amyloid fibrils in vivo is thus an attractive therapeutic objective, achievement of which should promote regression of the deposits. |
| 1327 | 7753801 | Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosis. |
| 1328 | 7753801 | Serum amyloid P component (SAP) binds to all types of amyloid fibrils and is a universal constituent of amyloid deposits, including the plaques, amorphous amyloid beta protein deposits and neurofibrillary tangles of Alzheimer disease [Coria, F., Castano, E., Prelli, F., Larrondo-Lillo, M., van Duinen, S., Shelanski, M. |
| 1329 | 7753801 | Here we show that SAP prevents proteolysis of the amyloid fibrils of Alzheimer disease, of systemic amyloid A amyloidosis and of systemic monoclonal light chain amyloidosis and may thereby contribute to their persistence in vivo. |
| 1330 | 7753801 | Interference with binding of SAP to amyloid fibrils in vivo is thus an attractive therapeutic objective, achievement of which should promote regression of the deposits. |
| 1331 | 7753801 | Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosis. |
| 1332 | 7753801 | Serum amyloid P component (SAP) binds to all types of amyloid fibrils and is a universal constituent of amyloid deposits, including the plaques, amorphous amyloid beta protein deposits and neurofibrillary tangles of Alzheimer disease [Coria, F., Castano, E., Prelli, F., Larrondo-Lillo, M., van Duinen, S., Shelanski, M. |
| 1333 | 7753801 | Here we show that SAP prevents proteolysis of the amyloid fibrils of Alzheimer disease, of systemic amyloid A amyloidosis and of systemic monoclonal light chain amyloidosis and may thereby contribute to their persistence in vivo. |
| 1334 | 7753801 | Interference with binding of SAP to amyloid fibrils in vivo is thus an attractive therapeutic objective, achievement of which should promote regression of the deposits. |
| 1335 | 7771063 | Assignment of islet amyloid polypeptide (IAPP) gene to feline chromosome B4 using the polymerase chain reaction technique on feline-rodent hybrid cell lines. |
| 1336 | 7771063 | The most characteristic morphologic features of the pancreatic islets of human non-insulin-dependent diabetes mellitus (NIDDM, or type 2 diabetes mellitus) and of similar forms of diabetes in cats and macaques are the deposition of amyloid (islet amyloid) and the loss of beta cells. |
| 1337 | 7771063 | Islet amyloid is derived from islet amyloid polypeptide (IAPP), which is a normal secretory product of the beta cells. |
| 1338 | 7771063 | Assignment of islet amyloid polypeptide (IAPP) gene to feline chromosome B4 using the polymerase chain reaction technique on feline-rodent hybrid cell lines. |
| 1339 | 7771063 | The most characteristic morphologic features of the pancreatic islets of human non-insulin-dependent diabetes mellitus (NIDDM, or type 2 diabetes mellitus) and of similar forms of diabetes in cats and macaques are the deposition of amyloid (islet amyloid) and the loss of beta cells. |
| 1340 | 7771063 | Islet amyloid is derived from islet amyloid polypeptide (IAPP), which is a normal secretory product of the beta cells. |
| 1341 | 7771063 | Assignment of islet amyloid polypeptide (IAPP) gene to feline chromosome B4 using the polymerase chain reaction technique on feline-rodent hybrid cell lines. |
| 1342 | 7771063 | The most characteristic morphologic features of the pancreatic islets of human non-insulin-dependent diabetes mellitus (NIDDM, or type 2 diabetes mellitus) and of similar forms of diabetes in cats and macaques are the deposition of amyloid (islet amyloid) and the loss of beta cells. |
| 1343 | 7771063 | Islet amyloid is derived from islet amyloid polypeptide (IAPP), which is a normal secretory product of the beta cells. |
| 1344 | 7781840 | Amylin/islet amyloid polypeptide: biochemistry, physiology, patho-physiology. |
| 1345 | 7781840 | Amylin is packed in beta-cell granules and cosecreted with insulin in response to the same stimuli but, unlike other beta-cell products, it is produced from specific a gene on chromosome 12. |
| 1346 | 7796979 | Non-parallelism of islet amyloid polypeptide (amylin) and insulin gene expression in rats islets following dexamethasone treatment. |
| 1347 | 7796979 | Islet amyloid polypeptide (IAPP), a novel islet hormone candidate, has been reported to be over-expressed relative to insulin in rats following dexamethasone treatment. |
| 1348 | 7796979 | Non-parallelism of islet amyloid polypeptide (amylin) and insulin gene expression in rats islets following dexamethasone treatment. |
| 1349 | 7796979 | Islet amyloid polypeptide (IAPP), a novel islet hormone candidate, has been reported to be over-expressed relative to insulin in rats following dexamethasone treatment. |
| 1350 | 7821732 | The extent to which this loss of insulin secretion reflects a major predisposing factor in the aetiology of this type of diabetes or is secondary to glucose toxicity or amyloid accumulation remains to be determined. |
| 1351 | 7831499 | Chronic exposure of cultured rat pancreatic islets to elevated concentrations of islet amyloid polypeptide (IAPP) causes a decrease in islet DNA content and medium insulin accumulation. |
| 1352 | 7831499 | The biological action of islet amyloid polypeptide (IAPP) remains to be established, although a role for IAPP in causing beta-cell failure in diabetes has been proposed. |
| 1353 | 7831499 | Chronic exposure of cultured rat pancreatic islets to elevated concentrations of islet amyloid polypeptide (IAPP) causes a decrease in islet DNA content and medium insulin accumulation. |
| 1354 | 7831499 | The biological action of islet amyloid polypeptide (IAPP) remains to be established, although a role for IAPP in causing beta-cell failure in diabetes has been proposed. |
| 1355 | 7868080 | Intracerebral and cerebrovascular beta-protein amyloid deposits are a hallmark of the pathology of both sporadic and familial Alzheimer's disease, beta 2-microglobulin-derived amyloid is a common complication of long term haemodialysis, and islet amyloid polypeptide is the fibril protein in the universal islet amyloidosis of type II diabetes mellitus. |
| 1356 | 7868080 | New fibril proteins have lately been identified in hereditary amyloidosis, including variants of gelsolin, apolipoprotein AI, lysozyme and fibrinogen. |
| 1357 | 7868080 | The development of radiolabelled serum amyloid P component (SAP) scintigraphy has allowed amyloid to be diagnosed non-invasively in vivo for the first time, provided unique insight into the distribution and size of amyloid deposits, and yielded novel information on the natural history and the effects of treatment. |
| 1358 | 7868080 | Intracerebral and cerebrovascular beta-protein amyloid deposits are a hallmark of the pathology of both sporadic and familial Alzheimer's disease, beta 2-microglobulin-derived amyloid is a common complication of long term haemodialysis, and islet amyloid polypeptide is the fibril protein in the universal islet amyloidosis of type II diabetes mellitus. |
| 1359 | 7868080 | New fibril proteins have lately been identified in hereditary amyloidosis, including variants of gelsolin, apolipoprotein AI, lysozyme and fibrinogen. |
| 1360 | 7868080 | The development of radiolabelled serum amyloid P component (SAP) scintigraphy has allowed amyloid to be diagnosed non-invasively in vivo for the first time, provided unique insight into the distribution and size of amyloid deposits, and yielded novel information on the natural history and the effects of treatment. |
| 1361 | 7904897 | Islet amyloid polypeptide gene expression in the endocrine pancreas of the rat: a combined in situ hybridization and immunocytochemical study. |
| 1362 | 7904897 | The expression of the islet amyloid polypeptide (IAPP) gene within the endocrine pancreas and its correlation with insular neuroendocrine peptide localization were investigated in the rat. |
| 1363 | 7904897 | Islet amyloid polypeptide gene expression in the endocrine pancreas of the rat: a combined in situ hybridization and immunocytochemical study. |
| 1364 | 7904897 | The expression of the islet amyloid polypeptide (IAPP) gene within the endocrine pancreas and its correlation with insular neuroendocrine peptide localization were investigated in the rat. |
| 1365 | 7929615 | Amylin is a 37-amino acid peptide first isolated, purified, and characterized from the amyloid deposits in the pancrease of type 2 diabetics. |
| 1366 | 7929615 | Amylin has structural and functional relationships to two other messenger proteins, calcitonin and CGRP. |
| 1367 | 7929615 | Amylin has relatively potent calcitonin-like activity on bone metabolism and weaker CGRP-like activity on the vasculature. |
| 1368 | 7929617 | Molecular physiology of the islet amyloid polypeptide (IAPP)/amylin gene in man, rat, and transgenic mice. |
| 1369 | 7929617 | Islet amyloid polypeptide ("amylin") is the major protein component of amyloid deposits in pancreatic islets of type 2 (non-insulin-dependent) diabetic patients. |
| 1370 | 7929617 | Islet amyloid polypeptide consists of 37 amino acids, is co-produced and co-secreted with insulin from islet beta-cells, can act as a hormone in regulation of carbohydrate metabolism, and is implicated in the pathogenesis of islet amyloid formation and of type 2 diabetes mellitus. |
| 1371 | 7929617 | Rat islet amyloid polypeptide differs from human islet amyloid polypeptide particularly in the region of amino acids 25-28, which is important for amyloid fibril formation. |
| 1372 | 7929617 | To study the genetic organization and biosynthesis of islet amyloid polypeptide, we have isolated and analyzed the human and rat islet amyloid polypeptide gene and corresponding cDNAs. |
| 1373 | 7929617 | Apart from a putative signal sequence, these precursors contain amino- and carboxy-terminal flanking peptides in addition to the mature islet amyloid polypeptide. |
| 1374 | 7929617 | To understand regulation of islet amyloid polypeptide gene expression, we have identified several potential cis-acting transcriptional control elements that influence beta-cell-specific islet amyloid polypeptide gene expression. |
| 1375 | 7929617 | Using antisera raised against synthetic human islet amyloid polypeptide we developed a specific and sensitive radioimmunoassay to measure levels of islet amyloid polypeptide in plasma and tissue extracts. |
| 1376 | 7929617 | Also antisera raised against the flanking peptides will be used in studying human islet amyloid polypeptide biosynthesis. |
| 1377 | 7929617 | Elevated plasma islet amyloid polypeptide levels have been demonstrated in some diabetic, glucose-intolerant, and obese individuals, as well as in rodent models of diabetes and obesity. |
| 1378 | 7929617 | To examine the potential role of islet amyloid polypeptide overproduction in the pathogenesis of islet amyloid formation and type 2 diabetes, we generated transgenic mice that overproduce either the amyloidogenic human islet amyloid polypeptide or the nonamyloidogenic rat islet amyloid polypeptide in their islet beta-cells. |
| 1379 | 7929617 | Despite moderately to highly (up to 15-fold) elevated plasma islet amyloid polypeptide levels, no marked hyperglycemia, hyperinsulinemia or obesity was observed. |
| 1380 | 7929617 | This suggests that chronic overproduction of islet amyloid polypeptide "per se" does not cause insulin resistance. |
| 1381 | 7929617 | No islet amyloid deposits were detected in mice up to 63 weeks of age, but in every mouse producing human islet amyloid polypeptide (as in man), accumulation of islet amyloid polypeptide was observed in beta-cell lysosomal bodies. |
| 1382 | 7929617 | Molecular physiology of the islet amyloid polypeptide (IAPP)/amylin gene in man, rat, and transgenic mice. |
| 1383 | 7929617 | Islet amyloid polypeptide ("amylin") is the major protein component of amyloid deposits in pancreatic islets of type 2 (non-insulin-dependent) diabetic patients. |
| 1384 | 7929617 | Islet amyloid polypeptide consists of 37 amino acids, is co-produced and co-secreted with insulin from islet beta-cells, can act as a hormone in regulation of carbohydrate metabolism, and is implicated in the pathogenesis of islet amyloid formation and of type 2 diabetes mellitus. |
| 1385 | 7929617 | Rat islet amyloid polypeptide differs from human islet amyloid polypeptide particularly in the region of amino acids 25-28, which is important for amyloid fibril formation. |
| 1386 | 7929617 | To study the genetic organization and biosynthesis of islet amyloid polypeptide, we have isolated and analyzed the human and rat islet amyloid polypeptide gene and corresponding cDNAs. |
| 1387 | 7929617 | Apart from a putative signal sequence, these precursors contain amino- and carboxy-terminal flanking peptides in addition to the mature islet amyloid polypeptide. |
| 1388 | 7929617 | To understand regulation of islet amyloid polypeptide gene expression, we have identified several potential cis-acting transcriptional control elements that influence beta-cell-specific islet amyloid polypeptide gene expression. |
| 1389 | 7929617 | Using antisera raised against synthetic human islet amyloid polypeptide we developed a specific and sensitive radioimmunoassay to measure levels of islet amyloid polypeptide in plasma and tissue extracts. |
| 1390 | 7929617 | Also antisera raised against the flanking peptides will be used in studying human islet amyloid polypeptide biosynthesis. |
| 1391 | 7929617 | Elevated plasma islet amyloid polypeptide levels have been demonstrated in some diabetic, glucose-intolerant, and obese individuals, as well as in rodent models of diabetes and obesity. |
| 1392 | 7929617 | To examine the potential role of islet amyloid polypeptide overproduction in the pathogenesis of islet amyloid formation and type 2 diabetes, we generated transgenic mice that overproduce either the amyloidogenic human islet amyloid polypeptide or the nonamyloidogenic rat islet amyloid polypeptide in their islet beta-cells. |
| 1393 | 7929617 | Despite moderately to highly (up to 15-fold) elevated plasma islet amyloid polypeptide levels, no marked hyperglycemia, hyperinsulinemia or obesity was observed. |
| 1394 | 7929617 | This suggests that chronic overproduction of islet amyloid polypeptide "per se" does not cause insulin resistance. |
| 1395 | 7929617 | No islet amyloid deposits were detected in mice up to 63 weeks of age, but in every mouse producing human islet amyloid polypeptide (as in man), accumulation of islet amyloid polypeptide was observed in beta-cell lysosomal bodies. |
| 1396 | 7929617 | Molecular physiology of the islet amyloid polypeptide (IAPP)/amylin gene in man, rat, and transgenic mice. |
| 1397 | 7929617 | Islet amyloid polypeptide ("amylin") is the major protein component of amyloid deposits in pancreatic islets of type 2 (non-insulin-dependent) diabetic patients. |
| 1398 | 7929617 | Islet amyloid polypeptide consists of 37 amino acids, is co-produced and co-secreted with insulin from islet beta-cells, can act as a hormone in regulation of carbohydrate metabolism, and is implicated in the pathogenesis of islet amyloid formation and of type 2 diabetes mellitus. |
| 1399 | 7929617 | Rat islet amyloid polypeptide differs from human islet amyloid polypeptide particularly in the region of amino acids 25-28, which is important for amyloid fibril formation. |
| 1400 | 7929617 | To study the genetic organization and biosynthesis of islet amyloid polypeptide, we have isolated and analyzed the human and rat islet amyloid polypeptide gene and corresponding cDNAs. |
| 1401 | 7929617 | Apart from a putative signal sequence, these precursors contain amino- and carboxy-terminal flanking peptides in addition to the mature islet amyloid polypeptide. |
| 1402 | 7929617 | To understand regulation of islet amyloid polypeptide gene expression, we have identified several potential cis-acting transcriptional control elements that influence beta-cell-specific islet amyloid polypeptide gene expression. |
| 1403 | 7929617 | Using antisera raised against synthetic human islet amyloid polypeptide we developed a specific and sensitive radioimmunoassay to measure levels of islet amyloid polypeptide in plasma and tissue extracts. |
| 1404 | 7929617 | Also antisera raised against the flanking peptides will be used in studying human islet amyloid polypeptide biosynthesis. |
| 1405 | 7929617 | Elevated plasma islet amyloid polypeptide levels have been demonstrated in some diabetic, glucose-intolerant, and obese individuals, as well as in rodent models of diabetes and obesity. |
| 1406 | 7929617 | To examine the potential role of islet amyloid polypeptide overproduction in the pathogenesis of islet amyloid formation and type 2 diabetes, we generated transgenic mice that overproduce either the amyloidogenic human islet amyloid polypeptide or the nonamyloidogenic rat islet amyloid polypeptide in their islet beta-cells. |
| 1407 | 7929617 | Despite moderately to highly (up to 15-fold) elevated plasma islet amyloid polypeptide levels, no marked hyperglycemia, hyperinsulinemia or obesity was observed. |
| 1408 | 7929617 | This suggests that chronic overproduction of islet amyloid polypeptide "per se" does not cause insulin resistance. |
| 1409 | 7929617 | No islet amyloid deposits were detected in mice up to 63 weeks of age, but in every mouse producing human islet amyloid polypeptide (as in man), accumulation of islet amyloid polypeptide was observed in beta-cell lysosomal bodies. |
| 1410 | 7929617 | Molecular physiology of the islet amyloid polypeptide (IAPP)/amylin gene in man, rat, and transgenic mice. |
| 1411 | 7929617 | Islet amyloid polypeptide ("amylin") is the major protein component of amyloid deposits in pancreatic islets of type 2 (non-insulin-dependent) diabetic patients. |
| 1412 | 7929617 | Islet amyloid polypeptide consists of 37 amino acids, is co-produced and co-secreted with insulin from islet beta-cells, can act as a hormone in regulation of carbohydrate metabolism, and is implicated in the pathogenesis of islet amyloid formation and of type 2 diabetes mellitus. |
| 1413 | 7929617 | Rat islet amyloid polypeptide differs from human islet amyloid polypeptide particularly in the region of amino acids 25-28, which is important for amyloid fibril formation. |
| 1414 | 7929617 | To study the genetic organization and biosynthesis of islet amyloid polypeptide, we have isolated and analyzed the human and rat islet amyloid polypeptide gene and corresponding cDNAs. |
| 1415 | 7929617 | Apart from a putative signal sequence, these precursors contain amino- and carboxy-terminal flanking peptides in addition to the mature islet amyloid polypeptide. |
| 1416 | 7929617 | To understand regulation of islet amyloid polypeptide gene expression, we have identified several potential cis-acting transcriptional control elements that influence beta-cell-specific islet amyloid polypeptide gene expression. |
| 1417 | 7929617 | Using antisera raised against synthetic human islet amyloid polypeptide we developed a specific and sensitive radioimmunoassay to measure levels of islet amyloid polypeptide in plasma and tissue extracts. |
| 1418 | 7929617 | Also antisera raised against the flanking peptides will be used in studying human islet amyloid polypeptide biosynthesis. |
| 1419 | 7929617 | Elevated plasma islet amyloid polypeptide levels have been demonstrated in some diabetic, glucose-intolerant, and obese individuals, as well as in rodent models of diabetes and obesity. |
| 1420 | 7929617 | To examine the potential role of islet amyloid polypeptide overproduction in the pathogenesis of islet amyloid formation and type 2 diabetes, we generated transgenic mice that overproduce either the amyloidogenic human islet amyloid polypeptide or the nonamyloidogenic rat islet amyloid polypeptide in their islet beta-cells. |
| 1421 | 7929617 | Despite moderately to highly (up to 15-fold) elevated plasma islet amyloid polypeptide levels, no marked hyperglycemia, hyperinsulinemia or obesity was observed. |
| 1422 | 7929617 | This suggests that chronic overproduction of islet amyloid polypeptide "per se" does not cause insulin resistance. |
| 1423 | 7929617 | No islet amyloid deposits were detected in mice up to 63 weeks of age, but in every mouse producing human islet amyloid polypeptide (as in man), accumulation of islet amyloid polypeptide was observed in beta-cell lysosomal bodies. |
| 1424 | 7929617 | Molecular physiology of the islet amyloid polypeptide (IAPP)/amylin gene in man, rat, and transgenic mice. |
| 1425 | 7929617 | Islet amyloid polypeptide ("amylin") is the major protein component of amyloid deposits in pancreatic islets of type 2 (non-insulin-dependent) diabetic patients. |
| 1426 | 7929617 | Islet amyloid polypeptide consists of 37 amino acids, is co-produced and co-secreted with insulin from islet beta-cells, can act as a hormone in regulation of carbohydrate metabolism, and is implicated in the pathogenesis of islet amyloid formation and of type 2 diabetes mellitus. |
| 1427 | 7929617 | Rat islet amyloid polypeptide differs from human islet amyloid polypeptide particularly in the region of amino acids 25-28, which is important for amyloid fibril formation. |
| 1428 | 7929617 | To study the genetic organization and biosynthesis of islet amyloid polypeptide, we have isolated and analyzed the human and rat islet amyloid polypeptide gene and corresponding cDNAs. |
| 1429 | 7929617 | Apart from a putative signal sequence, these precursors contain amino- and carboxy-terminal flanking peptides in addition to the mature islet amyloid polypeptide. |
| 1430 | 7929617 | To understand regulation of islet amyloid polypeptide gene expression, we have identified several potential cis-acting transcriptional control elements that influence beta-cell-specific islet amyloid polypeptide gene expression. |
| 1431 | 7929617 | Using antisera raised against synthetic human islet amyloid polypeptide we developed a specific and sensitive radioimmunoassay to measure levels of islet amyloid polypeptide in plasma and tissue extracts. |
| 1432 | 7929617 | Also antisera raised against the flanking peptides will be used in studying human islet amyloid polypeptide biosynthesis. |
| 1433 | 7929617 | Elevated plasma islet amyloid polypeptide levels have been demonstrated in some diabetic, glucose-intolerant, and obese individuals, as well as in rodent models of diabetes and obesity. |
| 1434 | 7929617 | To examine the potential role of islet amyloid polypeptide overproduction in the pathogenesis of islet amyloid formation and type 2 diabetes, we generated transgenic mice that overproduce either the amyloidogenic human islet amyloid polypeptide or the nonamyloidogenic rat islet amyloid polypeptide in their islet beta-cells. |
| 1435 | 7929617 | Despite moderately to highly (up to 15-fold) elevated plasma islet amyloid polypeptide levels, no marked hyperglycemia, hyperinsulinemia or obesity was observed. |
| 1436 | 7929617 | This suggests that chronic overproduction of islet amyloid polypeptide "per se" does not cause insulin resistance. |
| 1437 | 7929617 | No islet amyloid deposits were detected in mice up to 63 weeks of age, but in every mouse producing human islet amyloid polypeptide (as in man), accumulation of islet amyloid polypeptide was observed in beta-cell lysosomal bodies. |
| 1438 | 7929617 | Molecular physiology of the islet amyloid polypeptide (IAPP)/amylin gene in man, rat, and transgenic mice. |
| 1439 | 7929617 | Islet amyloid polypeptide ("amylin") is the major protein component of amyloid deposits in pancreatic islets of type 2 (non-insulin-dependent) diabetic patients. |
| 1440 | 7929617 | Islet amyloid polypeptide consists of 37 amino acids, is co-produced and co-secreted with insulin from islet beta-cells, can act as a hormone in regulation of carbohydrate metabolism, and is implicated in the pathogenesis of islet amyloid formation and of type 2 diabetes mellitus. |
| 1441 | 7929617 | Rat islet amyloid polypeptide differs from human islet amyloid polypeptide particularly in the region of amino acids 25-28, which is important for amyloid fibril formation. |
| 1442 | 7929617 | To study the genetic organization and biosynthesis of islet amyloid polypeptide, we have isolated and analyzed the human and rat islet amyloid polypeptide gene and corresponding cDNAs. |
| 1443 | 7929617 | Apart from a putative signal sequence, these precursors contain amino- and carboxy-terminal flanking peptides in addition to the mature islet amyloid polypeptide. |
| 1444 | 7929617 | To understand regulation of islet amyloid polypeptide gene expression, we have identified several potential cis-acting transcriptional control elements that influence beta-cell-specific islet amyloid polypeptide gene expression. |
| 1445 | 7929617 | Using antisera raised against synthetic human islet amyloid polypeptide we developed a specific and sensitive radioimmunoassay to measure levels of islet amyloid polypeptide in plasma and tissue extracts. |
| 1446 | 7929617 | Also antisera raised against the flanking peptides will be used in studying human islet amyloid polypeptide biosynthesis. |
| 1447 | 7929617 | Elevated plasma islet amyloid polypeptide levels have been demonstrated in some diabetic, glucose-intolerant, and obese individuals, as well as in rodent models of diabetes and obesity. |
| 1448 | 7929617 | To examine the potential role of islet amyloid polypeptide overproduction in the pathogenesis of islet amyloid formation and type 2 diabetes, we generated transgenic mice that overproduce either the amyloidogenic human islet amyloid polypeptide or the nonamyloidogenic rat islet amyloid polypeptide in their islet beta-cells. |
| 1449 | 7929617 | Despite moderately to highly (up to 15-fold) elevated plasma islet amyloid polypeptide levels, no marked hyperglycemia, hyperinsulinemia or obesity was observed. |
| 1450 | 7929617 | This suggests that chronic overproduction of islet amyloid polypeptide "per se" does not cause insulin resistance. |
| 1451 | 7929617 | No islet amyloid deposits were detected in mice up to 63 weeks of age, but in every mouse producing human islet amyloid polypeptide (as in man), accumulation of islet amyloid polypeptide was observed in beta-cell lysosomal bodies. |
| 1452 | 7929617 | Molecular physiology of the islet amyloid polypeptide (IAPP)/amylin gene in man, rat, and transgenic mice. |
| 1453 | 7929617 | Islet amyloid polypeptide ("amylin") is the major protein component of amyloid deposits in pancreatic islets of type 2 (non-insulin-dependent) diabetic patients. |
| 1454 | 7929617 | Islet amyloid polypeptide consists of 37 amino acids, is co-produced and co-secreted with insulin from islet beta-cells, can act as a hormone in regulation of carbohydrate metabolism, and is implicated in the pathogenesis of islet amyloid formation and of type 2 diabetes mellitus. |
| 1455 | 7929617 | Rat islet amyloid polypeptide differs from human islet amyloid polypeptide particularly in the region of amino acids 25-28, which is important for amyloid fibril formation. |
| 1456 | 7929617 | To study the genetic organization and biosynthesis of islet amyloid polypeptide, we have isolated and analyzed the human and rat islet amyloid polypeptide gene and corresponding cDNAs. |
| 1457 | 7929617 | Apart from a putative signal sequence, these precursors contain amino- and carboxy-terminal flanking peptides in addition to the mature islet amyloid polypeptide. |
| 1458 | 7929617 | To understand regulation of islet amyloid polypeptide gene expression, we have identified several potential cis-acting transcriptional control elements that influence beta-cell-specific islet amyloid polypeptide gene expression. |
| 1459 | 7929617 | Using antisera raised against synthetic human islet amyloid polypeptide we developed a specific and sensitive radioimmunoassay to measure levels of islet amyloid polypeptide in plasma and tissue extracts. |
| 1460 | 7929617 | Also antisera raised against the flanking peptides will be used in studying human islet amyloid polypeptide biosynthesis. |
| 1461 | 7929617 | Elevated plasma islet amyloid polypeptide levels have been demonstrated in some diabetic, glucose-intolerant, and obese individuals, as well as in rodent models of diabetes and obesity. |
| 1462 | 7929617 | To examine the potential role of islet amyloid polypeptide overproduction in the pathogenesis of islet amyloid formation and type 2 diabetes, we generated transgenic mice that overproduce either the amyloidogenic human islet amyloid polypeptide or the nonamyloidogenic rat islet amyloid polypeptide in their islet beta-cells. |
| 1463 | 7929617 | Despite moderately to highly (up to 15-fold) elevated plasma islet amyloid polypeptide levels, no marked hyperglycemia, hyperinsulinemia or obesity was observed. |
| 1464 | 7929617 | This suggests that chronic overproduction of islet amyloid polypeptide "per se" does not cause insulin resistance. |
| 1465 | 7929617 | No islet amyloid deposits were detected in mice up to 63 weeks of age, but in every mouse producing human islet amyloid polypeptide (as in man), accumulation of islet amyloid polypeptide was observed in beta-cell lysosomal bodies. |
| 1466 | 7929617 | Molecular physiology of the islet amyloid polypeptide (IAPP)/amylin gene in man, rat, and transgenic mice. |
| 1467 | 7929617 | Islet amyloid polypeptide ("amylin") is the major protein component of amyloid deposits in pancreatic islets of type 2 (non-insulin-dependent) diabetic patients. |
| 1468 | 7929617 | Islet amyloid polypeptide consists of 37 amino acids, is co-produced and co-secreted with insulin from islet beta-cells, can act as a hormone in regulation of carbohydrate metabolism, and is implicated in the pathogenesis of islet amyloid formation and of type 2 diabetes mellitus. |
| 1469 | 7929617 | Rat islet amyloid polypeptide differs from human islet amyloid polypeptide particularly in the region of amino acids 25-28, which is important for amyloid fibril formation. |
| 1470 | 7929617 | To study the genetic organization and biosynthesis of islet amyloid polypeptide, we have isolated and analyzed the human and rat islet amyloid polypeptide gene and corresponding cDNAs. |
| 1471 | 7929617 | Apart from a putative signal sequence, these precursors contain amino- and carboxy-terminal flanking peptides in addition to the mature islet amyloid polypeptide. |
| 1472 | 7929617 | To understand regulation of islet amyloid polypeptide gene expression, we have identified several potential cis-acting transcriptional control elements that influence beta-cell-specific islet amyloid polypeptide gene expression. |
| 1473 | 7929617 | Using antisera raised against synthetic human islet amyloid polypeptide we developed a specific and sensitive radioimmunoassay to measure levels of islet amyloid polypeptide in plasma and tissue extracts. |
| 1474 | 7929617 | Also antisera raised against the flanking peptides will be used in studying human islet amyloid polypeptide biosynthesis. |
| 1475 | 7929617 | Elevated plasma islet amyloid polypeptide levels have been demonstrated in some diabetic, glucose-intolerant, and obese individuals, as well as in rodent models of diabetes and obesity. |
| 1476 | 7929617 | To examine the potential role of islet amyloid polypeptide overproduction in the pathogenesis of islet amyloid formation and type 2 diabetes, we generated transgenic mice that overproduce either the amyloidogenic human islet amyloid polypeptide or the nonamyloidogenic rat islet amyloid polypeptide in their islet beta-cells. |
| 1477 | 7929617 | Despite moderately to highly (up to 15-fold) elevated plasma islet amyloid polypeptide levels, no marked hyperglycemia, hyperinsulinemia or obesity was observed. |
| 1478 | 7929617 | This suggests that chronic overproduction of islet amyloid polypeptide "per se" does not cause insulin resistance. |
| 1479 | 7929617 | No islet amyloid deposits were detected in mice up to 63 weeks of age, but in every mouse producing human islet amyloid polypeptide (as in man), accumulation of islet amyloid polypeptide was observed in beta-cell lysosomal bodies. |
| 1480 | 7929617 | Molecular physiology of the islet amyloid polypeptide (IAPP)/amylin gene in man, rat, and transgenic mice. |
| 1481 | 7929617 | Islet amyloid polypeptide ("amylin") is the major protein component of amyloid deposits in pancreatic islets of type 2 (non-insulin-dependent) diabetic patients. |
| 1482 | 7929617 | Islet amyloid polypeptide consists of 37 amino acids, is co-produced and co-secreted with insulin from islet beta-cells, can act as a hormone in regulation of carbohydrate metabolism, and is implicated in the pathogenesis of islet amyloid formation and of type 2 diabetes mellitus. |
| 1483 | 7929617 | Rat islet amyloid polypeptide differs from human islet amyloid polypeptide particularly in the region of amino acids 25-28, which is important for amyloid fibril formation. |
| 1484 | 7929617 | To study the genetic organization and biosynthesis of islet amyloid polypeptide, we have isolated and analyzed the human and rat islet amyloid polypeptide gene and corresponding cDNAs. |
| 1485 | 7929617 | Apart from a putative signal sequence, these precursors contain amino- and carboxy-terminal flanking peptides in addition to the mature islet amyloid polypeptide. |
| 1486 | 7929617 | To understand regulation of islet amyloid polypeptide gene expression, we have identified several potential cis-acting transcriptional control elements that influence beta-cell-specific islet amyloid polypeptide gene expression. |
| 1487 | 7929617 | Using antisera raised against synthetic human islet amyloid polypeptide we developed a specific and sensitive radioimmunoassay to measure levels of islet amyloid polypeptide in plasma and tissue extracts. |
| 1488 | 7929617 | Also antisera raised against the flanking peptides will be used in studying human islet amyloid polypeptide biosynthesis. |
| 1489 | 7929617 | Elevated plasma islet amyloid polypeptide levels have been demonstrated in some diabetic, glucose-intolerant, and obese individuals, as well as in rodent models of diabetes and obesity. |
| 1490 | 7929617 | To examine the potential role of islet amyloid polypeptide overproduction in the pathogenesis of islet amyloid formation and type 2 diabetes, we generated transgenic mice that overproduce either the amyloidogenic human islet amyloid polypeptide or the nonamyloidogenic rat islet amyloid polypeptide in their islet beta-cells. |
| 1491 | 7929617 | Despite moderately to highly (up to 15-fold) elevated plasma islet amyloid polypeptide levels, no marked hyperglycemia, hyperinsulinemia or obesity was observed. |
| 1492 | 7929617 | This suggests that chronic overproduction of islet amyloid polypeptide "per se" does not cause insulin resistance. |
| 1493 | 7929617 | No islet amyloid deposits were detected in mice up to 63 weeks of age, but in every mouse producing human islet amyloid polypeptide (as in man), accumulation of islet amyloid polypeptide was observed in beta-cell lysosomal bodies. |
| 1494 | 7929617 | Molecular physiology of the islet amyloid polypeptide (IAPP)/amylin gene in man, rat, and transgenic mice. |
| 1495 | 7929617 | Islet amyloid polypeptide ("amylin") is the major protein component of amyloid deposits in pancreatic islets of type 2 (non-insulin-dependent) diabetic patients. |
| 1496 | 7929617 | Islet amyloid polypeptide consists of 37 amino acids, is co-produced and co-secreted with insulin from islet beta-cells, can act as a hormone in regulation of carbohydrate metabolism, and is implicated in the pathogenesis of islet amyloid formation and of type 2 diabetes mellitus. |
| 1497 | 7929617 | Rat islet amyloid polypeptide differs from human islet amyloid polypeptide particularly in the region of amino acids 25-28, which is important for amyloid fibril formation. |
| 1498 | 7929617 | To study the genetic organization and biosynthesis of islet amyloid polypeptide, we have isolated and analyzed the human and rat islet amyloid polypeptide gene and corresponding cDNAs. |
| 1499 | 7929617 | Apart from a putative signal sequence, these precursors contain amino- and carboxy-terminal flanking peptides in addition to the mature islet amyloid polypeptide. |
| 1500 | 7929617 | To understand regulation of islet amyloid polypeptide gene expression, we have identified several potential cis-acting transcriptional control elements that influence beta-cell-specific islet amyloid polypeptide gene expression. |
| 1501 | 7929617 | Using antisera raised against synthetic human islet amyloid polypeptide we developed a specific and sensitive radioimmunoassay to measure levels of islet amyloid polypeptide in plasma and tissue extracts. |
| 1502 | 7929617 | Also antisera raised against the flanking peptides will be used in studying human islet amyloid polypeptide biosynthesis. |
| 1503 | 7929617 | Elevated plasma islet amyloid polypeptide levels have been demonstrated in some diabetic, glucose-intolerant, and obese individuals, as well as in rodent models of diabetes and obesity. |
| 1504 | 7929617 | To examine the potential role of islet amyloid polypeptide overproduction in the pathogenesis of islet amyloid formation and type 2 diabetes, we generated transgenic mice that overproduce either the amyloidogenic human islet amyloid polypeptide or the nonamyloidogenic rat islet amyloid polypeptide in their islet beta-cells. |
| 1505 | 7929617 | Despite moderately to highly (up to 15-fold) elevated plasma islet amyloid polypeptide levels, no marked hyperglycemia, hyperinsulinemia or obesity was observed. |
| 1506 | 7929617 | This suggests that chronic overproduction of islet amyloid polypeptide "per se" does not cause insulin resistance. |
| 1507 | 7929617 | No islet amyloid deposits were detected in mice up to 63 weeks of age, but in every mouse producing human islet amyloid polypeptide (as in man), accumulation of islet amyloid polypeptide was observed in beta-cell lysosomal bodies. |
| 1508 | 7929617 | Molecular physiology of the islet amyloid polypeptide (IAPP)/amylin gene in man, rat, and transgenic mice. |
| 1509 | 7929617 | Islet amyloid polypeptide ("amylin") is the major protein component of amyloid deposits in pancreatic islets of type 2 (non-insulin-dependent) diabetic patients. |
| 1510 | 7929617 | Islet amyloid polypeptide consists of 37 amino acids, is co-produced and co-secreted with insulin from islet beta-cells, can act as a hormone in regulation of carbohydrate metabolism, and is implicated in the pathogenesis of islet amyloid formation and of type 2 diabetes mellitus. |
| 1511 | 7929617 | Rat islet amyloid polypeptide differs from human islet amyloid polypeptide particularly in the region of amino acids 25-28, which is important for amyloid fibril formation. |
| 1512 | 7929617 | To study the genetic organization and biosynthesis of islet amyloid polypeptide, we have isolated and analyzed the human and rat islet amyloid polypeptide gene and corresponding cDNAs. |
| 1513 | 7929617 | Apart from a putative signal sequence, these precursors contain amino- and carboxy-terminal flanking peptides in addition to the mature islet amyloid polypeptide. |
| 1514 | 7929617 | To understand regulation of islet amyloid polypeptide gene expression, we have identified several potential cis-acting transcriptional control elements that influence beta-cell-specific islet amyloid polypeptide gene expression. |
| 1515 | 7929617 | Using antisera raised against synthetic human islet amyloid polypeptide we developed a specific and sensitive radioimmunoassay to measure levels of islet amyloid polypeptide in plasma and tissue extracts. |
| 1516 | 7929617 | Also antisera raised against the flanking peptides will be used in studying human islet amyloid polypeptide biosynthesis. |
| 1517 | 7929617 | Elevated plasma islet amyloid polypeptide levels have been demonstrated in some diabetic, glucose-intolerant, and obese individuals, as well as in rodent models of diabetes and obesity. |
| 1518 | 7929617 | To examine the potential role of islet amyloid polypeptide overproduction in the pathogenesis of islet amyloid formation and type 2 diabetes, we generated transgenic mice that overproduce either the amyloidogenic human islet amyloid polypeptide or the nonamyloidogenic rat islet amyloid polypeptide in their islet beta-cells. |
| 1519 | 7929617 | Despite moderately to highly (up to 15-fold) elevated plasma islet amyloid polypeptide levels, no marked hyperglycemia, hyperinsulinemia or obesity was observed. |
| 1520 | 7929617 | This suggests that chronic overproduction of islet amyloid polypeptide "per se" does not cause insulin resistance. |
| 1521 | 7929617 | No islet amyloid deposits were detected in mice up to 63 weeks of age, but in every mouse producing human islet amyloid polypeptide (as in man), accumulation of islet amyloid polypeptide was observed in beta-cell lysosomal bodies. |
| 1522 | 7929617 | Molecular physiology of the islet amyloid polypeptide (IAPP)/amylin gene in man, rat, and transgenic mice. |
| 1523 | 7929617 | Islet amyloid polypeptide ("amylin") is the major protein component of amyloid deposits in pancreatic islets of type 2 (non-insulin-dependent) diabetic patients. |
| 1524 | 7929617 | Islet amyloid polypeptide consists of 37 amino acids, is co-produced and co-secreted with insulin from islet beta-cells, can act as a hormone in regulation of carbohydrate metabolism, and is implicated in the pathogenesis of islet amyloid formation and of type 2 diabetes mellitus. |
| 1525 | 7929617 | Rat islet amyloid polypeptide differs from human islet amyloid polypeptide particularly in the region of amino acids 25-28, which is important for amyloid fibril formation. |
| 1526 | 7929617 | To study the genetic organization and biosynthesis of islet amyloid polypeptide, we have isolated and analyzed the human and rat islet amyloid polypeptide gene and corresponding cDNAs. |
| 1527 | 7929617 | Apart from a putative signal sequence, these precursors contain amino- and carboxy-terminal flanking peptides in addition to the mature islet amyloid polypeptide. |
| 1528 | 7929617 | To understand regulation of islet amyloid polypeptide gene expression, we have identified several potential cis-acting transcriptional control elements that influence beta-cell-specific islet amyloid polypeptide gene expression. |
| 1529 | 7929617 | Using antisera raised against synthetic human islet amyloid polypeptide we developed a specific and sensitive radioimmunoassay to measure levels of islet amyloid polypeptide in plasma and tissue extracts. |
| 1530 | 7929617 | Also antisera raised against the flanking peptides will be used in studying human islet amyloid polypeptide biosynthesis. |
| 1531 | 7929617 | Elevated plasma islet amyloid polypeptide levels have been demonstrated in some diabetic, glucose-intolerant, and obese individuals, as well as in rodent models of diabetes and obesity. |
| 1532 | 7929617 | To examine the potential role of islet amyloid polypeptide overproduction in the pathogenesis of islet amyloid formation and type 2 diabetes, we generated transgenic mice that overproduce either the amyloidogenic human islet amyloid polypeptide or the nonamyloidogenic rat islet amyloid polypeptide in their islet beta-cells. |
| 1533 | 7929617 | Despite moderately to highly (up to 15-fold) elevated plasma islet amyloid polypeptide levels, no marked hyperglycemia, hyperinsulinemia or obesity was observed. |
| 1534 | 7929617 | This suggests that chronic overproduction of islet amyloid polypeptide "per se" does not cause insulin resistance. |
| 1535 | 7929617 | No islet amyloid deposits were detected in mice up to 63 weeks of age, but in every mouse producing human islet amyloid polypeptide (as in man), accumulation of islet amyloid polypeptide was observed in beta-cell lysosomal bodies. |
| 1536 | 7929617 | Molecular physiology of the islet amyloid polypeptide (IAPP)/amylin gene in man, rat, and transgenic mice. |
| 1537 | 7929617 | Islet amyloid polypeptide ("amylin") is the major protein component of amyloid deposits in pancreatic islets of type 2 (non-insulin-dependent) diabetic patients. |
| 1538 | 7929617 | Islet amyloid polypeptide consists of 37 amino acids, is co-produced and co-secreted with insulin from islet beta-cells, can act as a hormone in regulation of carbohydrate metabolism, and is implicated in the pathogenesis of islet amyloid formation and of type 2 diabetes mellitus. |
| 1539 | 7929617 | Rat islet amyloid polypeptide differs from human islet amyloid polypeptide particularly in the region of amino acids 25-28, which is important for amyloid fibril formation. |
| 1540 | 7929617 | To study the genetic organization and biosynthesis of islet amyloid polypeptide, we have isolated and analyzed the human and rat islet amyloid polypeptide gene and corresponding cDNAs. |
| 1541 | 7929617 | Apart from a putative signal sequence, these precursors contain amino- and carboxy-terminal flanking peptides in addition to the mature islet amyloid polypeptide. |
| 1542 | 7929617 | To understand regulation of islet amyloid polypeptide gene expression, we have identified several potential cis-acting transcriptional control elements that influence beta-cell-specific islet amyloid polypeptide gene expression. |
| 1543 | 7929617 | Using antisera raised against synthetic human islet amyloid polypeptide we developed a specific and sensitive radioimmunoassay to measure levels of islet amyloid polypeptide in plasma and tissue extracts. |
| 1544 | 7929617 | Also antisera raised against the flanking peptides will be used in studying human islet amyloid polypeptide biosynthesis. |
| 1545 | 7929617 | Elevated plasma islet amyloid polypeptide levels have been demonstrated in some diabetic, glucose-intolerant, and obese individuals, as well as in rodent models of diabetes and obesity. |
| 1546 | 7929617 | To examine the potential role of islet amyloid polypeptide overproduction in the pathogenesis of islet amyloid formation and type 2 diabetes, we generated transgenic mice that overproduce either the amyloidogenic human islet amyloid polypeptide or the nonamyloidogenic rat islet amyloid polypeptide in their islet beta-cells. |
| 1547 | 7929617 | Despite moderately to highly (up to 15-fold) elevated plasma islet amyloid polypeptide levels, no marked hyperglycemia, hyperinsulinemia or obesity was observed. |
| 1548 | 7929617 | This suggests that chronic overproduction of islet amyloid polypeptide "per se" does not cause insulin resistance. |
| 1549 | 7929617 | No islet amyloid deposits were detected in mice up to 63 weeks of age, but in every mouse producing human islet amyloid polypeptide (as in man), accumulation of islet amyloid polypeptide was observed in beta-cell lysosomal bodies. |
| 1550 | 7929617 | Molecular physiology of the islet amyloid polypeptide (IAPP)/amylin gene in man, rat, and transgenic mice. |
| 1551 | 7929617 | Islet amyloid polypeptide ("amylin") is the major protein component of amyloid deposits in pancreatic islets of type 2 (non-insulin-dependent) diabetic patients. |
| 1552 | 7929617 | Islet amyloid polypeptide consists of 37 amino acids, is co-produced and co-secreted with insulin from islet beta-cells, can act as a hormone in regulation of carbohydrate metabolism, and is implicated in the pathogenesis of islet amyloid formation and of type 2 diabetes mellitus. |
| 1553 | 7929617 | Rat islet amyloid polypeptide differs from human islet amyloid polypeptide particularly in the region of amino acids 25-28, which is important for amyloid fibril formation. |
| 1554 | 7929617 | To study the genetic organization and biosynthesis of islet amyloid polypeptide, we have isolated and analyzed the human and rat islet amyloid polypeptide gene and corresponding cDNAs. |
| 1555 | 7929617 | Apart from a putative signal sequence, these precursors contain amino- and carboxy-terminal flanking peptides in addition to the mature islet amyloid polypeptide. |
| 1556 | 7929617 | To understand regulation of islet amyloid polypeptide gene expression, we have identified several potential cis-acting transcriptional control elements that influence beta-cell-specific islet amyloid polypeptide gene expression. |
| 1557 | 7929617 | Using antisera raised against synthetic human islet amyloid polypeptide we developed a specific and sensitive radioimmunoassay to measure levels of islet amyloid polypeptide in plasma and tissue extracts. |
| 1558 | 7929617 | Also antisera raised against the flanking peptides will be used in studying human islet amyloid polypeptide biosynthesis. |
| 1559 | 7929617 | Elevated plasma islet amyloid polypeptide levels have been demonstrated in some diabetic, glucose-intolerant, and obese individuals, as well as in rodent models of diabetes and obesity. |
| 1560 | 7929617 | To examine the potential role of islet amyloid polypeptide overproduction in the pathogenesis of islet amyloid formation and type 2 diabetes, we generated transgenic mice that overproduce either the amyloidogenic human islet amyloid polypeptide or the nonamyloidogenic rat islet amyloid polypeptide in their islet beta-cells. |
| 1561 | 7929617 | Despite moderately to highly (up to 15-fold) elevated plasma islet amyloid polypeptide levels, no marked hyperglycemia, hyperinsulinemia or obesity was observed. |
| 1562 | 7929617 | This suggests that chronic overproduction of islet amyloid polypeptide "per se" does not cause insulin resistance. |
| 1563 | 7929617 | No islet amyloid deposits were detected in mice up to 63 weeks of age, but in every mouse producing human islet amyloid polypeptide (as in man), accumulation of islet amyloid polypeptide was observed in beta-cell lysosomal bodies. |
| 1564 | 7958499 | Pancreatic expression and secretion of human islet amyloid polypeptide in a transgenic mouse. |
| 1565 | 7958499 | Islet amyloid polypeptide (IAPP) is a secretory product of the pancreatic beta-cell, which is the primary constituent of the islet amyloid that develops in type II diabetes. |
| 1566 | 7958499 | Pancreatic expression and secretion of human islet amyloid polypeptide in a transgenic mouse. |
| 1567 | 7958499 | Islet amyloid polypeptide (IAPP) is a secretory product of the pancreatic beta-cell, which is the primary constituent of the islet amyloid that develops in type II diabetes. |
| 1568 | 7962550 | Increased levels of circulating islet amyloid polypeptide in patients with chronic renal failure have no effect on insulin secretion. |
| 1569 | 7962550 | To elucidate the metabolism of islet amyloid polypeptide (IAPP) with respect to a possible renal elimination we investigated IAPP levels in 20 lean, nondiabetic patients with renal failure maintained on chronic hemodialysis (HD) and in 20 healthy controls. |
| 1570 | 7962550 | Increased levels of circulating islet amyloid polypeptide in patients with chronic renal failure have no effect on insulin secretion. |
| 1571 | 7962550 | To elucidate the metabolism of islet amyloid polypeptide (IAPP) with respect to a possible renal elimination we investigated IAPP levels in 20 lean, nondiabetic patients with renal failure maintained on chronic hemodialysis (HD) and in 20 healthy controls. |
| 1572 | 7983807 | Islet amyloid deposits are the characteristic lesions of the pancreas of the patients with non-insulin-dependent diabetes mellitus (NIDDM). |
| 1573 | 7983807 | Islet amyloid polypeptide (IAPP or amylin) is a 37 amino acid peptide, which was extracted and characterized from islet amyloid deposits in patients with NIDDM. |
| 1574 | 7983807 | Islet amyloid deposits are the characteristic lesions of the pancreas of the patients with non-insulin-dependent diabetes mellitus (NIDDM). |
| 1575 | 7983807 | Islet amyloid polypeptide (IAPP or amylin) is a 37 amino acid peptide, which was extracted and characterized from islet amyloid deposits in patients with NIDDM. |
| 1576 | 7983808 | [Construction of transgenic mouse system expressing human islet amyloid polypeptide (IAPP)/amylin]. |
| 1577 | 7983808 | To investigate the relationship between human islet amyloid polypeptide (IAPP)/amylin expression and islet amyloid deposits in the pathogenesis of human non-insulin-dependent diabetes mellitus (NIDDM), we generated transgenic mice using a human IAPP cDNA connected to an insulin promoter. |
| 1578 | 7983808 | [Construction of transgenic mouse system expressing human islet amyloid polypeptide (IAPP)/amylin]. |
| 1579 | 7983808 | To investigate the relationship between human islet amyloid polypeptide (IAPP)/amylin expression and islet amyloid deposits in the pathogenesis of human non-insulin-dependent diabetes mellitus (NIDDM), we generated transgenic mice using a human IAPP cDNA connected to an insulin promoter. |
| 1580 | 8027243 | We report islet hyperplasia, nesidioblastosis, and abundant islet amyloidosis (derived from islet amyloid polypeptide) in a case of severe insulin resistance due to a circulating antiinsulin receptor antibody. |
| 1581 | 8031680 | Increasing numbers of hereditary amyloid-related transthyretin mutations have been reported (more than 30 to date). |
| 1582 | 8031680 | In islet amyloid polypeptide, the amyloid of adult-onset diabetes, the amino-acid sequence Ala-Ile-Leu-Ser at positions 25 to 28 appears to be critical for fibrillogenesis. |
| 1583 | 8031680 | Increasing numbers of hereditary amyloid-related transthyretin mutations have been reported (more than 30 to date). |
| 1584 | 8031680 | In islet amyloid polypeptide, the amyloid of adult-onset diabetes, the amino-acid sequence Ala-Ile-Leu-Ser at positions 25 to 28 appears to be critical for fibrillogenesis. |
| 1585 | 8060096 | An improved method for the determination of islet amyloid polypeptide levels in plasma. |
| 1586 | 8060096 | We describe an improved method for the determination of islet amyloid polypeptide (IAPP) levels in plasma. |
| 1587 | 8060096 | An improved method for the determination of islet amyloid polypeptide levels in plasma. |
| 1588 | 8060096 | We describe an improved method for the determination of islet amyloid polypeptide (IAPP) levels in plasma. |
| 1589 | 8061570 | Islet amyloid polypeptide in Psammomys obesus: lack of correlation between insulin resistance and plasma IAPP levels. |
| 1590 | 8061570 | We have examined the presence of islet amyloid polypeptide (IAPP), or amylin, in these animals. |
| 1591 | 8061570 | Therefore, insulin resistance in Psammomys obesus does not appear to result from an elevated plasma IAPP level nor from development of amyloid deposits. |
| 1592 | 8061570 | Islet amyloid polypeptide in Psammomys obesus: lack of correlation between insulin resistance and plasma IAPP levels. |
| 1593 | 8061570 | We have examined the presence of islet amyloid polypeptide (IAPP), or amylin, in these animals. |
| 1594 | 8061570 | Therefore, insulin resistance in Psammomys obesus does not appear to result from an elevated plasma IAPP level nor from development of amyloid deposits. |
| 1595 | 8061570 | Islet amyloid polypeptide in Psammomys obesus: lack of correlation between insulin resistance and plasma IAPP levels. |
| 1596 | 8061570 | We have examined the presence of islet amyloid polypeptide (IAPP), or amylin, in these animals. |
| 1597 | 8061570 | Therefore, insulin resistance in Psammomys obesus does not appear to result from an elevated plasma IAPP level nor from development of amyloid deposits. |
| 1598 | 8076756 | Islet amyloid polypeptide is expressed in endocrine cells of the gastric mucosa in the rat and mouse. |
| 1599 | 8078905 | Intra- and extracellular amyloid fibrils are formed in cultured pancreatic islets of transgenic mice expressing human islet amyloid polypeptide. |
| 1600 | 8078905 | Islet amyloid polypeptide (IAPP) is the constituent peptide of amyloid deposits found in the islets of non-insulin-dependent diabetic patients. |
| 1601 | 8078905 | Formation of islet amyloid is associated with a progressive destruction of insulin-producing beta cells. |
| 1602 | 8078905 | Thus, glucose-induced expression and secretion of hIAPP in transgenic mouse islets can lead to formation of amyloid fibrils similar to that found in non-insulin-dependent diabetes mellitus. |
| 1603 | 8078905 | Intra- and extracellular amyloid fibrils are formed in cultured pancreatic islets of transgenic mice expressing human islet amyloid polypeptide. |
| 1604 | 8078905 | Islet amyloid polypeptide (IAPP) is the constituent peptide of amyloid deposits found in the islets of non-insulin-dependent diabetic patients. |
| 1605 | 8078905 | Formation of islet amyloid is associated with a progressive destruction of insulin-producing beta cells. |
| 1606 | 8078905 | Thus, glucose-induced expression and secretion of hIAPP in transgenic mouse islets can lead to formation of amyloid fibrils similar to that found in non-insulin-dependent diabetes mellitus. |
| 1607 | 8078905 | Intra- and extracellular amyloid fibrils are formed in cultured pancreatic islets of transgenic mice expressing human islet amyloid polypeptide. |
| 1608 | 8078905 | Islet amyloid polypeptide (IAPP) is the constituent peptide of amyloid deposits found in the islets of non-insulin-dependent diabetic patients. |
| 1609 | 8078905 | Formation of islet amyloid is associated with a progressive destruction of insulin-producing beta cells. |
| 1610 | 8078905 | Thus, glucose-induced expression and secretion of hIAPP in transgenic mouse islets can lead to formation of amyloid fibrils similar to that found in non-insulin-dependent diabetes mellitus. |
| 1611 | 8078905 | Intra- and extracellular amyloid fibrils are formed in cultured pancreatic islets of transgenic mice expressing human islet amyloid polypeptide. |
| 1612 | 8078905 | Islet amyloid polypeptide (IAPP) is the constituent peptide of amyloid deposits found in the islets of non-insulin-dependent diabetic patients. |
| 1613 | 8078905 | Formation of islet amyloid is associated with a progressive destruction of insulin-producing beta cells. |
| 1614 | 8078905 | Thus, glucose-induced expression and secretion of hIAPP in transgenic mouse islets can lead to formation of amyloid fibrils similar to that found in non-insulin-dependent diabetes mellitus. |
| 1615 | 8111613 | In both species, amyloid deposition occurs in pancreatic islets and is derived from the newly discovered pancreatic hormone islet amyloid polypeptide (IAPP), or amylin. |
| 1616 | 8111613 | Amylin also reduces insulin secretion and induces insulin resistance. |
| 1617 | 8163061 | The biological role of islet amyloid polypeptide (amylin) in diabetes: some recent results. |
| 1618 | 8168639 | Human islet amyloid polypeptide accumulates at similar sites in islets of transgenic mice and humans. |
| 1619 | 8168639 | The cellular mechanisms responsible for conversion of islet amyloid polypeptide (IAPP) into insoluble amyloid deposits in non-insulin-dependent diabetes mellitus (NIDDM) are not clear. |
| 1620 | 8168639 | Human islet amyloid polypeptide accumulates at similar sites in islets of transgenic mice and humans. |
| 1621 | 8168639 | The cellular mechanisms responsible for conversion of islet amyloid polypeptide (IAPP) into insoluble amyloid deposits in non-insulin-dependent diabetes mellitus (NIDDM) are not clear. |
| 1622 | 8200302 | Islet amyloid polypeptide gene: no evidence of abnormal promoter region in thirty-five type 2 diabetic patients. |
| 1623 | 8200302 | Aberrant expression of the IAPP gene may be involved in the pathogenesis and islet amyloid formation of type 2 (non-insulin dependent) diabetes mellitus. |
| 1624 | 8200302 | Islet amyloid polypeptide gene: no evidence of abnormal promoter region in thirty-five type 2 diabetic patients. |
| 1625 | 8200302 | Aberrant expression of the IAPP gene may be involved in the pathogenesis and islet amyloid formation of type 2 (non-insulin dependent) diabetes mellitus. |
| 1626 | 8201968 | This relative hypersecretion of amylin is thought to provide an important insight into how amylin aggregates to form islet amyloid deposits in non-insulin-dependent diabetes mellitus (NIDDM). |
| 1627 | 8204973 | Islet amyloid polypeptide (IAPP/amylin) in non-insulin-dependent diabetes mellitus. |
| 1628 | 8210295 | These could include 'defects' in islet cell function: examples could be mutations in the glucokinase gene and the genetic factors leading to amyloid deposition. |
| 1629 | 8212454 | Islet amyloid polypeptide: a review of its biology and potential roles in the pathogenesis of diabetes mellitus. |
| 1630 | 8212454 | Islet amyloid polypeptide (IAPP) is a recently discovered polypeptide that is the principal constituent of IA in human beings, cats, and macaques. |
| 1631 | 8212454 | Islet amyloid polypeptide: a review of its biology and potential roles in the pathogenesis of diabetes mellitus. |
| 1632 | 8212454 | Islet amyloid polypeptide (IAPP) is a recently discovered polypeptide that is the principal constituent of IA in human beings, cats, and macaques. |
| 1633 | 8239277 | A new hypothesis for the mechanism of amyloid toxicity, based on the calcium channel activity of amyloid beta protein (A beta P) in phospholipid bilayer membranes. |
| 1634 | 8245641 | [Islet amyloid polypeptide and diabetes mellitus]. |
| 1635 | 8277951 | Islet amyloid polypeptide in patients with pancreatic cancer and diabetes. |
| 1636 | 8288058 | Islet amyloid polypeptide in human insulinomas. |
| 1637 | 8288058 | Amyloid deposits that characteristically form in the pancreatic islets of patients with non-insulin-dependent diabetes mellitus (NIDDM) and in insulinomas are both derived from islet amyloid polypeptide (IAPP). |
| 1638 | 8288058 | Ubiquitin immunoreactivity also was observed as punctate intracellular labeling and within large extracellular amyloid deposits. |
| 1639 | 8288058 | Islet amyloid polypeptide in human insulinomas. |
| 1640 | 8288058 | Amyloid deposits that characteristically form in the pancreatic islets of patients with non-insulin-dependent diabetes mellitus (NIDDM) and in insulinomas are both derived from islet amyloid polypeptide (IAPP). |
| 1641 | 8288058 | Ubiquitin immunoreactivity also was observed as punctate intracellular labeling and within large extracellular amyloid deposits. |
| 1642 | 8288058 | Islet amyloid polypeptide in human insulinomas. |
| 1643 | 8288058 | Amyloid deposits that characteristically form in the pancreatic islets of patients with non-insulin-dependent diabetes mellitus (NIDDM) and in insulinomas are both derived from islet amyloid polypeptide (IAPP). |
| 1644 | 8288058 | Ubiquitin immunoreactivity also was observed as punctate intracellular labeling and within large extracellular amyloid deposits. |
| 1645 | 8304912 | Alternatively, in the development of diabetes, the genetic basis for insulin resistance may be necessary, but not sufficient, requiring a second major gene for beta-cell vulnerability (e.g. exhaustion, deterioration of function, amyloid deposition). |
| 1646 | 8305633 | Calcitonin gene-related peptide (CGRP) shares about 46% and 20% amino acid sequence homology with islet amyloid polypeptide (IAPP) and salmon calcitonin (sCT). |
| 1647 | 8305633 | The non-amidated form of hIAPP; human diabetes-associated peptide (hDAP) did not inhibit the binding of 125I-[His]hCGRP I and sCT was only effective at a high concentration (1 microM). |
| 1648 | 8305633 | Human CGRP I and cCGRP at 2.5 microM did not stimulate the activity of hamster insulinoma cell membranes adenylate cyclase, while glucagon (1 microM) induced a 2-fold increase. |
| 1649 | 8305633 | These results and the observation that cCGRP and hCGRP I did not influence adenylate cyclase activity provide further evidence for CGRP receptor subtypes. |
| 1650 | 8307253 | Chronic overproduction of islet amyloid polypeptide/amylin in transgenic mice: lysosomal localization of human islet amyloid polypeptide and lack of marked hyperglycaemia or hyperinsulinaemia. |
| 1651 | 8307253 | Type 2 (non-insulin-dependent) diabetes mellitus is characterised by hyperglycaemia, peripheral insulin resistance, impaired insulin secretion and pancreatic islet amyloid formation. |
| 1652 | 8307253 | The major constituent of islet amyloid is islet amyloid polypeptide (amylin). |
| 1653 | 8307253 | Islet amyloid polypeptide is synthesized by islet beta cells and co-secreted with insulin. |
| 1654 | 8307253 | The ability of islet amyloid polypeptide to form amyloid fibrils is related to its species-specific amino acid sequence. |
| 1655 | 8307253 | Pharmacological doses of islet amyloid polypeptide have been shown to inhibit insulin secretion as well as insulin action on peripheral tissues (insulin resistance). |
| 1656 | 8307253 | To examine the role of islet amyloid polypeptide in the pathogenesis of Type 2 diabetes, we have generated transgenic mice with the gene encoding either human islet amyloid polypeptide (which can form amyloid) or rat islet amyloid polypeptide, under control of an insulin promoter. |
| 1657 | 8307253 | Transgenic islet amyloid polypeptide mRNA was detected in the pancreas in all transgenic mice. |
| 1658 | 8307253 | Plasma islet amyloid polypeptide levels were significantly elevated (up to 15-fold) in three out of five transgenic lines, but elevated glucose levels, hyperinsulinaemia and obesity were not observed. |
| 1659 | 8307253 | This suggests that insulin resistance is not induced by chronic hypersecretion of islet amyloid polypeptide. |
| 1660 | 8307253 | Islet amyloid polypeptide immunoreactivity was localized to beta-cell secretory granules in all mice. |
| 1661 | 8307253 | Islet amyloid polypeptide immunoreactivity in beta-cell lysosomes was seen only in mice with the human islet amyloid polypeptide gene, as in human beta cells, and might represent an initial step in intracellular formation of amyloid fibrils. |
| 1662 | 8307253 | Chronic overproduction of islet amyloid polypeptide/amylin in transgenic mice: lysosomal localization of human islet amyloid polypeptide and lack of marked hyperglycaemia or hyperinsulinaemia. |
| 1663 | 8307253 | Type 2 (non-insulin-dependent) diabetes mellitus is characterised by hyperglycaemia, peripheral insulin resistance, impaired insulin secretion and pancreatic islet amyloid formation. |
| 1664 | 8307253 | The major constituent of islet amyloid is islet amyloid polypeptide (amylin). |
| 1665 | 8307253 | Islet amyloid polypeptide is synthesized by islet beta cells and co-secreted with insulin. |
| 1666 | 8307253 | The ability of islet amyloid polypeptide to form amyloid fibrils is related to its species-specific amino acid sequence. |
| 1667 | 8307253 | Pharmacological doses of islet amyloid polypeptide have been shown to inhibit insulin secretion as well as insulin action on peripheral tissues (insulin resistance). |
| 1668 | 8307253 | To examine the role of islet amyloid polypeptide in the pathogenesis of Type 2 diabetes, we have generated transgenic mice with the gene encoding either human islet amyloid polypeptide (which can form amyloid) or rat islet amyloid polypeptide, under control of an insulin promoter. |
| 1669 | 8307253 | Transgenic islet amyloid polypeptide mRNA was detected in the pancreas in all transgenic mice. |
| 1670 | 8307253 | Plasma islet amyloid polypeptide levels were significantly elevated (up to 15-fold) in three out of five transgenic lines, but elevated glucose levels, hyperinsulinaemia and obesity were not observed. |
| 1671 | 8307253 | This suggests that insulin resistance is not induced by chronic hypersecretion of islet amyloid polypeptide. |
| 1672 | 8307253 | Islet amyloid polypeptide immunoreactivity was localized to beta-cell secretory granules in all mice. |
| 1673 | 8307253 | Islet amyloid polypeptide immunoreactivity in beta-cell lysosomes was seen only in mice with the human islet amyloid polypeptide gene, as in human beta cells, and might represent an initial step in intracellular formation of amyloid fibrils. |
| 1674 | 8307253 | Chronic overproduction of islet amyloid polypeptide/amylin in transgenic mice: lysosomal localization of human islet amyloid polypeptide and lack of marked hyperglycaemia or hyperinsulinaemia. |
| 1675 | 8307253 | Type 2 (non-insulin-dependent) diabetes mellitus is characterised by hyperglycaemia, peripheral insulin resistance, impaired insulin secretion and pancreatic islet amyloid formation. |
| 1676 | 8307253 | The major constituent of islet amyloid is islet amyloid polypeptide (amylin). |
| 1677 | 8307253 | Islet amyloid polypeptide is synthesized by islet beta cells and co-secreted with insulin. |
| 1678 | 8307253 | The ability of islet amyloid polypeptide to form amyloid fibrils is related to its species-specific amino acid sequence. |
| 1679 | 8307253 | Pharmacological doses of islet amyloid polypeptide have been shown to inhibit insulin secretion as well as insulin action on peripheral tissues (insulin resistance). |
| 1680 | 8307253 | To examine the role of islet amyloid polypeptide in the pathogenesis of Type 2 diabetes, we have generated transgenic mice with the gene encoding either human islet amyloid polypeptide (which can form amyloid) or rat islet amyloid polypeptide, under control of an insulin promoter. |
| 1681 | 8307253 | Transgenic islet amyloid polypeptide mRNA was detected in the pancreas in all transgenic mice. |
| 1682 | 8307253 | Plasma islet amyloid polypeptide levels were significantly elevated (up to 15-fold) in three out of five transgenic lines, but elevated glucose levels, hyperinsulinaemia and obesity were not observed. |
| 1683 | 8307253 | This suggests that insulin resistance is not induced by chronic hypersecretion of islet amyloid polypeptide. |
| 1684 | 8307253 | Islet amyloid polypeptide immunoreactivity was localized to beta-cell secretory granules in all mice. |
| 1685 | 8307253 | Islet amyloid polypeptide immunoreactivity in beta-cell lysosomes was seen only in mice with the human islet amyloid polypeptide gene, as in human beta cells, and might represent an initial step in intracellular formation of amyloid fibrils. |
| 1686 | 8307253 | Chronic overproduction of islet amyloid polypeptide/amylin in transgenic mice: lysosomal localization of human islet amyloid polypeptide and lack of marked hyperglycaemia or hyperinsulinaemia. |
| 1687 | 8307253 | Type 2 (non-insulin-dependent) diabetes mellitus is characterised by hyperglycaemia, peripheral insulin resistance, impaired insulin secretion and pancreatic islet amyloid formation. |
| 1688 | 8307253 | The major constituent of islet amyloid is islet amyloid polypeptide (amylin). |
| 1689 | 8307253 | Islet amyloid polypeptide is synthesized by islet beta cells and co-secreted with insulin. |
| 1690 | 8307253 | The ability of islet amyloid polypeptide to form amyloid fibrils is related to its species-specific amino acid sequence. |
| 1691 | 8307253 | Pharmacological doses of islet amyloid polypeptide have been shown to inhibit insulin secretion as well as insulin action on peripheral tissues (insulin resistance). |
| 1692 | 8307253 | To examine the role of islet amyloid polypeptide in the pathogenesis of Type 2 diabetes, we have generated transgenic mice with the gene encoding either human islet amyloid polypeptide (which can form amyloid) or rat islet amyloid polypeptide, under control of an insulin promoter. |
| 1693 | 8307253 | Transgenic islet amyloid polypeptide mRNA was detected in the pancreas in all transgenic mice. |
| 1694 | 8307253 | Plasma islet amyloid polypeptide levels were significantly elevated (up to 15-fold) in three out of five transgenic lines, but elevated glucose levels, hyperinsulinaemia and obesity were not observed. |
| 1695 | 8307253 | This suggests that insulin resistance is not induced by chronic hypersecretion of islet amyloid polypeptide. |
| 1696 | 8307253 | Islet amyloid polypeptide immunoreactivity was localized to beta-cell secretory granules in all mice. |
| 1697 | 8307253 | Islet amyloid polypeptide immunoreactivity in beta-cell lysosomes was seen only in mice with the human islet amyloid polypeptide gene, as in human beta cells, and might represent an initial step in intracellular formation of amyloid fibrils. |
| 1698 | 8307253 | Chronic overproduction of islet amyloid polypeptide/amylin in transgenic mice: lysosomal localization of human islet amyloid polypeptide and lack of marked hyperglycaemia or hyperinsulinaemia. |
| 1699 | 8307253 | Type 2 (non-insulin-dependent) diabetes mellitus is characterised by hyperglycaemia, peripheral insulin resistance, impaired insulin secretion and pancreatic islet amyloid formation. |
| 1700 | 8307253 | The major constituent of islet amyloid is islet amyloid polypeptide (amylin). |
| 1701 | 8307253 | Islet amyloid polypeptide is synthesized by islet beta cells and co-secreted with insulin. |
| 1702 | 8307253 | The ability of islet amyloid polypeptide to form amyloid fibrils is related to its species-specific amino acid sequence. |
| 1703 | 8307253 | Pharmacological doses of islet amyloid polypeptide have been shown to inhibit insulin secretion as well as insulin action on peripheral tissues (insulin resistance). |
| 1704 | 8307253 | To examine the role of islet amyloid polypeptide in the pathogenesis of Type 2 diabetes, we have generated transgenic mice with the gene encoding either human islet amyloid polypeptide (which can form amyloid) or rat islet amyloid polypeptide, under control of an insulin promoter. |
| 1705 | 8307253 | Transgenic islet amyloid polypeptide mRNA was detected in the pancreas in all transgenic mice. |
| 1706 | 8307253 | Plasma islet amyloid polypeptide levels were significantly elevated (up to 15-fold) in three out of five transgenic lines, but elevated glucose levels, hyperinsulinaemia and obesity were not observed. |
| 1707 | 8307253 | This suggests that insulin resistance is not induced by chronic hypersecretion of islet amyloid polypeptide. |
| 1708 | 8307253 | Islet amyloid polypeptide immunoreactivity was localized to beta-cell secretory granules in all mice. |
| 1709 | 8307253 | Islet amyloid polypeptide immunoreactivity in beta-cell lysosomes was seen only in mice with the human islet amyloid polypeptide gene, as in human beta cells, and might represent an initial step in intracellular formation of amyloid fibrils. |
| 1710 | 8307253 | Chronic overproduction of islet amyloid polypeptide/amylin in transgenic mice: lysosomal localization of human islet amyloid polypeptide and lack of marked hyperglycaemia or hyperinsulinaemia. |
| 1711 | 8307253 | Type 2 (non-insulin-dependent) diabetes mellitus is characterised by hyperglycaemia, peripheral insulin resistance, impaired insulin secretion and pancreatic islet amyloid formation. |
| 1712 | 8307253 | The major constituent of islet amyloid is islet amyloid polypeptide (amylin). |
| 1713 | 8307253 | Islet amyloid polypeptide is synthesized by islet beta cells and co-secreted with insulin. |
| 1714 | 8307253 | The ability of islet amyloid polypeptide to form amyloid fibrils is related to its species-specific amino acid sequence. |
| 1715 | 8307253 | Pharmacological doses of islet amyloid polypeptide have been shown to inhibit insulin secretion as well as insulin action on peripheral tissues (insulin resistance). |
| 1716 | 8307253 | To examine the role of islet amyloid polypeptide in the pathogenesis of Type 2 diabetes, we have generated transgenic mice with the gene encoding either human islet amyloid polypeptide (which can form amyloid) or rat islet amyloid polypeptide, under control of an insulin promoter. |
| 1717 | 8307253 | Transgenic islet amyloid polypeptide mRNA was detected in the pancreas in all transgenic mice. |
| 1718 | 8307253 | Plasma islet amyloid polypeptide levels were significantly elevated (up to 15-fold) in three out of five transgenic lines, but elevated glucose levels, hyperinsulinaemia and obesity were not observed. |
| 1719 | 8307253 | This suggests that insulin resistance is not induced by chronic hypersecretion of islet amyloid polypeptide. |
| 1720 | 8307253 | Islet amyloid polypeptide immunoreactivity was localized to beta-cell secretory granules in all mice. |
| 1721 | 8307253 | Islet amyloid polypeptide immunoreactivity in beta-cell lysosomes was seen only in mice with the human islet amyloid polypeptide gene, as in human beta cells, and might represent an initial step in intracellular formation of amyloid fibrils. |
| 1722 | 8307253 | Chronic overproduction of islet amyloid polypeptide/amylin in transgenic mice: lysosomal localization of human islet amyloid polypeptide and lack of marked hyperglycaemia or hyperinsulinaemia. |
| 1723 | 8307253 | Type 2 (non-insulin-dependent) diabetes mellitus is characterised by hyperglycaemia, peripheral insulin resistance, impaired insulin secretion and pancreatic islet amyloid formation. |
| 1724 | 8307253 | The major constituent of islet amyloid is islet amyloid polypeptide (amylin). |
| 1725 | 8307253 | Islet amyloid polypeptide is synthesized by islet beta cells and co-secreted with insulin. |
| 1726 | 8307253 | The ability of islet amyloid polypeptide to form amyloid fibrils is related to its species-specific amino acid sequence. |
| 1727 | 8307253 | Pharmacological doses of islet amyloid polypeptide have been shown to inhibit insulin secretion as well as insulin action on peripheral tissues (insulin resistance). |
| 1728 | 8307253 | To examine the role of islet amyloid polypeptide in the pathogenesis of Type 2 diabetes, we have generated transgenic mice with the gene encoding either human islet amyloid polypeptide (which can form amyloid) or rat islet amyloid polypeptide, under control of an insulin promoter. |
| 1729 | 8307253 | Transgenic islet amyloid polypeptide mRNA was detected in the pancreas in all transgenic mice. |
| 1730 | 8307253 | Plasma islet amyloid polypeptide levels were significantly elevated (up to 15-fold) in three out of five transgenic lines, but elevated glucose levels, hyperinsulinaemia and obesity were not observed. |
| 1731 | 8307253 | This suggests that insulin resistance is not induced by chronic hypersecretion of islet amyloid polypeptide. |
| 1732 | 8307253 | Islet amyloid polypeptide immunoreactivity was localized to beta-cell secretory granules in all mice. |
| 1733 | 8307253 | Islet amyloid polypeptide immunoreactivity in beta-cell lysosomes was seen only in mice with the human islet amyloid polypeptide gene, as in human beta cells, and might represent an initial step in intracellular formation of amyloid fibrils. |
| 1734 | 8307253 | Chronic overproduction of islet amyloid polypeptide/amylin in transgenic mice: lysosomal localization of human islet amyloid polypeptide and lack of marked hyperglycaemia or hyperinsulinaemia. |
| 1735 | 8307253 | Type 2 (non-insulin-dependent) diabetes mellitus is characterised by hyperglycaemia, peripheral insulin resistance, impaired insulin secretion and pancreatic islet amyloid formation. |
| 1736 | 8307253 | The major constituent of islet amyloid is islet amyloid polypeptide (amylin). |
| 1737 | 8307253 | Islet amyloid polypeptide is synthesized by islet beta cells and co-secreted with insulin. |
| 1738 | 8307253 | The ability of islet amyloid polypeptide to form amyloid fibrils is related to its species-specific amino acid sequence. |
| 1739 | 8307253 | Pharmacological doses of islet amyloid polypeptide have been shown to inhibit insulin secretion as well as insulin action on peripheral tissues (insulin resistance). |
| 1740 | 8307253 | To examine the role of islet amyloid polypeptide in the pathogenesis of Type 2 diabetes, we have generated transgenic mice with the gene encoding either human islet amyloid polypeptide (which can form amyloid) or rat islet amyloid polypeptide, under control of an insulin promoter. |
| 1741 | 8307253 | Transgenic islet amyloid polypeptide mRNA was detected in the pancreas in all transgenic mice. |
| 1742 | 8307253 | Plasma islet amyloid polypeptide levels were significantly elevated (up to 15-fold) in three out of five transgenic lines, but elevated glucose levels, hyperinsulinaemia and obesity were not observed. |
| 1743 | 8307253 | This suggests that insulin resistance is not induced by chronic hypersecretion of islet amyloid polypeptide. |
| 1744 | 8307253 | Islet amyloid polypeptide immunoreactivity was localized to beta-cell secretory granules in all mice. |
| 1745 | 8307253 | Islet amyloid polypeptide immunoreactivity in beta-cell lysosomes was seen only in mice with the human islet amyloid polypeptide gene, as in human beta cells, and might represent an initial step in intracellular formation of amyloid fibrils. |
| 1746 | 8307253 | Chronic overproduction of islet amyloid polypeptide/amylin in transgenic mice: lysosomal localization of human islet amyloid polypeptide and lack of marked hyperglycaemia or hyperinsulinaemia. |
| 1747 | 8307253 | Type 2 (non-insulin-dependent) diabetes mellitus is characterised by hyperglycaemia, peripheral insulin resistance, impaired insulin secretion and pancreatic islet amyloid formation. |
| 1748 | 8307253 | The major constituent of islet amyloid is islet amyloid polypeptide (amylin). |
| 1749 | 8307253 | Islet amyloid polypeptide is synthesized by islet beta cells and co-secreted with insulin. |
| 1750 | 8307253 | The ability of islet amyloid polypeptide to form amyloid fibrils is related to its species-specific amino acid sequence. |
| 1751 | 8307253 | Pharmacological doses of islet amyloid polypeptide have been shown to inhibit insulin secretion as well as insulin action on peripheral tissues (insulin resistance). |
| 1752 | 8307253 | To examine the role of islet amyloid polypeptide in the pathogenesis of Type 2 diabetes, we have generated transgenic mice with the gene encoding either human islet amyloid polypeptide (which can form amyloid) or rat islet amyloid polypeptide, under control of an insulin promoter. |
| 1753 | 8307253 | Transgenic islet amyloid polypeptide mRNA was detected in the pancreas in all transgenic mice. |
| 1754 | 8307253 | Plasma islet amyloid polypeptide levels were significantly elevated (up to 15-fold) in three out of five transgenic lines, but elevated glucose levels, hyperinsulinaemia and obesity were not observed. |
| 1755 | 8307253 | This suggests that insulin resistance is not induced by chronic hypersecretion of islet amyloid polypeptide. |
| 1756 | 8307253 | Islet amyloid polypeptide immunoreactivity was localized to beta-cell secretory granules in all mice. |
| 1757 | 8307253 | Islet amyloid polypeptide immunoreactivity in beta-cell lysosomes was seen only in mice with the human islet amyloid polypeptide gene, as in human beta cells, and might represent an initial step in intracellular formation of amyloid fibrils. |
| 1758 | 8307253 | Chronic overproduction of islet amyloid polypeptide/amylin in transgenic mice: lysosomal localization of human islet amyloid polypeptide and lack of marked hyperglycaemia or hyperinsulinaemia. |
| 1759 | 8307253 | Type 2 (non-insulin-dependent) diabetes mellitus is characterised by hyperglycaemia, peripheral insulin resistance, impaired insulin secretion and pancreatic islet amyloid formation. |
| 1760 | 8307253 | The major constituent of islet amyloid is islet amyloid polypeptide (amylin). |
| 1761 | 8307253 | Islet amyloid polypeptide is synthesized by islet beta cells and co-secreted with insulin. |
| 1762 | 8307253 | The ability of islet amyloid polypeptide to form amyloid fibrils is related to its species-specific amino acid sequence. |
| 1763 | 8307253 | Pharmacological doses of islet amyloid polypeptide have been shown to inhibit insulin secretion as well as insulin action on peripheral tissues (insulin resistance). |
| 1764 | 8307253 | To examine the role of islet amyloid polypeptide in the pathogenesis of Type 2 diabetes, we have generated transgenic mice with the gene encoding either human islet amyloid polypeptide (which can form amyloid) or rat islet amyloid polypeptide, under control of an insulin promoter. |
| 1765 | 8307253 | Transgenic islet amyloid polypeptide mRNA was detected in the pancreas in all transgenic mice. |
| 1766 | 8307253 | Plasma islet amyloid polypeptide levels were significantly elevated (up to 15-fold) in three out of five transgenic lines, but elevated glucose levels, hyperinsulinaemia and obesity were not observed. |
| 1767 | 8307253 | This suggests that insulin resistance is not induced by chronic hypersecretion of islet amyloid polypeptide. |
| 1768 | 8307253 | Islet amyloid polypeptide immunoreactivity was localized to beta-cell secretory granules in all mice. |
| 1769 | 8307253 | Islet amyloid polypeptide immunoreactivity in beta-cell lysosomes was seen only in mice with the human islet amyloid polypeptide gene, as in human beta cells, and might represent an initial step in intracellular formation of amyloid fibrils. |
| 1770 | 8307253 | Chronic overproduction of islet amyloid polypeptide/amylin in transgenic mice: lysosomal localization of human islet amyloid polypeptide and lack of marked hyperglycaemia or hyperinsulinaemia. |
| 1771 | 8307253 | Type 2 (non-insulin-dependent) diabetes mellitus is characterised by hyperglycaemia, peripheral insulin resistance, impaired insulin secretion and pancreatic islet amyloid formation. |
| 1772 | 8307253 | The major constituent of islet amyloid is islet amyloid polypeptide (amylin). |
| 1773 | 8307253 | Islet amyloid polypeptide is synthesized by islet beta cells and co-secreted with insulin. |
| 1774 | 8307253 | The ability of islet amyloid polypeptide to form amyloid fibrils is related to its species-specific amino acid sequence. |
| 1775 | 8307253 | Pharmacological doses of islet amyloid polypeptide have been shown to inhibit insulin secretion as well as insulin action on peripheral tissues (insulin resistance). |
| 1776 | 8307253 | To examine the role of islet amyloid polypeptide in the pathogenesis of Type 2 diabetes, we have generated transgenic mice with the gene encoding either human islet amyloid polypeptide (which can form amyloid) or rat islet amyloid polypeptide, under control of an insulin promoter. |
| 1777 | 8307253 | Transgenic islet amyloid polypeptide mRNA was detected in the pancreas in all transgenic mice. |
| 1778 | 8307253 | Plasma islet amyloid polypeptide levels were significantly elevated (up to 15-fold) in three out of five transgenic lines, but elevated glucose levels, hyperinsulinaemia and obesity were not observed. |
| 1779 | 8307253 | This suggests that insulin resistance is not induced by chronic hypersecretion of islet amyloid polypeptide. |
| 1780 | 8307253 | Islet amyloid polypeptide immunoreactivity was localized to beta-cell secretory granules in all mice. |
| 1781 | 8307253 | Islet amyloid polypeptide immunoreactivity in beta-cell lysosomes was seen only in mice with the human islet amyloid polypeptide gene, as in human beta cells, and might represent an initial step in intracellular formation of amyloid fibrils. |
| 1782 | 8307253 | Chronic overproduction of islet amyloid polypeptide/amylin in transgenic mice: lysosomal localization of human islet amyloid polypeptide and lack of marked hyperglycaemia or hyperinsulinaemia. |
| 1783 | 8307253 | Type 2 (non-insulin-dependent) diabetes mellitus is characterised by hyperglycaemia, peripheral insulin resistance, impaired insulin secretion and pancreatic islet amyloid formation. |
| 1784 | 8307253 | The major constituent of islet amyloid is islet amyloid polypeptide (amylin). |
| 1785 | 8307253 | Islet amyloid polypeptide is synthesized by islet beta cells and co-secreted with insulin. |
| 1786 | 8307253 | The ability of islet amyloid polypeptide to form amyloid fibrils is related to its species-specific amino acid sequence. |
| 1787 | 8307253 | Pharmacological doses of islet amyloid polypeptide have been shown to inhibit insulin secretion as well as insulin action on peripheral tissues (insulin resistance). |
| 1788 | 8307253 | To examine the role of islet amyloid polypeptide in the pathogenesis of Type 2 diabetes, we have generated transgenic mice with the gene encoding either human islet amyloid polypeptide (which can form amyloid) or rat islet amyloid polypeptide, under control of an insulin promoter. |
| 1789 | 8307253 | Transgenic islet amyloid polypeptide mRNA was detected in the pancreas in all transgenic mice. |
| 1790 | 8307253 | Plasma islet amyloid polypeptide levels were significantly elevated (up to 15-fold) in three out of five transgenic lines, but elevated glucose levels, hyperinsulinaemia and obesity were not observed. |
| 1791 | 8307253 | This suggests that insulin resistance is not induced by chronic hypersecretion of islet amyloid polypeptide. |
| 1792 | 8307253 | Islet amyloid polypeptide immunoreactivity was localized to beta-cell secretory granules in all mice. |
| 1793 | 8307253 | Islet amyloid polypeptide immunoreactivity in beta-cell lysosomes was seen only in mice with the human islet amyloid polypeptide gene, as in human beta cells, and might represent an initial step in intracellular formation of amyloid fibrils. |
| 1794 | 8314019 | Pancreatic islet blood flow in the rat after administration of islet amyloid polypeptide or calcitonin gene-related peptide. |
| 1795 | 8314019 | Anesthetized male Sprague-Dawley rats (350-400 g) were injected intravenously with either 0.1, 1, 15, or 25 nmol rat islet amyloid polypeptide (IAPP), 65 or 650 pmol rat calcitonin gene-related peptide (CGRP), or saline alone. |
| 1796 | 8314019 | Pancreatic islet blood flow in the rat after administration of islet amyloid polypeptide or calcitonin gene-related peptide. |
| 1797 | 8314019 | Anesthetized male Sprague-Dawley rats (350-400 g) were injected intravenously with either 0.1, 1, 15, or 25 nmol rat islet amyloid polypeptide (IAPP), 65 or 650 pmol rat calcitonin gene-related peptide (CGRP), or saline alone. |
| 1798 | 8323756 | Islet amyloid polypeptide--hen or egg in type 2 diabetes pathogenesis? |
| 1799 | 8323756 | Islet amyloid polypeptide (IAPP or amylin) was first identified as the major peptide constituent of amyloid deposited in the islets of Langerhans in patients with type-2 diabetes mellitus or in insulinomas. |
| 1800 | 8323756 | Islet amyloid polypeptide--hen or egg in type 2 diabetes pathogenesis? |
| 1801 | 8323756 | Islet amyloid polypeptide (IAPP or amylin) was first identified as the major peptide constituent of amyloid deposited in the islets of Langerhans in patients with type-2 diabetes mellitus or in insulinomas. |
| 1802 | 8323757 | Whole-body autoradiography of 123I-labelled islet amyloid polypeptide (IAPP). |
| 1803 | 8323757 | Islet amyloid polypeptide (IAPP) in a 37 amino-acid pancreatic islet polypeptide, displaying about 50% amino-acid homology with neuropeptide calcitonin gene-related peptide (CGRP). |
| 1804 | 8323757 | Human IAPP has the ability to precipitate in the shape of amyloid in patients with type II (non-insulin dependent) diabetes but otherwise its functional or pathophysiological role is enigmatic. |
| 1805 | 8323757 | Whole-body autoradiography of 123I-labelled islet amyloid polypeptide (IAPP). |
| 1806 | 8323757 | Islet amyloid polypeptide (IAPP) in a 37 amino-acid pancreatic islet polypeptide, displaying about 50% amino-acid homology with neuropeptide calcitonin gene-related peptide (CGRP). |
| 1807 | 8323757 | Human IAPP has the ability to precipitate in the shape of amyloid in patients with type II (non-insulin dependent) diabetes but otherwise its functional or pathophysiological role is enigmatic. |
| 1808 | 8323757 | Whole-body autoradiography of 123I-labelled islet amyloid polypeptide (IAPP). |
| 1809 | 8323757 | Islet amyloid polypeptide (IAPP) in a 37 amino-acid pancreatic islet polypeptide, displaying about 50% amino-acid homology with neuropeptide calcitonin gene-related peptide (CGRP). |
| 1810 | 8323757 | Human IAPP has the ability to precipitate in the shape of amyloid in patients with type II (non-insulin dependent) diabetes but otherwise its functional or pathophysiological role is enigmatic. |
| 1811 | 8335181 | Evidence for selective release of rodent islet amyloid polypeptide through the constitutive secretory pathway. |
| 1812 | 8335181 | To determine the potential for differential release of islet amyloid polypeptide and insulin, we performed studies in rat islet monolayer cultures under conditions known to impair regulated beta-cell secretion. |
| 1813 | 8335181 | In inhibiting concentrations of epinephrine or the absence of calcium, islet amyloid polypeptide was secreted through a constitutive pathway while insulin was not. |
| 1814 | 8335181 | These findings suggest a mechanism for persistent islet amyloid polypeptide secretion and amyloid accumulation when regulated insulin release is impaired as in Type 2 (non-insulin-dependent) diabetes mellitus and insulinomas. |
| 1815 | 8335181 | Evidence for selective release of rodent islet amyloid polypeptide through the constitutive secretory pathway. |
| 1816 | 8335181 | To determine the potential for differential release of islet amyloid polypeptide and insulin, we performed studies in rat islet monolayer cultures under conditions known to impair regulated beta-cell secretion. |
| 1817 | 8335181 | In inhibiting concentrations of epinephrine or the absence of calcium, islet amyloid polypeptide was secreted through a constitutive pathway while insulin was not. |
| 1818 | 8335181 | These findings suggest a mechanism for persistent islet amyloid polypeptide secretion and amyloid accumulation when regulated insulin release is impaired as in Type 2 (non-insulin-dependent) diabetes mellitus and insulinomas. |
| 1819 | 8335181 | Evidence for selective release of rodent islet amyloid polypeptide through the constitutive secretory pathway. |
| 1820 | 8335181 | To determine the potential for differential release of islet amyloid polypeptide and insulin, we performed studies in rat islet monolayer cultures under conditions known to impair regulated beta-cell secretion. |
| 1821 | 8335181 | In inhibiting concentrations of epinephrine or the absence of calcium, islet amyloid polypeptide was secreted through a constitutive pathway while insulin was not. |
| 1822 | 8335181 | These findings suggest a mechanism for persistent islet amyloid polypeptide secretion and amyloid accumulation when regulated insulin release is impaired as in Type 2 (non-insulin-dependent) diabetes mellitus and insulinomas. |
| 1823 | 8335181 | Evidence for selective release of rodent islet amyloid polypeptide through the constitutive secretory pathway. |
| 1824 | 8335181 | To determine the potential for differential release of islet amyloid polypeptide and insulin, we performed studies in rat islet monolayer cultures under conditions known to impair regulated beta-cell secretion. |
| 1825 | 8335181 | In inhibiting concentrations of epinephrine or the absence of calcium, islet amyloid polypeptide was secreted through a constitutive pathway while insulin was not. |
| 1826 | 8335181 | These findings suggest a mechanism for persistent islet amyloid polypeptide secretion and amyloid accumulation when regulated insulin release is impaired as in Type 2 (non-insulin-dependent) diabetes mellitus and insulinomas. |
| 1827 | 8344641 | Islet amyloid polypeptide/amylin contents in pancreata increase in genetically obese and diabetic mice. |
| 1828 | 8344641 | To search for a possible relationship between islet amyloid polypeptide (IAPP)/amylin and the pathophysiology of type 2 diabetes mellitus, we examined IAPP contents in the pancreata of genetically obese and diabetic mice (C57BL/6J ob/ob and KK mice), at 24 weeks of age, using a specific radioimmunoassay. |
| 1829 | 8344641 | Islet amyloid polypeptide/amylin contents in pancreata increase in genetically obese and diabetic mice. |
| 1830 | 8344641 | To search for a possible relationship between islet amyloid polypeptide (IAPP)/amylin and the pathophysiology of type 2 diabetes mellitus, we examined IAPP contents in the pancreata of genetically obese and diabetic mice (C57BL/6J ob/ob and KK mice), at 24 weeks of age, using a specific radioimmunoassay. |
| 1831 | 8345041 | The ability of TTR to form amyloid fibrils does not appear to be related to its affinity for T4. |
| 1832 | 8375592 | Regulation of islet amyloid polypeptide in human pancreatic islets. |
| 1833 | 8375592 | This study investigated the effect of glucose on islet amyloid polypeptide secretion, content, and mRNA synthesis of human pancreatic islets. |
| 1834 | 8375592 | The release of islet amyloid polypeptide from fresh isolated islets in response to glucose was parallel to that of insulin. |
| 1835 | 8375592 | The islet amyloid polypeptide-to-insulin molar ratios in response to 5.5 and 16.7 mM glucose were 1:16 and 1:15 respectively. |
| 1836 | 8375592 | The islet amyloid polypeptide response to the 1-day culture was similar to that of the fresh islets; however, after the 7-day culture the islet amyloid polypeptide and insulin secretory responses to glucose were dissociated. |
| 1837 | 8375592 | The insulin response of islets to a high-glucose stimulus was significantly (P < 0.001) increased, whereas the islet amyloid polypeptide response of islets to the same stimulus was blunted. |
| 1838 | 8375592 | Quantification of both signals by densitometry showed a greater increase for islet amyloid polypeptide than for insulin. |
| 1839 | 8375592 | Regulation of islet amyloid polypeptide in human pancreatic islets. |
| 1840 | 8375592 | This study investigated the effect of glucose on islet amyloid polypeptide secretion, content, and mRNA synthesis of human pancreatic islets. |
| 1841 | 8375592 | The release of islet amyloid polypeptide from fresh isolated islets in response to glucose was parallel to that of insulin. |
| 1842 | 8375592 | The islet amyloid polypeptide-to-insulin molar ratios in response to 5.5 and 16.7 mM glucose were 1:16 and 1:15 respectively. |
| 1843 | 8375592 | The islet amyloid polypeptide response to the 1-day culture was similar to that of the fresh islets; however, after the 7-day culture the islet amyloid polypeptide and insulin secretory responses to glucose were dissociated. |
| 1844 | 8375592 | The insulin response of islets to a high-glucose stimulus was significantly (P < 0.001) increased, whereas the islet amyloid polypeptide response of islets to the same stimulus was blunted. |
| 1845 | 8375592 | Quantification of both signals by densitometry showed a greater increase for islet amyloid polypeptide than for insulin. |
| 1846 | 8375592 | Regulation of islet amyloid polypeptide in human pancreatic islets. |
| 1847 | 8375592 | This study investigated the effect of glucose on islet amyloid polypeptide secretion, content, and mRNA synthesis of human pancreatic islets. |
| 1848 | 8375592 | The release of islet amyloid polypeptide from fresh isolated islets in response to glucose was parallel to that of insulin. |
| 1849 | 8375592 | The islet amyloid polypeptide-to-insulin molar ratios in response to 5.5 and 16.7 mM glucose were 1:16 and 1:15 respectively. |
| 1850 | 8375592 | The islet amyloid polypeptide response to the 1-day culture was similar to that of the fresh islets; however, after the 7-day culture the islet amyloid polypeptide and insulin secretory responses to glucose were dissociated. |
| 1851 | 8375592 | The insulin response of islets to a high-glucose stimulus was significantly (P < 0.001) increased, whereas the islet amyloid polypeptide response of islets to the same stimulus was blunted. |
| 1852 | 8375592 | Quantification of both signals by densitometry showed a greater increase for islet amyloid polypeptide than for insulin. |
| 1853 | 8375592 | Regulation of islet amyloid polypeptide in human pancreatic islets. |
| 1854 | 8375592 | This study investigated the effect of glucose on islet amyloid polypeptide secretion, content, and mRNA synthesis of human pancreatic islets. |
| 1855 | 8375592 | The release of islet amyloid polypeptide from fresh isolated islets in response to glucose was parallel to that of insulin. |
| 1856 | 8375592 | The islet amyloid polypeptide-to-insulin molar ratios in response to 5.5 and 16.7 mM glucose were 1:16 and 1:15 respectively. |
| 1857 | 8375592 | The islet amyloid polypeptide response to the 1-day culture was similar to that of the fresh islets; however, after the 7-day culture the islet amyloid polypeptide and insulin secretory responses to glucose were dissociated. |
| 1858 | 8375592 | The insulin response of islets to a high-glucose stimulus was significantly (P < 0.001) increased, whereas the islet amyloid polypeptide response of islets to the same stimulus was blunted. |
| 1859 | 8375592 | Quantification of both signals by densitometry showed a greater increase for islet amyloid polypeptide than for insulin. |
| 1860 | 8375592 | Regulation of islet amyloid polypeptide in human pancreatic islets. |
| 1861 | 8375592 | This study investigated the effect of glucose on islet amyloid polypeptide secretion, content, and mRNA synthesis of human pancreatic islets. |
| 1862 | 8375592 | The release of islet amyloid polypeptide from fresh isolated islets in response to glucose was parallel to that of insulin. |
| 1863 | 8375592 | The islet amyloid polypeptide-to-insulin molar ratios in response to 5.5 and 16.7 mM glucose were 1:16 and 1:15 respectively. |
| 1864 | 8375592 | The islet amyloid polypeptide response to the 1-day culture was similar to that of the fresh islets; however, after the 7-day culture the islet amyloid polypeptide and insulin secretory responses to glucose were dissociated. |
| 1865 | 8375592 | The insulin response of islets to a high-glucose stimulus was significantly (P < 0.001) increased, whereas the islet amyloid polypeptide response of islets to the same stimulus was blunted. |
| 1866 | 8375592 | Quantification of both signals by densitometry showed a greater increase for islet amyloid polypeptide than for insulin. |
| 1867 | 8375592 | Regulation of islet amyloid polypeptide in human pancreatic islets. |
| 1868 | 8375592 | This study investigated the effect of glucose on islet amyloid polypeptide secretion, content, and mRNA synthesis of human pancreatic islets. |
| 1869 | 8375592 | The release of islet amyloid polypeptide from fresh isolated islets in response to glucose was parallel to that of insulin. |
| 1870 | 8375592 | The islet amyloid polypeptide-to-insulin molar ratios in response to 5.5 and 16.7 mM glucose were 1:16 and 1:15 respectively. |
| 1871 | 8375592 | The islet amyloid polypeptide response to the 1-day culture was similar to that of the fresh islets; however, after the 7-day culture the islet amyloid polypeptide and insulin secretory responses to glucose were dissociated. |
| 1872 | 8375592 | The insulin response of islets to a high-glucose stimulus was significantly (P < 0.001) increased, whereas the islet amyloid polypeptide response of islets to the same stimulus was blunted. |
| 1873 | 8375592 | Quantification of both signals by densitometry showed a greater increase for islet amyloid polypeptide than for insulin. |
| 1874 | 8375592 | Regulation of islet amyloid polypeptide in human pancreatic islets. |
| 1875 | 8375592 | This study investigated the effect of glucose on islet amyloid polypeptide secretion, content, and mRNA synthesis of human pancreatic islets. |
| 1876 | 8375592 | The release of islet amyloid polypeptide from fresh isolated islets in response to glucose was parallel to that of insulin. |
| 1877 | 8375592 | The islet amyloid polypeptide-to-insulin molar ratios in response to 5.5 and 16.7 mM glucose were 1:16 and 1:15 respectively. |
| 1878 | 8375592 | The islet amyloid polypeptide response to the 1-day culture was similar to that of the fresh islets; however, after the 7-day culture the islet amyloid polypeptide and insulin secretory responses to glucose were dissociated. |
| 1879 | 8375592 | The insulin response of islets to a high-glucose stimulus was significantly (P < 0.001) increased, whereas the islet amyloid polypeptide response of islets to the same stimulus was blunted. |
| 1880 | 8375592 | Quantification of both signals by densitometry showed a greater increase for islet amyloid polypeptide than for insulin. |
| 1881 | 8380642 | Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum. |
| 1882 | 8405756 | Inhibition of insulin secretion, but normal peripheral insulin sensitivity, in a patient with a malignant endocrine pancreatic tumour producing high amounts of an islet amyloid polypeptide-like molecule. |
| 1883 | 8405756 | Islet amyloid polypeptide or amylin is a polypeptide secreted mainly from the pancreatic beta cells together with insulin upon stimulation. |
| 1884 | 8405756 | High levels of islet amyloid polypeptide have also been shown to increase the peripheral insulin resistance and consequently a role for islet amyloid polypeptide in the glucose homeostasis has been suggested. |
| 1885 | 8405756 | We have studied the glucose homeostasis in a patient with a malignant endocrine pancreatic tumour producing large amounts of an islet amyloid polypeptide-like molecule (about 400 times the upper reference level for islet amyloid polypeptide). |
| 1886 | 8405756 | However, culture of rat islets with normal human serum supplemented with synthetic rat islet amyloid polypeptide did not affect the glucose-stimulated insulin release. |
| 1887 | 8405756 | Inhibition of insulin secretion, but normal peripheral insulin sensitivity, in a patient with a malignant endocrine pancreatic tumour producing high amounts of an islet amyloid polypeptide-like molecule. |
| 1888 | 8405756 | Islet amyloid polypeptide or amylin is a polypeptide secreted mainly from the pancreatic beta cells together with insulin upon stimulation. |
| 1889 | 8405756 | High levels of islet amyloid polypeptide have also been shown to increase the peripheral insulin resistance and consequently a role for islet amyloid polypeptide in the glucose homeostasis has been suggested. |
| 1890 | 8405756 | We have studied the glucose homeostasis in a patient with a malignant endocrine pancreatic tumour producing large amounts of an islet amyloid polypeptide-like molecule (about 400 times the upper reference level for islet amyloid polypeptide). |
| 1891 | 8405756 | However, culture of rat islets with normal human serum supplemented with synthetic rat islet amyloid polypeptide did not affect the glucose-stimulated insulin release. |
| 1892 | 8405756 | Inhibition of insulin secretion, but normal peripheral insulin sensitivity, in a patient with a malignant endocrine pancreatic tumour producing high amounts of an islet amyloid polypeptide-like molecule. |
| 1893 | 8405756 | Islet amyloid polypeptide or amylin is a polypeptide secreted mainly from the pancreatic beta cells together with insulin upon stimulation. |
| 1894 | 8405756 | High levels of islet amyloid polypeptide have also been shown to increase the peripheral insulin resistance and consequently a role for islet amyloid polypeptide in the glucose homeostasis has been suggested. |
| 1895 | 8405756 | We have studied the glucose homeostasis in a patient with a malignant endocrine pancreatic tumour producing large amounts of an islet amyloid polypeptide-like molecule (about 400 times the upper reference level for islet amyloid polypeptide). |
| 1896 | 8405756 | However, culture of rat islets with normal human serum supplemented with synthetic rat islet amyloid polypeptide did not affect the glucose-stimulated insulin release. |
| 1897 | 8405756 | Inhibition of insulin secretion, but normal peripheral insulin sensitivity, in a patient with a malignant endocrine pancreatic tumour producing high amounts of an islet amyloid polypeptide-like molecule. |
| 1898 | 8405756 | Islet amyloid polypeptide or amylin is a polypeptide secreted mainly from the pancreatic beta cells together with insulin upon stimulation. |
| 1899 | 8405756 | High levels of islet amyloid polypeptide have also been shown to increase the peripheral insulin resistance and consequently a role for islet amyloid polypeptide in the glucose homeostasis has been suggested. |
| 1900 | 8405756 | We have studied the glucose homeostasis in a patient with a malignant endocrine pancreatic tumour producing large amounts of an islet amyloid polypeptide-like molecule (about 400 times the upper reference level for islet amyloid polypeptide). |
| 1901 | 8405756 | However, culture of rat islets with normal human serum supplemented with synthetic rat islet amyloid polypeptide did not affect the glucose-stimulated insulin release. |
| 1902 | 8405756 | Inhibition of insulin secretion, but normal peripheral insulin sensitivity, in a patient with a malignant endocrine pancreatic tumour producing high amounts of an islet amyloid polypeptide-like molecule. |
| 1903 | 8405756 | Islet amyloid polypeptide or amylin is a polypeptide secreted mainly from the pancreatic beta cells together with insulin upon stimulation. |
| 1904 | 8405756 | High levels of islet amyloid polypeptide have also been shown to increase the peripheral insulin resistance and consequently a role for islet amyloid polypeptide in the glucose homeostasis has been suggested. |
| 1905 | 8405756 | We have studied the glucose homeostasis in a patient with a malignant endocrine pancreatic tumour producing large amounts of an islet amyloid polypeptide-like molecule (about 400 times the upper reference level for islet amyloid polypeptide). |
| 1906 | 8405756 | However, culture of rat islets with normal human serum supplemented with synthetic rat islet amyloid polypeptide did not affect the glucose-stimulated insulin release. |
| 1907 | 8425669 | Influence of islet amyloid polypeptide and the 8-37 fragment of islet amyloid polypeptide on insulin release from perifused rat islets. |
| 1908 | 8425669 | IAPP at 10(-7) M reduced insulin release by 32% from 7.1 (95% Cl 5.8-8.6) to 4.8 (3.0-7.5) fmol.min-1 x islet-1 (P = 0.046, n = 7). |
| 1909 | 8425669 | IAPP at 1.5 x 10(-6) M reduced insulin release by 62% from 6.5 (3.4-12.3) to 2.5 (1.4-4.4) fmol.min-1 x islet-1 (P = 0.001, n = 6). |
| 1910 | 8449286 | Formation of islet amyloid from islet amyloid polypeptide. |
| 1911 | 8460100 | Molecular form of islet amyloid polypeptide (amylin) released from isolated rat islets of Langerhans. |
| 1912 | 8460100 | Islet amyloid polypeptide (IAPP) is a 37-amino acid residue polypeptide, originally isolated from the pancreatic amyloid deposits of patients with type II diabetes mellitus. |
| 1913 | 8460100 | Molecular form of islet amyloid polypeptide (amylin) released from isolated rat islets of Langerhans. |
| 1914 | 8460100 | Islet amyloid polypeptide (IAPP) is a 37-amino acid residue polypeptide, originally isolated from the pancreatic amyloid deposits of patients with type II diabetes mellitus. |
| 1915 | 8462623 | Accumulation of amyloid over many years can lead to slowly progressive disruption of islet architecture and possibly to some of the abnormalities in insulin secretion, as found in NIDDM patients. |
| 1916 | 8477877 | Islet amyloid polypeptide: demonstration of mRNA in human pancreatic islets by in situ hybridization in islets with and without amyloid deposits. |
| 1917 | 8477877 | Islet amyloid polypeptide which is normally coexpressed with insulin in beta cells, forms amyloid deposits especially in islets of Type 2 (non-insulin-dependent) diabetic subjects. |
| 1918 | 8477877 | Occurrence of islet amyloid is paradoxically associated with loss of islet amyloid polypeptide immunoreactivity in beta cells. |
| 1919 | 8477877 | The present study was undertaken to examine whether the islet amyloid polypeptide gene is expressed in islets with decreased islet amyloid polypeptide immunoreactivity. |
| 1920 | 8477877 | Pancreatic tissue from 14 patients, 7 with Type 2 diabetes and 7 non-diabetic, were obtained at autopsy or surgery and studied for islet amyloid polypeptide expression by in situ hybridization and for presence of insulin and islet amyloid polypeptide by immunohistochemistry. |
| 1921 | 8477877 | Six of the specimens from the diabetic and three of those from the non-diabetic patients had varying degrees of islet amyloid polypeptide-derived islet amyloid. |
| 1922 | 8477877 | Amyloid deposits were associated with decreased numbers of beta cells with islet amyloid polypeptide immunoreactivity despite an apparent normal frequency of insulin-containing cells. |
| 1923 | 8477877 | This discrepancy might reflect an alteration in islet amyloid polypeptide production or processing at a transcriptional or post-transcriptional level. |
| 1924 | 8477877 | In contrast to the varying immunohistochemical patterns, islets of all categories showed strong labelling using an islet amyloid polypeptide probe for in situ hybridization. |
| 1925 | 8477877 | It is concluded that islet amyloid polypeptide production is not altered at the transcriptional level. |
| 1926 | 8477877 | The following possibilities remain: (1) islet amyloid polypeptide production may be altered at a post-transcriptional level or (2) that islet amyloid polypeptide production is normal but the reduced immunoreactivity of the cells reflects a reduced storage of IAPP in secretory granules. |
| 1927 | 8477877 | Islet amyloid polypeptide: demonstration of mRNA in human pancreatic islets by in situ hybridization in islets with and without amyloid deposits. |
| 1928 | 8477877 | Islet amyloid polypeptide which is normally coexpressed with insulin in beta cells, forms amyloid deposits especially in islets of Type 2 (non-insulin-dependent) diabetic subjects. |
| 1929 | 8477877 | Occurrence of islet amyloid is paradoxically associated with loss of islet amyloid polypeptide immunoreactivity in beta cells. |
| 1930 | 8477877 | The present study was undertaken to examine whether the islet amyloid polypeptide gene is expressed in islets with decreased islet amyloid polypeptide immunoreactivity. |
| 1931 | 8477877 | Pancreatic tissue from 14 patients, 7 with Type 2 diabetes and 7 non-diabetic, were obtained at autopsy or surgery and studied for islet amyloid polypeptide expression by in situ hybridization and for presence of insulin and islet amyloid polypeptide by immunohistochemistry. |
| 1932 | 8477877 | Six of the specimens from the diabetic and three of those from the non-diabetic patients had varying degrees of islet amyloid polypeptide-derived islet amyloid. |
| 1933 | 8477877 | Amyloid deposits were associated with decreased numbers of beta cells with islet amyloid polypeptide immunoreactivity despite an apparent normal frequency of insulin-containing cells. |
| 1934 | 8477877 | This discrepancy might reflect an alteration in islet amyloid polypeptide production or processing at a transcriptional or post-transcriptional level. |
| 1935 | 8477877 | In contrast to the varying immunohistochemical patterns, islets of all categories showed strong labelling using an islet amyloid polypeptide probe for in situ hybridization. |
| 1936 | 8477877 | It is concluded that islet amyloid polypeptide production is not altered at the transcriptional level. |
| 1937 | 8477877 | The following possibilities remain: (1) islet amyloid polypeptide production may be altered at a post-transcriptional level or (2) that islet amyloid polypeptide production is normal but the reduced immunoreactivity of the cells reflects a reduced storage of IAPP in secretory granules. |
| 1938 | 8477877 | Islet amyloid polypeptide: demonstration of mRNA in human pancreatic islets by in situ hybridization in islets with and without amyloid deposits. |
| 1939 | 8477877 | Islet amyloid polypeptide which is normally coexpressed with insulin in beta cells, forms amyloid deposits especially in islets of Type 2 (non-insulin-dependent) diabetic subjects. |
| 1940 | 8477877 | Occurrence of islet amyloid is paradoxically associated with loss of islet amyloid polypeptide immunoreactivity in beta cells. |
| 1941 | 8477877 | The present study was undertaken to examine whether the islet amyloid polypeptide gene is expressed in islets with decreased islet amyloid polypeptide immunoreactivity. |
| 1942 | 8477877 | Pancreatic tissue from 14 patients, 7 with Type 2 diabetes and 7 non-diabetic, were obtained at autopsy or surgery and studied for islet amyloid polypeptide expression by in situ hybridization and for presence of insulin and islet amyloid polypeptide by immunohistochemistry. |
| 1943 | 8477877 | Six of the specimens from the diabetic and three of those from the non-diabetic patients had varying degrees of islet amyloid polypeptide-derived islet amyloid. |
| 1944 | 8477877 | Amyloid deposits were associated with decreased numbers of beta cells with islet amyloid polypeptide immunoreactivity despite an apparent normal frequency of insulin-containing cells. |
| 1945 | 8477877 | This discrepancy might reflect an alteration in islet amyloid polypeptide production or processing at a transcriptional or post-transcriptional level. |
| 1946 | 8477877 | In contrast to the varying immunohistochemical patterns, islets of all categories showed strong labelling using an islet amyloid polypeptide probe for in situ hybridization. |
| 1947 | 8477877 | It is concluded that islet amyloid polypeptide production is not altered at the transcriptional level. |
| 1948 | 8477877 | The following possibilities remain: (1) islet amyloid polypeptide production may be altered at a post-transcriptional level or (2) that islet amyloid polypeptide production is normal but the reduced immunoreactivity of the cells reflects a reduced storage of IAPP in secretory granules. |
| 1949 | 8477877 | Islet amyloid polypeptide: demonstration of mRNA in human pancreatic islets by in situ hybridization in islets with and without amyloid deposits. |
| 1950 | 8477877 | Islet amyloid polypeptide which is normally coexpressed with insulin in beta cells, forms amyloid deposits especially in islets of Type 2 (non-insulin-dependent) diabetic subjects. |
| 1951 | 8477877 | Occurrence of islet amyloid is paradoxically associated with loss of islet amyloid polypeptide immunoreactivity in beta cells. |
| 1952 | 8477877 | The present study was undertaken to examine whether the islet amyloid polypeptide gene is expressed in islets with decreased islet amyloid polypeptide immunoreactivity. |
| 1953 | 8477877 | Pancreatic tissue from 14 patients, 7 with Type 2 diabetes and 7 non-diabetic, were obtained at autopsy or surgery and studied for islet amyloid polypeptide expression by in situ hybridization and for presence of insulin and islet amyloid polypeptide by immunohistochemistry. |
| 1954 | 8477877 | Six of the specimens from the diabetic and three of those from the non-diabetic patients had varying degrees of islet amyloid polypeptide-derived islet amyloid. |
| 1955 | 8477877 | Amyloid deposits were associated with decreased numbers of beta cells with islet amyloid polypeptide immunoreactivity despite an apparent normal frequency of insulin-containing cells. |
| 1956 | 8477877 | This discrepancy might reflect an alteration in islet amyloid polypeptide production or processing at a transcriptional or post-transcriptional level. |
| 1957 | 8477877 | In contrast to the varying immunohistochemical patterns, islets of all categories showed strong labelling using an islet amyloid polypeptide probe for in situ hybridization. |
| 1958 | 8477877 | It is concluded that islet amyloid polypeptide production is not altered at the transcriptional level. |
| 1959 | 8477877 | The following possibilities remain: (1) islet amyloid polypeptide production may be altered at a post-transcriptional level or (2) that islet amyloid polypeptide production is normal but the reduced immunoreactivity of the cells reflects a reduced storage of IAPP in secretory granules. |
| 1960 | 8477877 | Islet amyloid polypeptide: demonstration of mRNA in human pancreatic islets by in situ hybridization in islets with and without amyloid deposits. |
| 1961 | 8477877 | Islet amyloid polypeptide which is normally coexpressed with insulin in beta cells, forms amyloid deposits especially in islets of Type 2 (non-insulin-dependent) diabetic subjects. |
| 1962 | 8477877 | Occurrence of islet amyloid is paradoxically associated with loss of islet amyloid polypeptide immunoreactivity in beta cells. |
| 1963 | 8477877 | The present study was undertaken to examine whether the islet amyloid polypeptide gene is expressed in islets with decreased islet amyloid polypeptide immunoreactivity. |
| 1964 | 8477877 | Pancreatic tissue from 14 patients, 7 with Type 2 diabetes and 7 non-diabetic, were obtained at autopsy or surgery and studied for islet amyloid polypeptide expression by in situ hybridization and for presence of insulin and islet amyloid polypeptide by immunohistochemistry. |
| 1965 | 8477877 | Six of the specimens from the diabetic and three of those from the non-diabetic patients had varying degrees of islet amyloid polypeptide-derived islet amyloid. |
| 1966 | 8477877 | Amyloid deposits were associated with decreased numbers of beta cells with islet amyloid polypeptide immunoreactivity despite an apparent normal frequency of insulin-containing cells. |
| 1967 | 8477877 | This discrepancy might reflect an alteration in islet amyloid polypeptide production or processing at a transcriptional or post-transcriptional level. |
| 1968 | 8477877 | In contrast to the varying immunohistochemical patterns, islets of all categories showed strong labelling using an islet amyloid polypeptide probe for in situ hybridization. |
| 1969 | 8477877 | It is concluded that islet amyloid polypeptide production is not altered at the transcriptional level. |
| 1970 | 8477877 | The following possibilities remain: (1) islet amyloid polypeptide production may be altered at a post-transcriptional level or (2) that islet amyloid polypeptide production is normal but the reduced immunoreactivity of the cells reflects a reduced storage of IAPP in secretory granules. |
| 1971 | 8477877 | Islet amyloid polypeptide: demonstration of mRNA in human pancreatic islets by in situ hybridization in islets with and without amyloid deposits. |
| 1972 | 8477877 | Islet amyloid polypeptide which is normally coexpressed with insulin in beta cells, forms amyloid deposits especially in islets of Type 2 (non-insulin-dependent) diabetic subjects. |
| 1973 | 8477877 | Occurrence of islet amyloid is paradoxically associated with loss of islet amyloid polypeptide immunoreactivity in beta cells. |
| 1974 | 8477877 | The present study was undertaken to examine whether the islet amyloid polypeptide gene is expressed in islets with decreased islet amyloid polypeptide immunoreactivity. |
| 1975 | 8477877 | Pancreatic tissue from 14 patients, 7 with Type 2 diabetes and 7 non-diabetic, were obtained at autopsy or surgery and studied for islet amyloid polypeptide expression by in situ hybridization and for presence of insulin and islet amyloid polypeptide by immunohistochemistry. |
| 1976 | 8477877 | Six of the specimens from the diabetic and three of those from the non-diabetic patients had varying degrees of islet amyloid polypeptide-derived islet amyloid. |
| 1977 | 8477877 | Amyloid deposits were associated with decreased numbers of beta cells with islet amyloid polypeptide immunoreactivity despite an apparent normal frequency of insulin-containing cells. |
| 1978 | 8477877 | This discrepancy might reflect an alteration in islet amyloid polypeptide production or processing at a transcriptional or post-transcriptional level. |
| 1979 | 8477877 | In contrast to the varying immunohistochemical patterns, islets of all categories showed strong labelling using an islet amyloid polypeptide probe for in situ hybridization. |
| 1980 | 8477877 | It is concluded that islet amyloid polypeptide production is not altered at the transcriptional level. |
| 1981 | 8477877 | The following possibilities remain: (1) islet amyloid polypeptide production may be altered at a post-transcriptional level or (2) that islet amyloid polypeptide production is normal but the reduced immunoreactivity of the cells reflects a reduced storage of IAPP in secretory granules. |
| 1982 | 8477877 | Islet amyloid polypeptide: demonstration of mRNA in human pancreatic islets by in situ hybridization in islets with and without amyloid deposits. |
| 1983 | 8477877 | Islet amyloid polypeptide which is normally coexpressed with insulin in beta cells, forms amyloid deposits especially in islets of Type 2 (non-insulin-dependent) diabetic subjects. |
| 1984 | 8477877 | Occurrence of islet amyloid is paradoxically associated with loss of islet amyloid polypeptide immunoreactivity in beta cells. |
| 1985 | 8477877 | The present study was undertaken to examine whether the islet amyloid polypeptide gene is expressed in islets with decreased islet amyloid polypeptide immunoreactivity. |
| 1986 | 8477877 | Pancreatic tissue from 14 patients, 7 with Type 2 diabetes and 7 non-diabetic, were obtained at autopsy or surgery and studied for islet amyloid polypeptide expression by in situ hybridization and for presence of insulin and islet amyloid polypeptide by immunohistochemistry. |
| 1987 | 8477877 | Six of the specimens from the diabetic and three of those from the non-diabetic patients had varying degrees of islet amyloid polypeptide-derived islet amyloid. |
| 1988 | 8477877 | Amyloid deposits were associated with decreased numbers of beta cells with islet amyloid polypeptide immunoreactivity despite an apparent normal frequency of insulin-containing cells. |
| 1989 | 8477877 | This discrepancy might reflect an alteration in islet amyloid polypeptide production or processing at a transcriptional or post-transcriptional level. |
| 1990 | 8477877 | In contrast to the varying immunohistochemical patterns, islets of all categories showed strong labelling using an islet amyloid polypeptide probe for in situ hybridization. |
| 1991 | 8477877 | It is concluded that islet amyloid polypeptide production is not altered at the transcriptional level. |
| 1992 | 8477877 | The following possibilities remain: (1) islet amyloid polypeptide production may be altered at a post-transcriptional level or (2) that islet amyloid polypeptide production is normal but the reduced immunoreactivity of the cells reflects a reduced storage of IAPP in secretory granules. |
| 1993 | 8477877 | Islet amyloid polypeptide: demonstration of mRNA in human pancreatic islets by in situ hybridization in islets with and without amyloid deposits. |
| 1994 | 8477877 | Islet amyloid polypeptide which is normally coexpressed with insulin in beta cells, forms amyloid deposits especially in islets of Type 2 (non-insulin-dependent) diabetic subjects. |
| 1995 | 8477877 | Occurrence of islet amyloid is paradoxically associated with loss of islet amyloid polypeptide immunoreactivity in beta cells. |
| 1996 | 8477877 | The present study was undertaken to examine whether the islet amyloid polypeptide gene is expressed in islets with decreased islet amyloid polypeptide immunoreactivity. |
| 1997 | 8477877 | Pancreatic tissue from 14 patients, 7 with Type 2 diabetes and 7 non-diabetic, were obtained at autopsy or surgery and studied for islet amyloid polypeptide expression by in situ hybridization and for presence of insulin and islet amyloid polypeptide by immunohistochemistry. |
| 1998 | 8477877 | Six of the specimens from the diabetic and three of those from the non-diabetic patients had varying degrees of islet amyloid polypeptide-derived islet amyloid. |
| 1999 | 8477877 | Amyloid deposits were associated with decreased numbers of beta cells with islet amyloid polypeptide immunoreactivity despite an apparent normal frequency of insulin-containing cells. |
| 2000 | 8477877 | This discrepancy might reflect an alteration in islet amyloid polypeptide production or processing at a transcriptional or post-transcriptional level. |
| 2001 | 8477877 | In contrast to the varying immunohistochemical patterns, islets of all categories showed strong labelling using an islet amyloid polypeptide probe for in situ hybridization. |
| 2002 | 8477877 | It is concluded that islet amyloid polypeptide production is not altered at the transcriptional level. |
| 2003 | 8477877 | The following possibilities remain: (1) islet amyloid polypeptide production may be altered at a post-transcriptional level or (2) that islet amyloid polypeptide production is normal but the reduced immunoreactivity of the cells reflects a reduced storage of IAPP in secretory granules. |
| 2004 | 8477877 | Islet amyloid polypeptide: demonstration of mRNA in human pancreatic islets by in situ hybridization in islets with and without amyloid deposits. |
| 2005 | 8477877 | Islet amyloid polypeptide which is normally coexpressed with insulin in beta cells, forms amyloid deposits especially in islets of Type 2 (non-insulin-dependent) diabetic subjects. |
| 2006 | 8477877 | Occurrence of islet amyloid is paradoxically associated with loss of islet amyloid polypeptide immunoreactivity in beta cells. |
| 2007 | 8477877 | The present study was undertaken to examine whether the islet amyloid polypeptide gene is expressed in islets with decreased islet amyloid polypeptide immunoreactivity. |
| 2008 | 8477877 | Pancreatic tissue from 14 patients, 7 with Type 2 diabetes and 7 non-diabetic, were obtained at autopsy or surgery and studied for islet amyloid polypeptide expression by in situ hybridization and for presence of insulin and islet amyloid polypeptide by immunohistochemistry. |
| 2009 | 8477877 | Six of the specimens from the diabetic and three of those from the non-diabetic patients had varying degrees of islet amyloid polypeptide-derived islet amyloid. |
| 2010 | 8477877 | Amyloid deposits were associated with decreased numbers of beta cells with islet amyloid polypeptide immunoreactivity despite an apparent normal frequency of insulin-containing cells. |
| 2011 | 8477877 | This discrepancy might reflect an alteration in islet amyloid polypeptide production or processing at a transcriptional or post-transcriptional level. |
| 2012 | 8477877 | In contrast to the varying immunohistochemical patterns, islets of all categories showed strong labelling using an islet amyloid polypeptide probe for in situ hybridization. |
| 2013 | 8477877 | It is concluded that islet amyloid polypeptide production is not altered at the transcriptional level. |
| 2014 | 8477877 | The following possibilities remain: (1) islet amyloid polypeptide production may be altered at a post-transcriptional level or (2) that islet amyloid polypeptide production is normal but the reduced immunoreactivity of the cells reflects a reduced storage of IAPP in secretory granules. |
| 2015 | 8477877 | Islet amyloid polypeptide: demonstration of mRNA in human pancreatic islets by in situ hybridization in islets with and without amyloid deposits. |
| 2016 | 8477877 | Islet amyloid polypeptide which is normally coexpressed with insulin in beta cells, forms amyloid deposits especially in islets of Type 2 (non-insulin-dependent) diabetic subjects. |
| 2017 | 8477877 | Occurrence of islet amyloid is paradoxically associated with loss of islet amyloid polypeptide immunoreactivity in beta cells. |
| 2018 | 8477877 | The present study was undertaken to examine whether the islet amyloid polypeptide gene is expressed in islets with decreased islet amyloid polypeptide immunoreactivity. |
| 2019 | 8477877 | Pancreatic tissue from 14 patients, 7 with Type 2 diabetes and 7 non-diabetic, were obtained at autopsy or surgery and studied for islet amyloid polypeptide expression by in situ hybridization and for presence of insulin and islet amyloid polypeptide by immunohistochemistry. |
| 2020 | 8477877 | Six of the specimens from the diabetic and three of those from the non-diabetic patients had varying degrees of islet amyloid polypeptide-derived islet amyloid. |
| 2021 | 8477877 | Amyloid deposits were associated with decreased numbers of beta cells with islet amyloid polypeptide immunoreactivity despite an apparent normal frequency of insulin-containing cells. |
| 2022 | 8477877 | This discrepancy might reflect an alteration in islet amyloid polypeptide production or processing at a transcriptional or post-transcriptional level. |
| 2023 | 8477877 | In contrast to the varying immunohistochemical patterns, islets of all categories showed strong labelling using an islet amyloid polypeptide probe for in situ hybridization. |
| 2024 | 8477877 | It is concluded that islet amyloid polypeptide production is not altered at the transcriptional level. |
| 2025 | 8477877 | The following possibilities remain: (1) islet amyloid polypeptide production may be altered at a post-transcriptional level or (2) that islet amyloid polypeptide production is normal but the reduced immunoreactivity of the cells reflects a reduced storage of IAPP in secretory granules. |
| 2026 | 8477877 | Islet amyloid polypeptide: demonstration of mRNA in human pancreatic islets by in situ hybridization in islets with and without amyloid deposits. |
| 2027 | 8477877 | Islet amyloid polypeptide which is normally coexpressed with insulin in beta cells, forms amyloid deposits especially in islets of Type 2 (non-insulin-dependent) diabetic subjects. |
| 2028 | 8477877 | Occurrence of islet amyloid is paradoxically associated with loss of islet amyloid polypeptide immunoreactivity in beta cells. |
| 2029 | 8477877 | The present study was undertaken to examine whether the islet amyloid polypeptide gene is expressed in islets with decreased islet amyloid polypeptide immunoreactivity. |
| 2030 | 8477877 | Pancreatic tissue from 14 patients, 7 with Type 2 diabetes and 7 non-diabetic, were obtained at autopsy or surgery and studied for islet amyloid polypeptide expression by in situ hybridization and for presence of insulin and islet amyloid polypeptide by immunohistochemistry. |
| 2031 | 8477877 | Six of the specimens from the diabetic and three of those from the non-diabetic patients had varying degrees of islet amyloid polypeptide-derived islet amyloid. |
| 2032 | 8477877 | Amyloid deposits were associated with decreased numbers of beta cells with islet amyloid polypeptide immunoreactivity despite an apparent normal frequency of insulin-containing cells. |
| 2033 | 8477877 | This discrepancy might reflect an alteration in islet amyloid polypeptide production or processing at a transcriptional or post-transcriptional level. |
| 2034 | 8477877 | In contrast to the varying immunohistochemical patterns, islets of all categories showed strong labelling using an islet amyloid polypeptide probe for in situ hybridization. |
| 2035 | 8477877 | It is concluded that islet amyloid polypeptide production is not altered at the transcriptional level. |
| 2036 | 8477877 | The following possibilities remain: (1) islet amyloid polypeptide production may be altered at a post-transcriptional level or (2) that islet amyloid polypeptide production is normal but the reduced immunoreactivity of the cells reflects a reduced storage of IAPP in secretory granules. |
| 2037 | 8477949 | Amylin is a normal secretory protein of the pancreatic beta-cells as well as a major constituent of the islet amyloid deposits in patients with non-insulin-dependent diabetes mellitus. |
| 2038 | 8477949 | Amylin did not alter glucose-stimulated secretion of insulin but significantly inhibited arginine-stimulated secretion of insulin (control: 20.9 +/- 1.4 pmol/min; amylin group: 14.8 +/- 1.6 pmol/min, p < 0.05). |
| 2039 | 8479567 | [Islet amyloid polypeptide or amylin; breakthrough in the diagnosis and prevention of type II diabetes mellitus?]. |
| 2040 | 8483872 | Marked islet amyloid polypeptide-positive amyloid deposition: a possible cause of severely insulin-deficient diabetes mellitus with atrophied exocrine pancreas. |
| 2041 | 8483872 | Islets replaced by islet amyloid polypeptide (IAPP)-positive amyloid (IAPP-AM) amounted to 77% in the tail, 74% in the body, and 73% in the head of the pancreas. |
| 2042 | 8483872 | Marked islet amyloid polypeptide-positive amyloid deposition: a possible cause of severely insulin-deficient diabetes mellitus with atrophied exocrine pancreas. |
| 2043 | 8483872 | Islets replaced by islet amyloid polypeptide (IAPP)-positive amyloid (IAPP-AM) amounted to 77% in the tail, 74% in the body, and 73% in the head of the pancreas. |
| 2044 | 8484788 | Strong promoter activity of human and rat islet amyloid polypeptide/amylin gene constructs in mouse beta cells (beta TC 3). |
| 2045 | 8484788 | Islet amyloid polypeptide (IAPP)('amylin') is co-produced with insulin in pancreatic beta cells and is the formative polypeptide of pancreatic amyloid in patients with type 2 (non-insulin-dependent) diabetes mellitus. |
| 2046 | 8484788 | Strong promoter activity of human and rat islet amyloid polypeptide/amylin gene constructs in mouse beta cells (beta TC 3). |
| 2047 | 8484788 | Islet amyloid polypeptide (IAPP)('amylin') is co-produced with insulin in pancreatic beta cells and is the formative polypeptide of pancreatic amyloid in patients with type 2 (non-insulin-dependent) diabetes mellitus. |
| 2048 | 8495092 | Plasma concentration of islet amyloid polypeptide in healthy children and patients with insulin-dependent diabetes mellitus. |
| 2049 | 8495745 | Human islet amyloid polypeptide transgenic mice as a model of non-insulin-dependent diabetes mellitus (NIDDM). |
| 2050 | 8495745 | To model islet amyloidogenesis in NIDDM and explore the glucoregulatory role of islet amyloid polypeptide (IAPP), we have created transgenic mice containing a rat insulin-I promoter-human IAPP fusion gene. |
| 2051 | 8495745 | Human islet amyloid polypeptide transgenic mice as a model of non-insulin-dependent diabetes mellitus (NIDDM). |
| 2052 | 8495745 | To model islet amyloidogenesis in NIDDM and explore the glucoregulatory role of islet amyloid polypeptide (IAPP), we have created transgenic mice containing a rat insulin-I promoter-human IAPP fusion gene. |
| 2053 | 8508614 | Plasma concentrations of islet amyloid polypeptide after glucagon administration in type 2 diabetic patients and non-diabetic subjects. |
| 2054 | 8508614 | Islet amyloid polypeptide (IAPP) is the main constituent of pancreatic islet amyloid, observed in the pancreases from patients with Type 2 diabetes mellitus. |
| 2055 | 8508614 | Plasma concentrations of islet amyloid polypeptide after glucagon administration in type 2 diabetic patients and non-diabetic subjects. |
| 2056 | 8508614 | Islet amyloid polypeptide (IAPP) is the main constituent of pancreatic islet amyloid, observed in the pancreases from patients with Type 2 diabetes mellitus. |
| 2057 | 8513090 | The recent discovery that IAPP, or amylin, a polypeptide solubilized from the amyloid substance found in the islets of Langerhans of most type II diabetics, is secreted along with insulin by beta cells and possesses anti-insulinic effects has opened new perspectives in the etiopathogenesis of this type of diabetes. |
| 2058 | 8529120 | Amyloid formation in response to beta cell stress occurs in vitro, but not in vivo, in islets of transgenic mice expressing human islet amyloid polypeptide. |
| 2059 | 8529518 | Islet amyloid is formed from the islet amyloid polypeptide (IAPP), a normal constituent of B-cells, co-secreted with insulin. |
| 2060 | 8529518 | A mutation of the glucokinase gene in MODY leads to diminished B-cell secretion but not amyloid formation. |
| 2061 | 8529518 | Islet amyloid is formed from the islet amyloid polypeptide (IAPP), a normal constituent of B-cells, co-secreted with insulin. |
| 2062 | 8529518 | A mutation of the glucokinase gene in MODY leads to diminished B-cell secretion but not amyloid formation. |
| 2063 | 8549854 | Genes known to be highly expressed in beta-cells were represented at a high frequency, namely insulin (15 of 80 clones), islet amyloid polypeptide (8 of 80 clones), proinsulin convertase 1 (6 of 80 clones), and neuropeptide Y (2 of 80 clones). |
| 2064 | 8557106 | Processing of pro-islet amyloid polypeptide (proIAPP) by the prohormone convertase PC2. |
| 2065 | 8557106 | Islet amyloid polypeptide (IAPP), 'amylin', is the component peptide of islet amyloid formed in Type 2 diabetes. |
| 2066 | 8557106 | An in vitro translation/translocation system was used to separately examine processing of human proIAPP by the beta-cell endopeptidases PC2, PC3 or furin. |
| 2067 | 8557106 | ProIAPP was converted to mature IAPP by PC2 but there was little conversion by furin or PC3. |
| 2068 | 8557106 | Processing of pro-islet amyloid polypeptide (proIAPP) by the prohormone convertase PC2. |
| 2069 | 8557106 | Islet amyloid polypeptide (IAPP), 'amylin', is the component peptide of islet amyloid formed in Type 2 diabetes. |
| 2070 | 8557106 | An in vitro translation/translocation system was used to separately examine processing of human proIAPP by the beta-cell endopeptidases PC2, PC3 or furin. |
| 2071 | 8557106 | ProIAPP was converted to mature IAPP by PC2 but there was little conversion by furin or PC3. |
| 2072 | 8567648 | Amylin is a 37-amino acid cytotoxic constituent of amyloid deposits found in the islets of Langerhans of patients with type II diabetes. |
| 2073 | 8578004 | Amylin immunoreactivity in the rat trachea and characterization of the interaction of amylin and somatostatin on airway mucus secretion. |
| 2074 | 8578004 | It is the major component of the islet amyloid typically found in non-insulin-dependent diabetes mellitus. |
| 2075 | 8578004 | Amylin may influence airway mucus secretion by paracrine and endocrine mechanisms, and our data suggest that amylin and somatostatin belong to the increasing number of peptides that are known to influence airway function. |
| 2076 | 8593932 | Linkage studies of the islet amyloid polypeptide/amylin and liver glycogen synthase genes and NIDDM. |
| 2077 | 8593932 | We have used this approach to identify a marker for the islet amyloid polypeptide gene on chromosome 12. |
| 2078 | 8593932 | Affected sib pair studies using a simple sequence repeat DNA polymorphism physically linked to the islet amyloid polypeptide and liver glycogen synthase genes showed no evidence for linkage with NIDDM, indicating that they are not major genes contributing to NIDDM susceptibility. |
| 2079 | 8593932 | Linkage studies of the islet amyloid polypeptide/amylin and liver glycogen synthase genes and NIDDM. |
| 2080 | 8593932 | We have used this approach to identify a marker for the islet amyloid polypeptide gene on chromosome 12. |
| 2081 | 8593932 | Affected sib pair studies using a simple sequence repeat DNA polymorphism physically linked to the islet amyloid polypeptide and liver glycogen synthase genes showed no evidence for linkage with NIDDM, indicating that they are not major genes contributing to NIDDM susceptibility. |
| 2082 | 8593932 | Linkage studies of the islet amyloid polypeptide/amylin and liver glycogen synthase genes and NIDDM. |
| 2083 | 8593932 | We have used this approach to identify a marker for the islet amyloid polypeptide gene on chromosome 12. |
| 2084 | 8593932 | Affected sib pair studies using a simple sequence repeat DNA polymorphism physically linked to the islet amyloid polypeptide and liver glycogen synthase genes showed no evidence for linkage with NIDDM, indicating that they are not major genes contributing to NIDDM susceptibility. |
| 2085 | 8616529 | Increased plasma levels of islet amyloid polypeptide in patients with primary hyperparathyroidism. |
| 2086 | 8616529 | Amylin, also named islet amyloid polypeptide (IAPP), is a protein that is processed and released from pancreatic beta-cells in parallel with insulin. |
| 2087 | 8616529 | Islet amyloid polypeptide is currently studied with regard to a role for insulin resistance in non-insulin-dependent diabetes. |
| 2088 | 8616529 | Increased plasma levels of islet amyloid polypeptide in patients with primary hyperparathyroidism. |
| 2089 | 8616529 | Amylin, also named islet amyloid polypeptide (IAPP), is a protein that is processed and released from pancreatic beta-cells in parallel with insulin. |
| 2090 | 8616529 | Islet amyloid polypeptide is currently studied with regard to a role for insulin resistance in non-insulin-dependent diabetes. |
| 2091 | 8616529 | Increased plasma levels of islet amyloid polypeptide in patients with primary hyperparathyroidism. |
| 2092 | 8616529 | Amylin, also named islet amyloid polypeptide (IAPP), is a protein that is processed and released from pancreatic beta-cells in parallel with insulin. |
| 2093 | 8616529 | Islet amyloid polypeptide is currently studied with regard to a role for insulin resistance in non-insulin-dependent diabetes. |
| 2094 | 8622964 | Islet amyloid formation associated with hyperglycemia in transgenic mice with pancreatic beta cell expression of human islet amyloid polypeptide. |
| 2095 | 8622964 | Pancreatic islet amyloid deposits are a characteristic pathologic feature of non-insulin-dependent diabetes mellitus and contain islet amyloid polypeptide (IAPP; amylin). |
| 2096 | 8622964 | We used transgenic mice that express human IAPP in pancreatic beta cells to explore the potential role of islet amyloid in the pathogenesis of non-insulin-dependent diabetes mellitus. |
| 2097 | 8622964 | Islet amyloid formation associated with hyperglycemia in transgenic mice with pancreatic beta cell expression of human islet amyloid polypeptide. |
| 2098 | 8622964 | Pancreatic islet amyloid deposits are a characteristic pathologic feature of non-insulin-dependent diabetes mellitus and contain islet amyloid polypeptide (IAPP; amylin). |
| 2099 | 8622964 | We used transgenic mice that express human IAPP in pancreatic beta cells to explore the potential role of islet amyloid in the pathogenesis of non-insulin-dependent diabetes mellitus. |
| 2100 | 8622964 | Islet amyloid formation associated with hyperglycemia in transgenic mice with pancreatic beta cell expression of human islet amyloid polypeptide. |
| 2101 | 8622964 | Pancreatic islet amyloid deposits are a characteristic pathologic feature of non-insulin-dependent diabetes mellitus and contain islet amyloid polypeptide (IAPP; amylin). |
| 2102 | 8622964 | We used transgenic mice that express human IAPP in pancreatic beta cells to explore the potential role of islet amyloid in the pathogenesis of non-insulin-dependent diabetes mellitus. |
| 2103 | 8643694 | Zn2+ interaction with Alzheimer amyloid beta protein calcium channels. |
| 2104 | 8643694 | The Alzheimer disease 40-residue amyloid beta protein (AbetaP[1-40]) forms cation-selective channels across acidic phospholipid bilayer membranes with spontaneous transitions over a wide range of conductances ranging from 40 to 4000 pS. |
| 2105 | 8643694 | Zn2+ interaction with Alzheimer amyloid beta protein calcium channels. |
| 2106 | 8643694 | The Alzheimer disease 40-residue amyloid beta protein (AbetaP[1-40]) forms cation-selective channels across acidic phospholipid bilayer membranes with spontaneous transitions over a wide range of conductances ranging from 40 to 4000 pS. |
| 2107 | 8645452 | Islet amyloid in type 2 (non-insulin-dependent) diabetes. |
| 2108 | 8645452 | Islet amyloid is formed from islet amyloid polypeptide (IAPP). |
| 2109 | 8645452 | Islet amyloid in type 2 (non-insulin-dependent) diabetes. |
| 2110 | 8645452 | Islet amyloid is formed from islet amyloid polypeptide (IAPP). |
| 2111 | 8674834 | Differential expression of islet amyloid polypeptide (amylin) and insulin in experimental diabetes in rodents. |
| 2112 | 8674834 | An increased ratio of islet amyloid polypeptide (IAPP) to insulin for mRNA and peptide content in pancreatic extracts and for secretion has been observed in experimental diabetes, suggesting a differentially regulated IAPP and insulin expression. |
| 2113 | 8674834 | Differential expression of islet amyloid polypeptide (amylin) and insulin in experimental diabetes in rodents. |
| 2114 | 8674834 | An increased ratio of islet amyloid polypeptide (IAPP) to insulin for mRNA and peptide content in pancreatic extracts and for secretion has been observed in experimental diabetes, suggesting a differentially regulated IAPP and insulin expression. |
| 2115 | 8690157 | Treatment with growth hormone and dexamethasone in mice transgenic for human islet amyloid polypeptide causes islet amyloidosis and beta-cell dysfunction. |
| 2116 | 8690157 | Islet amyloid derived from islet amyloid polypeptide (IAPP) is a well-recognized feature of type II diabetes. |
| 2117 | 8690157 | In the present study, we sought to test the hypothesis that pharmacological induction of insulin resistance in a mouse transgenic (TG) for human IAPP would induce islet amyloid and beta-cell dysfunction. |
| 2118 | 8690157 | Treatment with growth hormone and dexamethasone in mice transgenic for human islet amyloid polypeptide causes islet amyloidosis and beta-cell dysfunction. |
| 2119 | 8690157 | Islet amyloid derived from islet amyloid polypeptide (IAPP) is a well-recognized feature of type II diabetes. |
| 2120 | 8690157 | In the present study, we sought to test the hypothesis that pharmacological induction of insulin resistance in a mouse transgenic (TG) for human IAPP would induce islet amyloid and beta-cell dysfunction. |
| 2121 | 8690157 | Treatment with growth hormone and dexamethasone in mice transgenic for human islet amyloid polypeptide causes islet amyloidosis and beta-cell dysfunction. |
| 2122 | 8690157 | Islet amyloid derived from islet amyloid polypeptide (IAPP) is a well-recognized feature of type II diabetes. |
| 2123 | 8690157 | In the present study, we sought to test the hypothesis that pharmacological induction of insulin resistance in a mouse transgenic (TG) for human IAPP would induce islet amyloid and beta-cell dysfunction. |
| 2124 | 8692984 | Spontaneous diabetes mellitus in transgenic mice expressing human islet amyloid polypeptide. |
| 2125 | 8692984 | The islet in non-insulin-dependent diabetes mellitus (NIDDM) is characterized by loss of beta cells and large local deposits of amyloid derived from the 37-amino acid protein, islet amyloid polypeptide (IAPP). |
| 2126 | 8692984 | Spontaneous diabetes mellitus in transgenic mice expressing human islet amyloid polypeptide. |
| 2127 | 8692984 | The islet in non-insulin-dependent diabetes mellitus (NIDDM) is characterized by loss of beta cells and large local deposits of amyloid derived from the 37-amino acid protein, islet amyloid polypeptide (IAPP). |
| 2128 | 8736810 | Islet amyloid polypeptide: actions and role in the pathogenesis of diabetes. |
| 2129 | 8740943 | Lack of islet amyloid polypeptide/amylin-immunoreactivity in urine collected from healthy volunteers after ingestion of a carbohydrate-rich meal. |
| 2130 | 8740943 | Islet amyloid polypeptide (IAPP), or amylin, is synthesized by beta cells in the islets of Langerhans of the pancreas. |
| 2131 | 8740943 | Lack of islet amyloid polypeptide/amylin-immunoreactivity in urine collected from healthy volunteers after ingestion of a carbohydrate-rich meal. |
| 2132 | 8740943 | Islet amyloid polypeptide (IAPP), or amylin, is synthesized by beta cells in the islets of Langerhans of the pancreas. |
| 2133 | 8772610 | Islet amyloidosis derived from islet amyloid polypeptide is a characteristic feature of diabetes mellitus in CF as well as type II diabetes mellitus. |
| 2134 | 8781760 | Islet amyloid polypeptide (amylin) and insulin are differentially expressed in chronic diabetes induced by streptozotocin in rats. |
| 2135 | 8781760 | Islet amyloid polypeptide (IAPP) is overexpressed relative to insulin under several experimental conditions relevant to diabetes mellitus, including the immediate phase (7 days) following induction of streptozotocin diabetes. |
| 2136 | 8781760 | Immunocytochemistry revealed that IAPP predominantly occurred in insulin cells and to a lesser extent in somatostatin cells at all treatments examined. |
| 2137 | 8781760 | An over-expression of IAPP relative to insulin may therefore be involved in diabetes pathogenesis, contributing to its metabolic perturbations, possibly through the capacity of IAPP to restrain insulin release and action and to form islet amyloid. |
| 2138 | 8781760 | Islet amyloid polypeptide (amylin) and insulin are differentially expressed in chronic diabetes induced by streptozotocin in rats. |
| 2139 | 8781760 | Islet amyloid polypeptide (IAPP) is overexpressed relative to insulin under several experimental conditions relevant to diabetes mellitus, including the immediate phase (7 days) following induction of streptozotocin diabetes. |
| 2140 | 8781760 | Immunocytochemistry revealed that IAPP predominantly occurred in insulin cells and to a lesser extent in somatostatin cells at all treatments examined. |
| 2141 | 8781760 | An over-expression of IAPP relative to insulin may therefore be involved in diabetes pathogenesis, contributing to its metabolic perturbations, possibly through the capacity of IAPP to restrain insulin release and action and to form islet amyloid. |
| 2142 | 8781760 | Islet amyloid polypeptide (amylin) and insulin are differentially expressed in chronic diabetes induced by streptozotocin in rats. |
| 2143 | 8781760 | Islet amyloid polypeptide (IAPP) is overexpressed relative to insulin under several experimental conditions relevant to diabetes mellitus, including the immediate phase (7 days) following induction of streptozotocin diabetes. |
| 2144 | 8781760 | Immunocytochemistry revealed that IAPP predominantly occurred in insulin cells and to a lesser extent in somatostatin cells at all treatments examined. |
| 2145 | 8781760 | An over-expression of IAPP relative to insulin may therefore be involved in diabetes pathogenesis, contributing to its metabolic perturbations, possibly through the capacity of IAPP to restrain insulin release and action and to form islet amyloid. |
| 2146 | 8795087 | Islet amyloid polypeptide (IAPP) secretion from pancreatic islets isolated from non-obese diabetic (NOD) mice. |
| 2147 | 8795087 | The secretion of islet amyloid polypeptide (IAPP) during the course of insulin-dependent diabetes mellitus (IDDM) is essentially unknown. |
| 2148 | 8795087 | If extrapolated to the early prediabetic phase of human IDDM, this would mean that a relative hypersecretion of insulin in relation to IAPP might occur, due to an increased secretory demand for insulin or due to an intrinsic change in the biology of the secretory cells. |
| 2149 | 8795087 | Islet amyloid polypeptide (IAPP) secretion from pancreatic islets isolated from non-obese diabetic (NOD) mice. |
| 2150 | 8795087 | The secretion of islet amyloid polypeptide (IAPP) during the course of insulin-dependent diabetes mellitus (IDDM) is essentially unknown. |
| 2151 | 8795087 | If extrapolated to the early prediabetic phase of human IDDM, this would mean that a relative hypersecretion of insulin in relation to IAPP might occur, due to an increased secretory demand for insulin or due to an intrinsic change in the biology of the secretory cells. |
| 2152 | 8845588 | These include reducing the amyloid precursor protein pool in familial amyloid polyneuropathy by liver transplantation, inhibiting nidus formation in familial Mediterranean fever by the use of colchicine, inhibiting amyloid precursor protein/heparan sulphate interaction in experimental inflammation-associated amyloidosis by the use of novel small molecule anionic sulphates and sulphonates, and the use of new analogues of doxorubicin in light chain amyloidosis to accelerate amyloid removal. |
| 2153 | 8845588 | The potential significance of local and systemic amyloid deposits is discussed in the light of new information on the genetics of Alzheimer's disease, observations made in patients receiving long term dialysis for renal failure, and the potential involvement of amyloid deposits in the pathogenesis of non-insulin-dependent diabetes mellitus. |
| 2154 | 8845588 | These include reducing the amyloid precursor protein pool in familial amyloid polyneuropathy by liver transplantation, inhibiting nidus formation in familial Mediterranean fever by the use of colchicine, inhibiting amyloid precursor protein/heparan sulphate interaction in experimental inflammation-associated amyloidosis by the use of novel small molecule anionic sulphates and sulphonates, and the use of new analogues of doxorubicin in light chain amyloidosis to accelerate amyloid removal. |
| 2155 | 8845588 | The potential significance of local and systemic amyloid deposits is discussed in the light of new information on the genetics of Alzheimer's disease, observations made in patients receiving long term dialysis for renal failure, and the potential involvement of amyloid deposits in the pathogenesis of non-insulin-dependent diabetes mellitus. |
| 2156 | 8869295 | Apolipoprotein E is associated with islet amyloid and other amyloidoses: implications for Alzheimer's disease. |
| 2157 | 8869295 | Apolipoprotein E (ApoE) has recently been proposed as an aetiological factor of Alzheimer's disease (AD): ApoE is co-localized to amyloid plaques and neurofibrillary tangles in the brain and binds to A beta-protein in vitro. |
| 2158 | 8869295 | Islet amyloid is formed from islet amyloid polypeptide (IAPP) in pancreatic islets of 90 per cent of patients with non-insulin-dependent diabetes mellitus (NIDDM) which, like AD, is an age-dependent pathology. |
| 2159 | 8869295 | The relationship of ApoE to islet amyloid and other amyloidoses is largely unknown. |
| 2160 | 8869295 | In this study, ApoE was localized by immunocytochemistry on pancreatic specimens from non-diabetic man, monkey, and mouse, and on amyloid-containing human tissues from pancreas, heart, brain, and intestine. |
| 2161 | 8869295 | All types of amyloid deposits, irrespective of the constituent peptide, site of deposition, or species, showed immunoreactivity for ApoE (ApoE-IR). |
| 2162 | 8869295 | Quantitative morphometry showed that similar proportions of islet amyloid were labelled for IAPP and ApoE in monkey islets. |
| 2163 | 8869295 | These results suggest that the association of ApoE with amyloid is non-specific for AD or to the component peptide of amyloid fibrils. |
| 2164 | 8869295 | If ApoE promotes amyloid formation, its synthesis in pancreatic islets could be important for the initiation or the development of pancreatic amyloid in NIDDM. |
| 2165 | 8869295 | Apolipoprotein E is associated with islet amyloid and other amyloidoses: implications for Alzheimer's disease. |
| 2166 | 8869295 | Apolipoprotein E (ApoE) has recently been proposed as an aetiological factor of Alzheimer's disease (AD): ApoE is co-localized to amyloid plaques and neurofibrillary tangles in the brain and binds to A beta-protein in vitro. |
| 2167 | 8869295 | Islet amyloid is formed from islet amyloid polypeptide (IAPP) in pancreatic islets of 90 per cent of patients with non-insulin-dependent diabetes mellitus (NIDDM) which, like AD, is an age-dependent pathology. |
| 2168 | 8869295 | The relationship of ApoE to islet amyloid and other amyloidoses is largely unknown. |
| 2169 | 8869295 | In this study, ApoE was localized by immunocytochemistry on pancreatic specimens from non-diabetic man, monkey, and mouse, and on amyloid-containing human tissues from pancreas, heart, brain, and intestine. |
| 2170 | 8869295 | All types of amyloid deposits, irrespective of the constituent peptide, site of deposition, or species, showed immunoreactivity for ApoE (ApoE-IR). |
| 2171 | 8869295 | Quantitative morphometry showed that similar proportions of islet amyloid were labelled for IAPP and ApoE in monkey islets. |
| 2172 | 8869295 | These results suggest that the association of ApoE with amyloid is non-specific for AD or to the component peptide of amyloid fibrils. |
| 2173 | 8869295 | If ApoE promotes amyloid formation, its synthesis in pancreatic islets could be important for the initiation or the development of pancreatic amyloid in NIDDM. |
| 2174 | 8869295 | Apolipoprotein E is associated with islet amyloid and other amyloidoses: implications for Alzheimer's disease. |
| 2175 | 8869295 | Apolipoprotein E (ApoE) has recently been proposed as an aetiological factor of Alzheimer's disease (AD): ApoE is co-localized to amyloid plaques and neurofibrillary tangles in the brain and binds to A beta-protein in vitro. |
| 2176 | 8869295 | Islet amyloid is formed from islet amyloid polypeptide (IAPP) in pancreatic islets of 90 per cent of patients with non-insulin-dependent diabetes mellitus (NIDDM) which, like AD, is an age-dependent pathology. |
| 2177 | 8869295 | The relationship of ApoE to islet amyloid and other amyloidoses is largely unknown. |
| 2178 | 8869295 | In this study, ApoE was localized by immunocytochemistry on pancreatic specimens from non-diabetic man, monkey, and mouse, and on amyloid-containing human tissues from pancreas, heart, brain, and intestine. |
| 2179 | 8869295 | All types of amyloid deposits, irrespective of the constituent peptide, site of deposition, or species, showed immunoreactivity for ApoE (ApoE-IR). |
| 2180 | 8869295 | Quantitative morphometry showed that similar proportions of islet amyloid were labelled for IAPP and ApoE in monkey islets. |
| 2181 | 8869295 | These results suggest that the association of ApoE with amyloid is non-specific for AD or to the component peptide of amyloid fibrils. |
| 2182 | 8869295 | If ApoE promotes amyloid formation, its synthesis in pancreatic islets could be important for the initiation or the development of pancreatic amyloid in NIDDM. |
| 2183 | 8869295 | Apolipoprotein E is associated with islet amyloid and other amyloidoses: implications for Alzheimer's disease. |
| 2184 | 8869295 | Apolipoprotein E (ApoE) has recently been proposed as an aetiological factor of Alzheimer's disease (AD): ApoE is co-localized to amyloid plaques and neurofibrillary tangles in the brain and binds to A beta-protein in vitro. |
| 2185 | 8869295 | Islet amyloid is formed from islet amyloid polypeptide (IAPP) in pancreatic islets of 90 per cent of patients with non-insulin-dependent diabetes mellitus (NIDDM) which, like AD, is an age-dependent pathology. |
| 2186 | 8869295 | The relationship of ApoE to islet amyloid and other amyloidoses is largely unknown. |
| 2187 | 8869295 | In this study, ApoE was localized by immunocytochemistry on pancreatic specimens from non-diabetic man, monkey, and mouse, and on amyloid-containing human tissues from pancreas, heart, brain, and intestine. |
| 2188 | 8869295 | All types of amyloid deposits, irrespective of the constituent peptide, site of deposition, or species, showed immunoreactivity for ApoE (ApoE-IR). |
| 2189 | 8869295 | Quantitative morphometry showed that similar proportions of islet amyloid were labelled for IAPP and ApoE in monkey islets. |
| 2190 | 8869295 | These results suggest that the association of ApoE with amyloid is non-specific for AD or to the component peptide of amyloid fibrils. |
| 2191 | 8869295 | If ApoE promotes amyloid formation, its synthesis in pancreatic islets could be important for the initiation or the development of pancreatic amyloid in NIDDM. |
| 2192 | 8869295 | Apolipoprotein E is associated with islet amyloid and other amyloidoses: implications for Alzheimer's disease. |
| 2193 | 8869295 | Apolipoprotein E (ApoE) has recently been proposed as an aetiological factor of Alzheimer's disease (AD): ApoE is co-localized to amyloid plaques and neurofibrillary tangles in the brain and binds to A beta-protein in vitro. |
| 2194 | 8869295 | Islet amyloid is formed from islet amyloid polypeptide (IAPP) in pancreatic islets of 90 per cent of patients with non-insulin-dependent diabetes mellitus (NIDDM) which, like AD, is an age-dependent pathology. |
| 2195 | 8869295 | The relationship of ApoE to islet amyloid and other amyloidoses is largely unknown. |
| 2196 | 8869295 | In this study, ApoE was localized by immunocytochemistry on pancreatic specimens from non-diabetic man, monkey, and mouse, and on amyloid-containing human tissues from pancreas, heart, brain, and intestine. |
| 2197 | 8869295 | All types of amyloid deposits, irrespective of the constituent peptide, site of deposition, or species, showed immunoreactivity for ApoE (ApoE-IR). |
| 2198 | 8869295 | Quantitative morphometry showed that similar proportions of islet amyloid were labelled for IAPP and ApoE in monkey islets. |
| 2199 | 8869295 | These results suggest that the association of ApoE with amyloid is non-specific for AD or to the component peptide of amyloid fibrils. |
| 2200 | 8869295 | If ApoE promotes amyloid formation, its synthesis in pancreatic islets could be important for the initiation or the development of pancreatic amyloid in NIDDM. |
| 2201 | 8869295 | Apolipoprotein E is associated with islet amyloid and other amyloidoses: implications for Alzheimer's disease. |
| 2202 | 8869295 | Apolipoprotein E (ApoE) has recently been proposed as an aetiological factor of Alzheimer's disease (AD): ApoE is co-localized to amyloid plaques and neurofibrillary tangles in the brain and binds to A beta-protein in vitro. |
| 2203 | 8869295 | Islet amyloid is formed from islet amyloid polypeptide (IAPP) in pancreatic islets of 90 per cent of patients with non-insulin-dependent diabetes mellitus (NIDDM) which, like AD, is an age-dependent pathology. |
| 2204 | 8869295 | The relationship of ApoE to islet amyloid and other amyloidoses is largely unknown. |
| 2205 | 8869295 | In this study, ApoE was localized by immunocytochemistry on pancreatic specimens from non-diabetic man, monkey, and mouse, and on amyloid-containing human tissues from pancreas, heart, brain, and intestine. |
| 2206 | 8869295 | All types of amyloid deposits, irrespective of the constituent peptide, site of deposition, or species, showed immunoreactivity for ApoE (ApoE-IR). |
| 2207 | 8869295 | Quantitative morphometry showed that similar proportions of islet amyloid were labelled for IAPP and ApoE in monkey islets. |
| 2208 | 8869295 | These results suggest that the association of ApoE with amyloid is non-specific for AD or to the component peptide of amyloid fibrils. |
| 2209 | 8869295 | If ApoE promotes amyloid formation, its synthesis in pancreatic islets could be important for the initiation or the development of pancreatic amyloid in NIDDM. |
| 2210 | 8869295 | Apolipoprotein E is associated with islet amyloid and other amyloidoses: implications for Alzheimer's disease. |
| 2211 | 8869295 | Apolipoprotein E (ApoE) has recently been proposed as an aetiological factor of Alzheimer's disease (AD): ApoE is co-localized to amyloid plaques and neurofibrillary tangles in the brain and binds to A beta-protein in vitro. |
| 2212 | 8869295 | Islet amyloid is formed from islet amyloid polypeptide (IAPP) in pancreatic islets of 90 per cent of patients with non-insulin-dependent diabetes mellitus (NIDDM) which, like AD, is an age-dependent pathology. |
| 2213 | 8869295 | The relationship of ApoE to islet amyloid and other amyloidoses is largely unknown. |
| 2214 | 8869295 | In this study, ApoE was localized by immunocytochemistry on pancreatic specimens from non-diabetic man, monkey, and mouse, and on amyloid-containing human tissues from pancreas, heart, brain, and intestine. |
| 2215 | 8869295 | All types of amyloid deposits, irrespective of the constituent peptide, site of deposition, or species, showed immunoreactivity for ApoE (ApoE-IR). |
| 2216 | 8869295 | Quantitative morphometry showed that similar proportions of islet amyloid were labelled for IAPP and ApoE in monkey islets. |
| 2217 | 8869295 | These results suggest that the association of ApoE with amyloid is non-specific for AD or to the component peptide of amyloid fibrils. |
| 2218 | 8869295 | If ApoE promotes amyloid formation, its synthesis in pancreatic islets could be important for the initiation or the development of pancreatic amyloid in NIDDM. |
| 2219 | 8869295 | Apolipoprotein E is associated with islet amyloid and other amyloidoses: implications for Alzheimer's disease. |
| 2220 | 8869295 | Apolipoprotein E (ApoE) has recently been proposed as an aetiological factor of Alzheimer's disease (AD): ApoE is co-localized to amyloid plaques and neurofibrillary tangles in the brain and binds to A beta-protein in vitro. |
| 2221 | 8869295 | Islet amyloid is formed from islet amyloid polypeptide (IAPP) in pancreatic islets of 90 per cent of patients with non-insulin-dependent diabetes mellitus (NIDDM) which, like AD, is an age-dependent pathology. |
| 2222 | 8869295 | The relationship of ApoE to islet amyloid and other amyloidoses is largely unknown. |
| 2223 | 8869295 | In this study, ApoE was localized by immunocytochemistry on pancreatic specimens from non-diabetic man, monkey, and mouse, and on amyloid-containing human tissues from pancreas, heart, brain, and intestine. |
| 2224 | 8869295 | All types of amyloid deposits, irrespective of the constituent peptide, site of deposition, or species, showed immunoreactivity for ApoE (ApoE-IR). |
| 2225 | 8869295 | Quantitative morphometry showed that similar proportions of islet amyloid were labelled for IAPP and ApoE in monkey islets. |
| 2226 | 8869295 | These results suggest that the association of ApoE with amyloid is non-specific for AD or to the component peptide of amyloid fibrils. |
| 2227 | 8869295 | If ApoE promotes amyloid formation, its synthesis in pancreatic islets could be important for the initiation or the development of pancreatic amyloid in NIDDM. |
| 2228 | 8869295 | Apolipoprotein E is associated with islet amyloid and other amyloidoses: implications for Alzheimer's disease. |
| 2229 | 8869295 | Apolipoprotein E (ApoE) has recently been proposed as an aetiological factor of Alzheimer's disease (AD): ApoE is co-localized to amyloid plaques and neurofibrillary tangles in the brain and binds to A beta-protein in vitro. |
| 2230 | 8869295 | Islet amyloid is formed from islet amyloid polypeptide (IAPP) in pancreatic islets of 90 per cent of patients with non-insulin-dependent diabetes mellitus (NIDDM) which, like AD, is an age-dependent pathology. |
| 2231 | 8869295 | The relationship of ApoE to islet amyloid and other amyloidoses is largely unknown. |
| 2232 | 8869295 | In this study, ApoE was localized by immunocytochemistry on pancreatic specimens from non-diabetic man, monkey, and mouse, and on amyloid-containing human tissues from pancreas, heart, brain, and intestine. |
| 2233 | 8869295 | All types of amyloid deposits, irrespective of the constituent peptide, site of deposition, or species, showed immunoreactivity for ApoE (ApoE-IR). |
| 2234 | 8869295 | Quantitative morphometry showed that similar proportions of islet amyloid were labelled for IAPP and ApoE in monkey islets. |
| 2235 | 8869295 | These results suggest that the association of ApoE with amyloid is non-specific for AD or to the component peptide of amyloid fibrils. |
| 2236 | 8869295 | If ApoE promotes amyloid formation, its synthesis in pancreatic islets could be important for the initiation or the development of pancreatic amyloid in NIDDM. |
| 2237 | 8877314 | Amylin, amyloid and age-related disease. |
| 2238 | 8877314 | Amylin, a 37-amino acid peptide, is cosecreted with insulin from the beta-cells of the pancreatic islets in normal response to physiological stimuli. |
| 2239 | 8877314 | It is the major protein of islet amyloid, which is usually present in the pancreases of people with non-insulin-dependent (type II) diabetes mellitus. |
| 2240 | 8877314 | Amylin elicits potent effects on carbohydrate metabolism in rodent tissues, causing insulin resistance in skeletal muscle and liver. |
| 2241 | 8877314 | Amylin, amyloid and age-related disease. |
| 2242 | 8877314 | Amylin, a 37-amino acid peptide, is cosecreted with insulin from the beta-cells of the pancreatic islets in normal response to physiological stimuli. |
| 2243 | 8877314 | It is the major protein of islet amyloid, which is usually present in the pancreases of people with non-insulin-dependent (type II) diabetes mellitus. |
| 2244 | 8877314 | Amylin elicits potent effects on carbohydrate metabolism in rodent tissues, causing insulin resistance in skeletal muscle and liver. |
| 2245 | 8884847 | Increased storage and secretion of islet amyloid polypeptide relative to insulin in the spontaneously diabetic GK rat. |
| 2246 | 8884847 | We have investigated whether a possible dysregulation of the storage and function of islet amyloid polypeptide (IAPP) in the endocrine pancreas of 4-month-old spontaneously diabetic Goto-Kakizaki (GK) rats might contribute to the impairment of glucose-induced insulin secretion previously reported in these rats. |
| 2247 | 8884847 | Increased storage and secretion of islet amyloid polypeptide relative to insulin in the spontaneously diabetic GK rat. |
| 2248 | 8884847 | We have investigated whether a possible dysregulation of the storage and function of islet amyloid polypeptide (IAPP) in the endocrine pancreas of 4-month-old spontaneously diabetic Goto-Kakizaki (GK) rats might contribute to the impairment of glucose-induced insulin secretion previously reported in these rats. |
| 2249 | 8885173 | Islet amyloid and islet amyloid polypeptide in cynomolgus macaques (Macaca fascicularis): an animal model of human non-insulin-dependent diabetes mellitus. |
| 2250 | 8885173 | In addition, the cDNA-predicted amino acid sequence for islet amyloid polypeptide (IAPP) of this species was determined. |
| 2251 | 8885173 | Islet amyloid and islet amyloid polypeptide in cynomolgus macaques (Macaca fascicularis): an animal model of human non-insulin-dependent diabetes mellitus. |
| 2252 | 8885173 | In addition, the cDNA-predicted amino acid sequence for islet amyloid polypeptide (IAPP) of this species was determined. |
| 2253 | 8894481 | Islet amyloid polypeptide (IAPP) gives rise to islet amyloid fibrils in NIDDM. |
| 2254 | 8916142 | AApoAII amyloid deposits studied in one senescence-accelerated mouse P1 (SAMP1), congenic mice that have the amyloidogenic apolipoprotein A-II of SAMP1 mice, and AKR mice all reacted with biotinylated 6D12 by formic acid pretreatment, whereas AA amyloid deposits did not react with the antibody. |
| 2255 | 8916142 | The immunoreaction with anti-apolipoprotein A-II for amyloid deposits in senile mice was approximately homogeneous in intensity; on the other hand the reaction with biotinylated 6D12 was irregular in distribution and intensity over the amyloid deposits. |
| 2256 | 8916142 | AApoAII amyloid deposits studied in one senescence-accelerated mouse P1 (SAMP1), congenic mice that have the amyloidogenic apolipoprotein A-II of SAMP1 mice, and AKR mice all reacted with biotinylated 6D12 by formic acid pretreatment, whereas AA amyloid deposits did not react with the antibody. |
| 2257 | 8916142 | The immunoreaction with anti-apolipoprotein A-II for amyloid deposits in senile mice was approximately homogeneous in intensity; on the other hand the reaction with biotinylated 6D12 was irregular in distribution and intensity over the amyloid deposits. |
| 2258 | 8918714 | It has recently been shown that beta 2-microglobulin isolated from amyloid deposits in dialysis patients is modified by advanced glycation (AGE). |
| 2259 | 8922372 | PDX-1 induces insulin and glucokinase gene expressions in alphaTC1 clone 6 cells in the presence of betacellulin. |
| 2260 | 8922372 | Among the two important transcription factors for insulin gene expression, IEF1 is present both in alpha- and beta-cells, but PDX-1/IPF1/STF-1/IDX-1, a homeodomain-containing transcription factor, is present in beta-cells but not in alpha-cells. |
| 2261 | 8922372 | The exogenous expression of PDX-1 in alphaTC1.6 cells alone could induce islet amyloid polypeptide (IAPP) mRNA expression in the cells but not the expression of insulin, glucokinase, or GLUT2 gene. |
| 2262 | 8922372 | However, when betacellulin was added to the medium, the PDX-1-expressing alphaTC1.6 cells, but not the control alphaTC1.6 cells, came to express insulin and glucokinase mRNAs. |
| 2263 | 8922372 | This did not occur with other growth factors such as epidermal growth factor, transforming growth factor alpha, and insulin-like growth factor I. |
| 2264 | 8922372 | GLUT2 mRNA remained undetectable in the PDX-1--expressing alphaTC1.6 cells. |
| 2265 | 8922372 | These observations demonstrate the potency of PDX-1 for the expression of the insulin, glucokinase, and IAPP genes and suggest that certain regulatory factors, which can partially be modified by betacellulin, also contribute to the beta-cell specificity of gene expression. |
| 2266 | 8922536 | Islet amyloid polypeptide/amylin contents in pancreas change with increasing age in genetically obese and diabetic mice. |
| 2267 | 8922536 | To search for a possible relationship between islet amyloid polypeptide (IAPP)/amylin and the pathophysiology of non-insulin-dependent (type 2) diabetes mellitus (NIDDM), we examined the changes in IAPP contents in the pancreata of genetically obese and diabetic mice (C57BL/6J ob/ob and C57BL/KsJ db/db mice). |
| 2268 | 8922536 | Islet amyloid polypeptide/amylin contents in pancreas change with increasing age in genetically obese and diabetic mice. |
| 2269 | 8922536 | To search for a possible relationship between islet amyloid polypeptide (IAPP)/amylin and the pathophysiology of non-insulin-dependent (type 2) diabetes mellitus (NIDDM), we examined the changes in IAPP contents in the pancreata of genetically obese and diabetic mice (C57BL/6J ob/ob and C57BL/KsJ db/db mice). |
| 2270 | 8997219 | Islet amyloid polypeptide and insulin gene expression are regulated in parallel by glucose in vivo in rats. |
| 2271 | 8997219 | Islet amyloid polypeptide (IAPP) is a novel amyloid-forming beta-cell hormone with putative roles in glucose metabolism and non-insulin-dependent diabetes mellitus (NIDDM) pathogenesis. |
| 2272 | 8997219 | Hence, IAPP could, by elevated local concentrations, contribute to amyloid formation and/or affect metabolism unfavorably by inhibition of insulin release and action. |
| 2273 | 8997219 | Islet amyloid polypeptide and insulin gene expression are regulated in parallel by glucose in vivo in rats. |
| 2274 | 8997219 | Islet amyloid polypeptide (IAPP) is a novel amyloid-forming beta-cell hormone with putative roles in glucose metabolism and non-insulin-dependent diabetes mellitus (NIDDM) pathogenesis. |
| 2275 | 8997219 | Hence, IAPP could, by elevated local concentrations, contribute to amyloid formation and/or affect metabolism unfavorably by inhibition of insulin release and action. |
| 2276 | 8997219 | Islet amyloid polypeptide and insulin gene expression are regulated in parallel by glucose in vivo in rats. |
| 2277 | 8997219 | Islet amyloid polypeptide (IAPP) is a novel amyloid-forming beta-cell hormone with putative roles in glucose metabolism and non-insulin-dependent diabetes mellitus (NIDDM) pathogenesis. |
| 2278 | 8997219 | Hence, IAPP could, by elevated local concentrations, contribute to amyloid formation and/or affect metabolism unfavorably by inhibition of insulin release and action. |
| 2279 | 9037136 | Biologically active human islet amyloid polypeptide/amylin in transgenic mice. |
| 2280 | 9048345 | The presence of AGE in beta 2-microglobulin-amyloid fibrils of dialysis-related amyloidosis, one of the characteristic features of which is an accelerated bone resorption around amyloid deposits, was recently demonstrated. |
| 2281 | 9071971 | Differential effect of insulin treatment on islet amyloid polypeptide (amylin) and insulin gene expression in streptozotocin-induced diabetes in rats. |
| 2282 | 9071971 | Islet amyloid polypeptide (IAPP) is a beta cell hormone, which forms islet amyloid in non-insulin-dependent diabetes mellitus and may oppose insulin action and release. |
| 2283 | 9071971 | It is therefore unlikely that insulin will protect against amyloid formation and metabolic perturbations which may arise as a consequence of IAPP overexpression. |
| 2284 | 9071971 | Differential effect of insulin treatment on islet amyloid polypeptide (amylin) and insulin gene expression in streptozotocin-induced diabetes in rats. |
| 2285 | 9071971 | Islet amyloid polypeptide (IAPP) is a beta cell hormone, which forms islet amyloid in non-insulin-dependent diabetes mellitus and may oppose insulin action and release. |
| 2286 | 9071971 | It is therefore unlikely that insulin will protect against amyloid formation and metabolic perturbations which may arise as a consequence of IAPP overexpression. |
| 2287 | 9071971 | Differential effect of insulin treatment on islet amyloid polypeptide (amylin) and insulin gene expression in streptozotocin-induced diabetes in rats. |
| 2288 | 9071971 | Islet amyloid polypeptide (IAPP) is a beta cell hormone, which forms islet amyloid in non-insulin-dependent diabetes mellitus and may oppose insulin action and release. |
| 2289 | 9071971 | It is therefore unlikely that insulin will protect against amyloid formation and metabolic perturbations which may arise as a consequence of IAPP overexpression. |
| 2290 | 9075800 | Elevated islet amyloid pancreatic polypeptide and proinsulin in lean gestational diabetes. |
| 2291 | 9075800 | Recent research indicates that islet amyloid pancreatic polypeptide (IAPP) might have a regulatory effect on beta-cell insulin processing and secretion. |
| 2292 | 9075800 | To study such interaction in more detail, IAPP secretion and kinetics and the serum concentrations of proinsulin were assessed both before and after delivery in lean pregnant women with gestational diabetes mellitus (GDM patients) in comparison to those with normal glucose tolerance (NGT) and to nonpregnant healthy lean (control) and obese insulin-resistant women during oral glucose tolerance tests. |
| 2293 | 9075800 | Pregnancy induced a more marked fourfold increase in apparent total IAPP secretion rate (TIR) (GDM patients, 172 +/- 31 pmol x 1(-1) x 3 h(-1); NGT subjects, 166 +/- 31 pmol x 1(-1) x 3 h(-1); control subjects, 40 +/- 1 pmol 1(-1) x 3 h(-1)) and a twofold rise in its fractional clearance versus control subjects (P < 0.01), whereas in GDM patients a 30% increase of IAPP secretion and a decreased clearance was found, compared with obese insulin-resistant women (TIR, 112 +/- 14 pmol x 1(-1) x 3 h(-1)). |
| 2294 | 9075800 | The increase in IAPP secretion in both pregnant groups was much higher than that of the insulin groups, resulting in a marked change of the IAPP-insulin cosecretion factor when compared with lean or obese nonpregnant women (P < 0.0005). |
| 2295 | 9075800 | After delivery, total IAPP secretion (52.4 +/- 1.5 pmol/l) was completely normalized in the GDM group, as were the clearance rate and the IAPP-insulin cosecretion factor. |
| 2296 | 9075800 | In conclusion, IAPP hypersecretion is characteristic for pregnancy and might partially decrease hyperinsulinemia in pregnancy by inhibiting insulin secretion. |
| 2297 | 9075800 | Elevated islet amyloid pancreatic polypeptide and proinsulin in lean gestational diabetes. |
| 2298 | 9075800 | Recent research indicates that islet amyloid pancreatic polypeptide (IAPP) might have a regulatory effect on beta-cell insulin processing and secretion. |
| 2299 | 9075800 | To study such interaction in more detail, IAPP secretion and kinetics and the serum concentrations of proinsulin were assessed both before and after delivery in lean pregnant women with gestational diabetes mellitus (GDM patients) in comparison to those with normal glucose tolerance (NGT) and to nonpregnant healthy lean (control) and obese insulin-resistant women during oral glucose tolerance tests. |
| 2300 | 9075800 | Pregnancy induced a more marked fourfold increase in apparent total IAPP secretion rate (TIR) (GDM patients, 172 +/- 31 pmol x 1(-1) x 3 h(-1); NGT subjects, 166 +/- 31 pmol x 1(-1) x 3 h(-1); control subjects, 40 +/- 1 pmol 1(-1) x 3 h(-1)) and a twofold rise in its fractional clearance versus control subjects (P < 0.01), whereas in GDM patients a 30% increase of IAPP secretion and a decreased clearance was found, compared with obese insulin-resistant women (TIR, 112 +/- 14 pmol x 1(-1) x 3 h(-1)). |
| 2301 | 9075800 | The increase in IAPP secretion in both pregnant groups was much higher than that of the insulin groups, resulting in a marked change of the IAPP-insulin cosecretion factor when compared with lean or obese nonpregnant women (P < 0.0005). |
| 2302 | 9075800 | After delivery, total IAPP secretion (52.4 +/- 1.5 pmol/l) was completely normalized in the GDM group, as were the clearance rate and the IAPP-insulin cosecretion factor. |
| 2303 | 9075800 | In conclusion, IAPP hypersecretion is characteristic for pregnancy and might partially decrease hyperinsulinemia in pregnancy by inhibiting insulin secretion. |
| 2304 | 9084962 | Amylin (or islet amyloid polypeptide) has been reported to have binding sites in the central nervous system and the kidney and has been shown to activate plasma renin. |
| 2305 | 9142872 | Glucose regulation of islet amyloid polypeptide gene expression in rat pancreatic islets. |
| 2306 | 9142872 | Intracellular pathways by which glucose regulates islet amyloid polypeptide (IAPP) gene expression in pancreatic islets were studied. |
| 2307 | 9142872 | Glucose regulation of islet amyloid polypeptide gene expression in rat pancreatic islets. |
| 2308 | 9142872 | Intracellular pathways by which glucose regulates islet amyloid polypeptide (IAPP) gene expression in pancreatic islets were studied. |
| 2309 | 9163857 | Pancreas-specific protein (PASP), serum amyloid A (SAA), and neopterin (NEOP) in the diagnosis of rejection after simultaneous pancreas and kidney transplantation. |
| 2310 | 9163857 | In this study, serum (S), plasma (P), and urine (U) levels of pancreas-specific protein (P-PASP, U-PASP), neopterin (S-NEOP, U-NEOP), amylase (U-AMYL), and amyloid A (SAA) were measured daily in ten type I diabetic patients following simultaneous pancreas and kidney transplantation (SPK). |
| 2311 | 9163857 | Pancreas-specific protein (PASP), serum amyloid A (SAA), and neopterin (NEOP) in the diagnosis of rejection after simultaneous pancreas and kidney transplantation. |
| 2312 | 9163857 | In this study, serum (S), plasma (P), and urine (U) levels of pancreas-specific protein (P-PASP, U-PASP), neopterin (S-NEOP, U-NEOP), amylase (U-AMYL), and amyloid A (SAA) were measured daily in ten type I diabetic patients following simultaneous pancreas and kidney transplantation (SPK). |
| 2313 | 9206985 | Both in the hamster pancreatic cancer model and in patients, the development of cancer is associated with elevated plasma levels of islet amyloid polypeptide, which may be used as a tumor marker. |
| 2314 | 9209829 | Amylin, calcitonin gene-related peptide, calcitonin, and adrenomedullin: a peptide superfamily. |
| 2315 | 9209829 | Amylin (a 37-amino-acid peptide) is generated from a gene located on chromosome 12 (thought to be an evolutionary duplication of chromosome 11) and shares 46% amino acid sequence homology with CGRP and 20% with human CT. |
| 2316 | 9209829 | Amylin is predominantly located in the beta cells of the islets of the pancreas and may be involved in the pathogenesis of type II diabetes by deposition as amyloid within the pancreas, leading to beta cell destruction. |
| 2317 | 9209829 | Adrenomedullin, a recently discovered 52-amino-acid vasoactive peptide from adrenal tissue, shares 24% homology with CGRP and is also a member of this superfamily of peptides. |
| 2318 | 9209829 | Not only does adrenomedullin (13-52) show 24% amino acid homology with CGRP, it also has a biological activity profile similar to that of CGRP.CGRP, CT, and amylin are related to the insulin gene superfamily of peptides, which may all have diverged from a common ancestral gene during evolution. |
| 2319 | 9209829 | When the crystallographic- and nuclear magnetic resonance-based molecular modeling of the three-dimensional structure of CGRP, CT, amylin, and adrenomedullin peptides and their receptors is available, it will lead to a greater understanding of the involvement of this family of peptides in pathophysiology. |
| 2320 | 9209829 | Together, CGRP, CT, amylin and adrenomedullin have overlapping biological effects owing to their structures and cross-reactivity between receptors. |
| 2321 | 9209829 | I propose that CT, CGRP, adrenomedullin, and amylin belong to a family of G-protein-coupled receptors (an "insulin superfamily" of peptides) and therefore share some of the characteristics of insulin, such as growth factor-like effects, and possible interaction at insulin receptor sites as an antagonist. |
| 2322 | 9211494 | Fasting levels of islet amyloid polypeptide (IAPP), glucagon, and somatostatin were elevated in NIRD and IRD patients. |
| 2323 | 9212313 | Effect of insulin treatment on circulating islet amyloid polypeptide in patients with NIDDM. |
| 2324 | 9212313 | The objective was to evaluate the effect of insulin treatment on circulating islet amyloid polypeptide (IAPP). |
| 2325 | 9212313 | Effect of insulin treatment on circulating islet amyloid polypeptide in patients with NIDDM. |
| 2326 | 9212313 | The objective was to evaluate the effect of insulin treatment on circulating islet amyloid polypeptide (IAPP). |
| 2327 | 9216085 | Human amylin forms fibrillar amyloid between pancreatic islet cells in patients with non-insulin-dependent (type 2) diabetes mellitus. |
| 2328 | 9221931 | Islet amyloid polypeptide and calcitonin gene-related peptide expression are down-regulated in dorsal root ganglia upon sciatic nerve transection. |
| 2329 | 9221931 | Islet amyloid polypeptide (IAPP) is structurally related to calcitonin gene-related peptide (CGRP) and has been implicated in glucose homeostasis and diabetes pathogenesis because it is expressed in insulin cells and forms amyloid in pancreatic islets from type II diabetic patients. |
| 2330 | 9221931 | Islet amyloid polypeptide and calcitonin gene-related peptide expression are down-regulated in dorsal root ganglia upon sciatic nerve transection. |
| 2331 | 9221931 | Islet amyloid polypeptide (IAPP) is structurally related to calcitonin gene-related peptide (CGRP) and has been implicated in glucose homeostasis and diabetes pathogenesis because it is expressed in insulin cells and forms amyloid in pancreatic islets from type II diabetic patients. |
| 2332 | 9230354 | Transgenic overproduction of islet amyloid polypeptide (amylin) is not sufficient for islet amyloid formation. |
| 2333 | 9230354 | Islet amyloid polypeptide forms islet amyloid deposits in non-insulin-dependent diabetes mellitus. |
| 2334 | 9230354 | We have generated transgenic mice which express human islet amyloid polypeptide in their pancreatic beta cells yet do not develop islet amyloid deposits despite producing levels of the amyloidogenic human peptide 2 - 3 fold higher than the native (mouse) peptide. |
| 2335 | 9230354 | To determine whether marked overproduction of islet amyloid polypeptide is a potential cause of islet amyloid formation, we increased expression of this transgene by producing homozygous transgenic animals and by making heterozygous mice experimentally insulin resistant with nicotinic acid. |
| 2336 | 9230354 | Pancreatic content of islet amyloid polypeptide-like immunoreactivity in homozygous and nicotinic acid-treated mice was 2-fold (25 +/- 7 fmol/microg; n = 6) and 3.5-fold (47 +/- 20 fmol/microg; n = 3) higher, respectively, than that of untreated heterozygous animals (13+/-2 fmol/microg; n = 11; both p < 0.05). |
| 2337 | 9230354 | Despite this marked increase in production of islet amyloid polypeptide, neither group of mice developed gross islet amyloid deposits even after 16 months of age. |
| 2338 | 9230354 | We conclude that overproduction of islet amyloid polypeptide, even as produced by extreme insulin resistance, is not in itself sufficient for islet amyloid formation. |
| 2339 | 9230354 | Transgenic overproduction of islet amyloid polypeptide (amylin) is not sufficient for islet amyloid formation. |
| 2340 | 9230354 | Islet amyloid polypeptide forms islet amyloid deposits in non-insulin-dependent diabetes mellitus. |
| 2341 | 9230354 | We have generated transgenic mice which express human islet amyloid polypeptide in their pancreatic beta cells yet do not develop islet amyloid deposits despite producing levels of the amyloidogenic human peptide 2 - 3 fold higher than the native (mouse) peptide. |
| 2342 | 9230354 | To determine whether marked overproduction of islet amyloid polypeptide is a potential cause of islet amyloid formation, we increased expression of this transgene by producing homozygous transgenic animals and by making heterozygous mice experimentally insulin resistant with nicotinic acid. |
| 2343 | 9230354 | Pancreatic content of islet amyloid polypeptide-like immunoreactivity in homozygous and nicotinic acid-treated mice was 2-fold (25 +/- 7 fmol/microg; n = 6) and 3.5-fold (47 +/- 20 fmol/microg; n = 3) higher, respectively, than that of untreated heterozygous animals (13+/-2 fmol/microg; n = 11; both p < 0.05). |
| 2344 | 9230354 | Despite this marked increase in production of islet amyloid polypeptide, neither group of mice developed gross islet amyloid deposits even after 16 months of age. |
| 2345 | 9230354 | We conclude that overproduction of islet amyloid polypeptide, even as produced by extreme insulin resistance, is not in itself sufficient for islet amyloid formation. |
| 2346 | 9230354 | Transgenic overproduction of islet amyloid polypeptide (amylin) is not sufficient for islet amyloid formation. |
| 2347 | 9230354 | Islet amyloid polypeptide forms islet amyloid deposits in non-insulin-dependent diabetes mellitus. |
| 2348 | 9230354 | We have generated transgenic mice which express human islet amyloid polypeptide in their pancreatic beta cells yet do not develop islet amyloid deposits despite producing levels of the amyloidogenic human peptide 2 - 3 fold higher than the native (mouse) peptide. |
| 2349 | 9230354 | To determine whether marked overproduction of islet amyloid polypeptide is a potential cause of islet amyloid formation, we increased expression of this transgene by producing homozygous transgenic animals and by making heterozygous mice experimentally insulin resistant with nicotinic acid. |
| 2350 | 9230354 | Pancreatic content of islet amyloid polypeptide-like immunoreactivity in homozygous and nicotinic acid-treated mice was 2-fold (25 +/- 7 fmol/microg; n = 6) and 3.5-fold (47 +/- 20 fmol/microg; n = 3) higher, respectively, than that of untreated heterozygous animals (13+/-2 fmol/microg; n = 11; both p < 0.05). |
| 2351 | 9230354 | Despite this marked increase in production of islet amyloid polypeptide, neither group of mice developed gross islet amyloid deposits even after 16 months of age. |
| 2352 | 9230354 | We conclude that overproduction of islet amyloid polypeptide, even as produced by extreme insulin resistance, is not in itself sufficient for islet amyloid formation. |
| 2353 | 9230354 | Transgenic overproduction of islet amyloid polypeptide (amylin) is not sufficient for islet amyloid formation. |
| 2354 | 9230354 | Islet amyloid polypeptide forms islet amyloid deposits in non-insulin-dependent diabetes mellitus. |
| 2355 | 9230354 | We have generated transgenic mice which express human islet amyloid polypeptide in their pancreatic beta cells yet do not develop islet amyloid deposits despite producing levels of the amyloidogenic human peptide 2 - 3 fold higher than the native (mouse) peptide. |
| 2356 | 9230354 | To determine whether marked overproduction of islet amyloid polypeptide is a potential cause of islet amyloid formation, we increased expression of this transgene by producing homozygous transgenic animals and by making heterozygous mice experimentally insulin resistant with nicotinic acid. |
| 2357 | 9230354 | Pancreatic content of islet amyloid polypeptide-like immunoreactivity in homozygous and nicotinic acid-treated mice was 2-fold (25 +/- 7 fmol/microg; n = 6) and 3.5-fold (47 +/- 20 fmol/microg; n = 3) higher, respectively, than that of untreated heterozygous animals (13+/-2 fmol/microg; n = 11; both p < 0.05). |
| 2358 | 9230354 | Despite this marked increase in production of islet amyloid polypeptide, neither group of mice developed gross islet amyloid deposits even after 16 months of age. |
| 2359 | 9230354 | We conclude that overproduction of islet amyloid polypeptide, even as produced by extreme insulin resistance, is not in itself sufficient for islet amyloid formation. |
| 2360 | 9230354 | Transgenic overproduction of islet amyloid polypeptide (amylin) is not sufficient for islet amyloid formation. |
| 2361 | 9230354 | Islet amyloid polypeptide forms islet amyloid deposits in non-insulin-dependent diabetes mellitus. |
| 2362 | 9230354 | We have generated transgenic mice which express human islet amyloid polypeptide in their pancreatic beta cells yet do not develop islet amyloid deposits despite producing levels of the amyloidogenic human peptide 2 - 3 fold higher than the native (mouse) peptide. |
| 2363 | 9230354 | To determine whether marked overproduction of islet amyloid polypeptide is a potential cause of islet amyloid formation, we increased expression of this transgene by producing homozygous transgenic animals and by making heterozygous mice experimentally insulin resistant with nicotinic acid. |
| 2364 | 9230354 | Pancreatic content of islet amyloid polypeptide-like immunoreactivity in homozygous and nicotinic acid-treated mice was 2-fold (25 +/- 7 fmol/microg; n = 6) and 3.5-fold (47 +/- 20 fmol/microg; n = 3) higher, respectively, than that of untreated heterozygous animals (13+/-2 fmol/microg; n = 11; both p < 0.05). |
| 2365 | 9230354 | Despite this marked increase in production of islet amyloid polypeptide, neither group of mice developed gross islet amyloid deposits even after 16 months of age. |
| 2366 | 9230354 | We conclude that overproduction of islet amyloid polypeptide, even as produced by extreme insulin resistance, is not in itself sufficient for islet amyloid formation. |
| 2367 | 9230354 | Transgenic overproduction of islet amyloid polypeptide (amylin) is not sufficient for islet amyloid formation. |
| 2368 | 9230354 | Islet amyloid polypeptide forms islet amyloid deposits in non-insulin-dependent diabetes mellitus. |
| 2369 | 9230354 | We have generated transgenic mice which express human islet amyloid polypeptide in their pancreatic beta cells yet do not develop islet amyloid deposits despite producing levels of the amyloidogenic human peptide 2 - 3 fold higher than the native (mouse) peptide. |
| 2370 | 9230354 | To determine whether marked overproduction of islet amyloid polypeptide is a potential cause of islet amyloid formation, we increased expression of this transgene by producing homozygous transgenic animals and by making heterozygous mice experimentally insulin resistant with nicotinic acid. |
| 2371 | 9230354 | Pancreatic content of islet amyloid polypeptide-like immunoreactivity in homozygous and nicotinic acid-treated mice was 2-fold (25 +/- 7 fmol/microg; n = 6) and 3.5-fold (47 +/- 20 fmol/microg; n = 3) higher, respectively, than that of untreated heterozygous animals (13+/-2 fmol/microg; n = 11; both p < 0.05). |
| 2372 | 9230354 | Despite this marked increase in production of islet amyloid polypeptide, neither group of mice developed gross islet amyloid deposits even after 16 months of age. |
| 2373 | 9230354 | We conclude that overproduction of islet amyloid polypeptide, even as produced by extreme insulin resistance, is not in itself sufficient for islet amyloid formation. |
| 2374 | 9230354 | Transgenic overproduction of islet amyloid polypeptide (amylin) is not sufficient for islet amyloid formation. |
| 2375 | 9230354 | Islet amyloid polypeptide forms islet amyloid deposits in non-insulin-dependent diabetes mellitus. |
| 2376 | 9230354 | We have generated transgenic mice which express human islet amyloid polypeptide in their pancreatic beta cells yet do not develop islet amyloid deposits despite producing levels of the amyloidogenic human peptide 2 - 3 fold higher than the native (mouse) peptide. |
| 2377 | 9230354 | To determine whether marked overproduction of islet amyloid polypeptide is a potential cause of islet amyloid formation, we increased expression of this transgene by producing homozygous transgenic animals and by making heterozygous mice experimentally insulin resistant with nicotinic acid. |
| 2378 | 9230354 | Pancreatic content of islet amyloid polypeptide-like immunoreactivity in homozygous and nicotinic acid-treated mice was 2-fold (25 +/- 7 fmol/microg; n = 6) and 3.5-fold (47 +/- 20 fmol/microg; n = 3) higher, respectively, than that of untreated heterozygous animals (13+/-2 fmol/microg; n = 11; both p < 0.05). |
| 2379 | 9230354 | Despite this marked increase in production of islet amyloid polypeptide, neither group of mice developed gross islet amyloid deposits even after 16 months of age. |
| 2380 | 9230354 | We conclude that overproduction of islet amyloid polypeptide, even as produced by extreme insulin resistance, is not in itself sufficient for islet amyloid formation. |
| 2381 | 9243100 | Altered immunoreactivity of islet amyloid polypeptide (IAPP) may reflect major modifications of the IAPP molecule in amyloidogenesis. |
| 2382 | 9243100 | We have developed a mouse monoclonal antibody against rat/mouse islet amyloid polypeptide (IAPP). |
| 2383 | 9243100 | Previous immunohistochemical studies of human pancreatic tissue from individuals with non-insulin-dependent diabetes mellitus (NIDDM) have revealed a paradoxical and unexplained lack of IAPP immunoreactivity in beta cells close to amyloid in spite of the presence of IAPP mRNA. |
| 2384 | 9243100 | Altered immunoreactivity of islet amyloid polypeptide (IAPP) may reflect major modifications of the IAPP molecule in amyloidogenesis. |
| 2385 | 9243100 | We have developed a mouse monoclonal antibody against rat/mouse islet amyloid polypeptide (IAPP). |
| 2386 | 9243100 | Previous immunohistochemical studies of human pancreatic tissue from individuals with non-insulin-dependent diabetes mellitus (NIDDM) have revealed a paradoxical and unexplained lack of IAPP immunoreactivity in beta cells close to amyloid in spite of the presence of IAPP mRNA. |
| 2387 | 9243100 | Altered immunoreactivity of islet amyloid polypeptide (IAPP) may reflect major modifications of the IAPP molecule in amyloidogenesis. |
| 2388 | 9243100 | We have developed a mouse monoclonal antibody against rat/mouse islet amyloid polypeptide (IAPP). |
| 2389 | 9243100 | Previous immunohistochemical studies of human pancreatic tissue from individuals with non-insulin-dependent diabetes mellitus (NIDDM) have revealed a paradoxical and unexplained lack of IAPP immunoreactivity in beta cells close to amyloid in spite of the presence of IAPP mRNA. |
| 2390 | 9251946 | Islet amyloid polypeptide (amylin) does not seem to be directly involved in the development of gestational diabetes mellitus. |
| 2391 | 9251946 | In order to define the islet amyloid polypeptide (IAPP) levels in gestational diabetes mellitus (GDM) and their interrelationship with the insulin levels, we studied (1) the placental RNA from 10 women (5 with GDM and 5 normals) for IAPP expression by Northern blotting and (2) 10 women with GDM during a 100-gram oral glucose tolerance test and compared these with 11 normal women matched for obesity and age. |
| 2392 | 9251946 | Islet amyloid polypeptide (amylin) does not seem to be directly involved in the development of gestational diabetes mellitus. |
| 2393 | 9251946 | In order to define the islet amyloid polypeptide (IAPP) levels in gestational diabetes mellitus (GDM) and their interrelationship with the insulin levels, we studied (1) the placental RNA from 10 women (5 with GDM and 5 normals) for IAPP expression by Northern blotting and (2) 10 women with GDM during a 100-gram oral glucose tolerance test and compared these with 11 normal women matched for obesity and age. |
| 2394 | 9259404 | This may relate to concurrent over-production of islet amyloid polypeptide (IAPP) by the pancreatic beta cells. |
| 2395 | 9278863 | Cloning of mouse islet amyloid polypeptide gene and characterization of its promoter. |
| 2396 | 9278863 | Islet amyloid polypeptide (IAPP) was isolated from islet amyloid deposits in patients with insulinoma and pancreatic islets of non-insulin-dependent diabetes mellitus (NIDDM) and several reports suggested that it may contribute to the development of NIDDM. |
| 2397 | 9278863 | Cloning of mouse islet amyloid polypeptide gene and characterization of its promoter. |
| 2398 | 9278863 | Islet amyloid polypeptide (IAPP) was isolated from islet amyloid deposits in patients with insulinoma and pancreatic islets of non-insulin-dependent diabetes mellitus (NIDDM) and several reports suggested that it may contribute to the development of NIDDM. |
| 2399 | 9281227 | [Amylin/IAPP (islet amyloid polypeptide)--physiology and clinical significance]. |
| 2400 | 9281227 | Amylin or islet amyloid polypeptide (IAPP) is the protein component of amyloid deposits commonly seen in pancreatic islets of patients with type 2 diabetes mellitus. |
| 2401 | 9281227 | [Amylin/IAPP (islet amyloid polypeptide)--physiology and clinical significance]. |
| 2402 | 9281227 | Amylin or islet amyloid polypeptide (IAPP) is the protein component of amyloid deposits commonly seen in pancreatic islets of patients with type 2 diabetes mellitus. |
| 2403 | 9282365 | Through comparative evaluations of prior histories of the diseases, such as diabetes mellitus, carpal tunnel syndrome, amyloid osteoarthropathy (AOA) and parathyroidectomy, along with large calcification of the nuchal soft tissues on plain films, it was found that DSA, in conjunction with NIS-I, correlated with only AOA (p < 0.05). |
| 2404 | 9284894 | Expression of human islet amyloid polypeptide/amylin impairs insulin secretion in mouse pancreatic beta cells. |
| 2405 | 9284894 | Non-insulin-dependent diabetes mellitus (NIDDM) is associated histopathologically with islet amyloid deposits of which a major component is islet amyloid polypeptide (IAPP)/amylin. |
| 2406 | 9284894 | Expression of human islet amyloid polypeptide/amylin impairs insulin secretion in mouse pancreatic beta cells. |
| 2407 | 9284894 | Non-insulin-dependent diabetes mellitus (NIDDM) is associated histopathologically with islet amyloid deposits of which a major component is islet amyloid polypeptide (IAPP)/amylin. |
| 2408 | 9353797 | More recently, islet amyloid polypeptide or amylin, and adrenomedullin were isolated from human insulinoma and pheochromocytoma respectively, and revealed between 25 and 50% sequence homology with CGRP. |
| 2409 | 9353797 | Based upon the differential biological activity of various CGRP analogs, the CGRP receptors have been classified in two major classes, namely the CGRP1 and CGRP2 subtypes. |
| 2410 | 9353797 | Indeed, modulation of adenylate cyclase activity following receptor activation has been reported for CGRP, amylin and adrenomedullin. |
| 2411 | 9353797 | The cloning of various calcitonin and most recently of CGRP1 and adrenomedullin receptors was reported and revealed structural similarities but also significant differences to other members of the G protein-coupled receptors. |
| 2412 | 9361089 | Islet amyloid polypeptide in Psammomys obesus (sand rat): effects of nutritionally induced diabetes and recovery on low-energy diet or vanadyl sulfate treatment. |
| 2413 | 9361089 | We investigated the possible relationship between islet amyloid polypeptide (IAPP) and the hyperinsulinemia and/or hyperglycemia that is seen in the desert-adapted gerbil Psammomys obesus, when the animal is transferred from a low-energy (LE) diet to a high-energy (HE) diet. |
| 2414 | 9361089 | Islet amyloid polypeptide in Psammomys obesus (sand rat): effects of nutritionally induced diabetes and recovery on low-energy diet or vanadyl sulfate treatment. |
| 2415 | 9361089 | We investigated the possible relationship between islet amyloid polypeptide (IAPP) and the hyperinsulinemia and/or hyperglycemia that is seen in the desert-adapted gerbil Psammomys obesus, when the animal is transferred from a low-energy (LE) diet to a high-energy (HE) diet. |
| 2416 | 9375734 | Amyloid fibrils are derived from different unrelated proteins in the different forms of the disease but share many common properties, including the capacity to bind the normal plasma protein serum amyloid P component (SAP). |
| 2417 | 9375734 | This is the basis for our development of radiolabelled SAP as a nuclear medicine tracer for the diagnosis and quantitative monitoring of amyloid. |
| 2418 | 9375734 | Amyloid fibrils are derived from different unrelated proteins in the different forms of the disease but share many common properties, including the capacity to bind the normal plasma protein serum amyloid P component (SAP). |
| 2419 | 9375734 | This is the basis for our development of radiolabelled SAP as a nuclear medicine tracer for the diagnosis and quantitative monitoring of amyloid. |
| 2420 | 9389420 | Serum sialic acid was confirmed as a marker of the acute-phase response since serum concentrations were significantly related to established acute-phase proteins such as alpha-1 acid glycoprotein (r = 0.82, p < 0.0001). |
| 2421 | 9389420 | There was a significant graded increase of serum sialic acid, alpha-1 acid glycoprotein, IL-6 and urinary albumin excretion rate amongst the three groups, with the lowest levels in non-diabetic subjects, intermediate levels in NIDDM patients without syndrome X and highest levels in NIDDM patients with syndrome X. |
| 2422 | 9389420 | C-reactive protein and cortisol levels were also higher in syndrome X-positive compared to X-negative patients and serum amyloid A was higher in both diabetic groups than in the control group. |
| 2423 | 9426315 | Fibrillar islet amyloid polypeptide (amylin) is internalised by macrophages but resists proteolytic degradation. |
| 2424 | 9426315 | Pancreatic islet amyloid, formed from islet amyloid polypeptide, is found in 96% of Type II (non-insulin-dependent) diabetic patients. |
| 2425 | 9426315 | Fibrils immunoreactive for islet amyloid polypeptide are found in macrophages associated with amyloid, suggesting that deposits can be phagocytosed. |
| 2426 | 9426315 | To determine the mechanism for the recognition and internalisation of fibrils, mouse peritoneal macrophages were cultured with fibrillar synthetic human islet amyloid polypeptide. |
| 2427 | 9426315 | Fibrillar islet amyloid polypeptide (amylin) is internalised by macrophages but resists proteolytic degradation. |
| 2428 | 9426315 | Pancreatic islet amyloid, formed from islet amyloid polypeptide, is found in 96% of Type II (non-insulin-dependent) diabetic patients. |
| 2429 | 9426315 | Fibrils immunoreactive for islet amyloid polypeptide are found in macrophages associated with amyloid, suggesting that deposits can be phagocytosed. |
| 2430 | 9426315 | To determine the mechanism for the recognition and internalisation of fibrils, mouse peritoneal macrophages were cultured with fibrillar synthetic human islet amyloid polypeptide. |
| 2431 | 9426315 | Fibrillar islet amyloid polypeptide (amylin) is internalised by macrophages but resists proteolytic degradation. |
| 2432 | 9426315 | Pancreatic islet amyloid, formed from islet amyloid polypeptide, is found in 96% of Type II (non-insulin-dependent) diabetic patients. |
| 2433 | 9426315 | Fibrils immunoreactive for islet amyloid polypeptide are found in macrophages associated with amyloid, suggesting that deposits can be phagocytosed. |
| 2434 | 9426315 | To determine the mechanism for the recognition and internalisation of fibrils, mouse peritoneal macrophages were cultured with fibrillar synthetic human islet amyloid polypeptide. |
| 2435 | 9426315 | Fibrillar islet amyloid polypeptide (amylin) is internalised by macrophages but resists proteolytic degradation. |
| 2436 | 9426315 | Pancreatic islet amyloid, formed from islet amyloid polypeptide, is found in 96% of Type II (non-insulin-dependent) diabetic patients. |
| 2437 | 9426315 | Fibrils immunoreactive for islet amyloid polypeptide are found in macrophages associated with amyloid, suggesting that deposits can be phagocytosed. |
| 2438 | 9426315 | To determine the mechanism for the recognition and internalisation of fibrils, mouse peritoneal macrophages were cultured with fibrillar synthetic human islet amyloid polypeptide. |
| 2439 | 9437230 | No correlation between insulin and islet amyloid polypeptide after stimulation with glucagon-like peptide-1 in type 2 diabetes. |
| 2440 | 9451476 | Islet cells containing immunoreactive insulin and islet amyloid polypeptide were plentiful, while those staining positive for glucagon and somatostatin were scarce in these grafts. |
| 2441 | 9492286 | Contribution of advanced glycosylation to the amyloidogenicity of islet amyloid polypeptide. |
| 2442 | 9492286 | The formation of amyloid within the islets of Langerhans is associated with the development of type II diabetes mellitus and occurs by the aggregation and insolubilization of islet amyloid polypeptide (IAPP). |
| 2443 | 9492286 | Contribution of advanced glycosylation to the amyloidogenicity of islet amyloid polypeptide. |
| 2444 | 9492286 | The formation of amyloid within the islets of Langerhans is associated with the development of type II diabetes mellitus and occurs by the aggregation and insolubilization of islet amyloid polypeptide (IAPP). |
| 2445 | 9506786 | In vitro insulin secretion and the response to glucose challenge of APPH and APA encapsulated islets were comparable to free islets. |
| 2446 | 9560308 | A novel assay in vitro of human islet amyloid polypeptide amyloidogenesis and effects of insulin secretory vesicle peptides on amyloid formation. |
| 2447 | 9560308 | Human islet amyloid polypeptide (IAPP) is a 37-residue peptide that is co-secreted with insulin by the beta-cell and might be involved in the pathogenesis of non-insulin-dependent diabetes mellitus. |
| 2448 | 9560308 | Because insulin resistance or hyperglycaemia increase the IAPP-to-insulin ratio, increased intracellular IAPP compared with insulin expression in genetically predisposed individuals might contribute to intracellular amyloid formation, beta-cell death and the genesis of non-insulin-dependent diabetes mellitus. |
| 2449 | 9560308 | A novel assay in vitro of human islet amyloid polypeptide amyloidogenesis and effects of insulin secretory vesicle peptides on amyloid formation. |
| 2450 | 9560308 | Human islet amyloid polypeptide (IAPP) is a 37-residue peptide that is co-secreted with insulin by the beta-cell and might be involved in the pathogenesis of non-insulin-dependent diabetes mellitus. |
| 2451 | 9560308 | Because insulin resistance or hyperglycaemia increase the IAPP-to-insulin ratio, increased intracellular IAPP compared with insulin expression in genetically predisposed individuals might contribute to intracellular amyloid formation, beta-cell death and the genesis of non-insulin-dependent diabetes mellitus. |
| 2452 | 9560308 | A novel assay in vitro of human islet amyloid polypeptide amyloidogenesis and effects of insulin secretory vesicle peptides on amyloid formation. |
| 2453 | 9560308 | Human islet amyloid polypeptide (IAPP) is a 37-residue peptide that is co-secreted with insulin by the beta-cell and might be involved in the pathogenesis of non-insulin-dependent diabetes mellitus. |
| 2454 | 9560308 | Because insulin resistance or hyperglycaemia increase the IAPP-to-insulin ratio, increased intracellular IAPP compared with insulin expression in genetically predisposed individuals might contribute to intracellular amyloid formation, beta-cell death and the genesis of non-insulin-dependent diabetes mellitus. |
| 2455 | 9568695 | Sulfate content and specific glycosaminoglycan backbone of perlecan are critical for perlecan's enhancement of islet amyloid polypeptide (amylin) fibril formation. |
| 2456 | 9568695 | Previous studies have also revealed the presence of the specific heparan sulfate proteoglycan, perlecan, colocalized to islet amyloid deposits, similar to perlecan's known involvement with other amyloid proteins. |
| 2457 | 9568695 | In the present study, perlecan purified from the Engelbreth-Holm-Swarm (EHS) tumor was used to define perlecan's interactions with amylin (i.e., islet amyloid polypeptide) and its effects on amylin fibril formation. |
| 2458 | 9568695 | Sulfate content and specific glycosaminoglycan backbone of perlecan are critical for perlecan's enhancement of islet amyloid polypeptide (amylin) fibril formation. |
| 2459 | 9568695 | Previous studies have also revealed the presence of the specific heparan sulfate proteoglycan, perlecan, colocalized to islet amyloid deposits, similar to perlecan's known involvement with other amyloid proteins. |
| 2460 | 9568695 | In the present study, perlecan purified from the Engelbreth-Holm-Swarm (EHS) tumor was used to define perlecan's interactions with amylin (i.e., islet amyloid polypeptide) and its effects on amylin fibril formation. |
| 2461 | 9568695 | Sulfate content and specific glycosaminoglycan backbone of perlecan are critical for perlecan's enhancement of islet amyloid polypeptide (amylin) fibril formation. |
| 2462 | 9568695 | Previous studies have also revealed the presence of the specific heparan sulfate proteoglycan, perlecan, colocalized to islet amyloid deposits, similar to perlecan's known involvement with other amyloid proteins. |
| 2463 | 9568695 | In the present study, perlecan purified from the Engelbreth-Holm-Swarm (EHS) tumor was used to define perlecan's interactions with amylin (i.e., islet amyloid polypeptide) and its effects on amylin fibril formation. |
| 2464 | 9568698 | Its major component is the normal beta-cell secretory product amylin, or islet amyloid polypeptide (IAPP). |
| 2465 | 9568698 | To determine whether increased or disproportionate release of amylin may explain the propensity for amyloid deposition in type 2 diabetes, we measured plasma amylin-like immunoreactivity (ALI) and immunoreactive insulin (IRI) release in response to an oral glucose load in 94 Japanese-American subjects with normal glucose tolerance (NGT; n=56), impaired glucose tolerance (IGT; n=10), and type 2 diabetes (n=28) as defined by World Health Organization criteria. |
| 2466 | 9568698 | Its major component is the normal beta-cell secretory product amylin, or islet amyloid polypeptide (IAPP). |
| 2467 | 9568698 | To determine whether increased or disproportionate release of amylin may explain the propensity for amyloid deposition in type 2 diabetes, we measured plasma amylin-like immunoreactivity (ALI) and immunoreactive insulin (IRI) release in response to an oral glucose load in 94 Japanese-American subjects with normal glucose tolerance (NGT; n=56), impaired glucose tolerance (IGT; n=10), and type 2 diabetes (n=28) as defined by World Health Organization criteria. |
| 2468 | 9584121 | These cells express some beta cell markers, such as islet amyloid polypeptide and Pdx1, but lack other definitive beta cell markers including glucose transporter 2 and Nkx6.1. |
| 2469 | 9588445 | Islet amyloid-associated diabetes in obese A(vy)/a mice expressing human islet amyloid polypeptide. |
| 2470 | 9588445 | We have previously shown that hemizygous transgenic mice expressing human islet amyloid polypeptide (hIAPP) in pancreatic beta-cells have no diabetic phenotype, whereas in the homozygous state, they developed severe, early-onset hyperglycemia associated with impaired insulin secretion and beta-cell death. |
| 2471 | 9588445 | We conclude that in transgenic mice expressing hIAPP, insulin resistance can induce overt, slow-onset diabetes associated with islet amyloid and decreased beta-cell mass. |
| 2472 | 9588445 | Islet amyloid-associated diabetes in obese A(vy)/a mice expressing human islet amyloid polypeptide. |
| 2473 | 9588445 | We have previously shown that hemizygous transgenic mice expressing human islet amyloid polypeptide (hIAPP) in pancreatic beta-cells have no diabetic phenotype, whereas in the homozygous state, they developed severe, early-onset hyperglycemia associated with impaired insulin secretion and beta-cell death. |
| 2474 | 9588445 | We conclude that in transgenic mice expressing hIAPP, insulin resistance can induce overt, slow-onset diabetes associated with islet amyloid and decreased beta-cell mass. |
| 2475 | 9588445 | Islet amyloid-associated diabetes in obese A(vy)/a mice expressing human islet amyloid polypeptide. |
| 2476 | 9588445 | We have previously shown that hemizygous transgenic mice expressing human islet amyloid polypeptide (hIAPP) in pancreatic beta-cells have no diabetic phenotype, whereas in the homozygous state, they developed severe, early-onset hyperglycemia associated with impaired insulin secretion and beta-cell death. |
| 2477 | 9588445 | We conclude that in transgenic mice expressing hIAPP, insulin resistance can induce overt, slow-onset diabetes associated with islet amyloid and decreased beta-cell mass. |
| 2478 | 9633536 | Formation of amylin-containing islet amyloid deposits may contribute to the progressive deterioration of beta cell function in non-insulin-dependent diabetes mellitus. |
| 2479 | 9637677 | These mice develop diabetes with age, and we show that IPF1/PDX1 is required for maintaining the beta cell identity by positively regulating insulin and islet amyloid polypeptide expression and by repressing glucagon expression. |
| 2480 | 9637677 | We also provide evidence that IPF1/PDX1 regulates the expression of Glut2 in a dosage-dependent manner suggesting that lowered IPF1/PDX1 activity may contribute to the development of type II diabetes by causing impaired expression of both Glut2 and insulin. |
| 2481 | 9715376 | The fact that both insulin resistance and impaired insulin release have been found to precede and predict NIDDM in prospective studies may be in part a reflection of just such relatedness. 4) Direct genetic analysis is effective in rarer forms of glucose intolerance (MODY, mitochondrial mutations, etc.) but encounters serious difficulties with typical late-onset NIDDM. |
| 2482 | 9715376 | Incidentally, any defect in insulin secretion, whether in normoglycemic or hyperglycemic persons, could be due to other factors than primary beta-cell dysfunction: amyloid deposits in the pancreas (126), changes in insulin secretagogues (amylin, GLP-1, GIP, galanin) (127-130), early intrauterine malnutrition (131). |
| 2483 | 9777946 | In this study, we examined the immunohistochemical localization of AGEs, amyloid beta protein (A beta), apolipoprotein E (ApoE), and tau protein in senile plaques, neurofibrillary tangles (NFTs), and cerebral amyloid angiopathy (CAA) in Alzheimer's disease and other neurodegenerative diseases (progressive supranuclear palsy, Pick's disease, and Guamanian amyotrophic lateral sclerosis/Parkinsonism-dementia complex). |
| 2484 | 9794114 | Type II (non-insulin-dependent) diabetes mellitus is associated with increased blood concentrations of markers of the acute-phase response, including sialic acid, alpha-1 acid glycoprotein, serum amyloid A, C-reactive protein and cortisol, and the main cytokine mediator of the response, interleukin-6. |
| 2485 | 9833947 | Transgenic overexpression of human islet amyloid polypeptide inhibits insulin secretion and glucose elimination after gastric glucose gavage in mice. |
| 2486 | 9833947 | Islet amyloid polypeptide (IAPP) is synthesized in islet beta cells and has been implicated in diabetes pathogenesis because it can inhibit insulin secretion and action and form fibrils leading to islet amyloidosis. |
| 2487 | 9833947 | Transgenic overexpression of human islet amyloid polypeptide inhibits insulin secretion and glucose elimination after gastric glucose gavage in mice. |
| 2488 | 9833947 | Islet amyloid polypeptide (IAPP) is synthesized in islet beta cells and has been implicated in diabetes pathogenesis because it can inhibit insulin secretion and action and form fibrils leading to islet amyloidosis. |
| 2489 | 9849972 | Here we review our studies on the embryonic islet expression of islet amyloid polypeptide (IAPP) and the PP-fold peptides pancreatic polypeptide (PP), peptide YY (PYY) and neuropeptide Y (NPY). |
| 2490 | 9849972 | As development proceeds, the insulin/IAPP phenotype is segregated from that of PYY/glucagon; with the formation of islet-like structures, insulin/IAPP-expressing cells primarily occupy their central portions, while PYY/glucagon-expressing cells are found in their periphery. |
| 2491 | 9849972 | At the time of formation of islet-like structures, expression of NPY is induced in the insulin/IAPP-containing cells. |
| 2492 | 9849972 | Whereas NPY-expression ceases at birth, PYY is constitutively expressed in non-beta-cells in the mature rat. |
| 2493 | 9862387 | Differing haemodynamic and catecholamine responses to exercise in three groups with peripheralautonomic dysfunction: insulin-dependent diabetes mellitus, familial amyloid polyneuropathy and pure autonomic failure. |
| 2494 | 9862387 | The haemodynamic and catecholamine responses to supine exercise, and the effect on standing blood pressure (BP), were studied in three groups with peripheral autonomic dysfunction; insulin-dependent diabetes mellitus (IDDM), familial amyloid polyneuropathy (FAP) and pure autonomic failure (PAF). |
| 2495 | 9862387 | With exercise, BP increased in controls, was unchanged in IDDM and FAP, and fell in PAF. |
| 2496 | 9862387 | Heart rate (HR) increased more in controls than IDDM, FAP or PAF. |
| 2497 | 9862387 | Cardiac index (CI) increased less in IDDM than controls, FAP or PAF. |
| 2498 | 9862387 | Systemic vascular resistance (SVR) fell similarly in controls and IDDM, with a greater fall in FAP and PAF. |
| 2499 | 9862387 | On standing, BP was unchanged in controls; BP fell pre- and post-exercise in IDDM, FAP and PAF, with a significantly greater fall post-exercise in FAP and PAF. |
| 2500 | 9862387 | Differing haemodynamic and catecholamine responses to exercise in three groups with peripheralautonomic dysfunction: insulin-dependent diabetes mellitus, familial amyloid polyneuropathy and pure autonomic failure. |
| 2501 | 9862387 | The haemodynamic and catecholamine responses to supine exercise, and the effect on standing blood pressure (BP), were studied in three groups with peripheral autonomic dysfunction; insulin-dependent diabetes mellitus (IDDM), familial amyloid polyneuropathy (FAP) and pure autonomic failure (PAF). |
| 2502 | 9862387 | With exercise, BP increased in controls, was unchanged in IDDM and FAP, and fell in PAF. |
| 2503 | 9862387 | Heart rate (HR) increased more in controls than IDDM, FAP or PAF. |
| 2504 | 9862387 | Cardiac index (CI) increased less in IDDM than controls, FAP or PAF. |
| 2505 | 9862387 | Systemic vascular resistance (SVR) fell similarly in controls and IDDM, with a greater fall in FAP and PAF. |
| 2506 | 9862387 | On standing, BP was unchanged in controls; BP fell pre- and post-exercise in IDDM, FAP and PAF, with a significantly greater fall post-exercise in FAP and PAF. |
| 2507 | 10026261 | Amylin, also known as islet amyloid polypeptide (IAPP), is the major protein component of the fibril deposits found in the pancreas of individuals with type II diabetes. |
| 2508 | 10036582 | Islet amyloid formed from islet amyloid polypeptide (IAPP, amylin) is found in spontaneously diabetic monkeys and cats. |
| 2509 | 10036583 | Quantitative immunohistochemical analysis of islet amyloid polypeptide (IAPP) in normal, impaired glucose tolerant, and diabetic cats. |
| 2510 | 10036583 | Islet amyloid polypeptide (IAPP, "amylin") has been proposed as having important roles in the pathogenesis of type 2 diabetes mellitus via its biological activity and by forming islet amyloid. |
| 2511 | 10036583 | The study provides evidence that an increased beta cell storage of IAPP independent of insulin may be an important factor in the early phase of the development of islet amyloid in this form of diabetes. |
| 2512 | 10036583 | Quantitative immunohistochemical analysis of islet amyloid polypeptide (IAPP) in normal, impaired glucose tolerant, and diabetic cats. |
| 2513 | 10036583 | Islet amyloid polypeptide (IAPP, "amylin") has been proposed as having important roles in the pathogenesis of type 2 diabetes mellitus via its biological activity and by forming islet amyloid. |
| 2514 | 10036583 | The study provides evidence that an increased beta cell storage of IAPP independent of insulin may be an important factor in the early phase of the development of islet amyloid in this form of diabetes. |
| 2515 | 10036583 | Quantitative immunohistochemical analysis of islet amyloid polypeptide (IAPP) in normal, impaired glucose tolerant, and diabetic cats. |
| 2516 | 10036583 | Islet amyloid polypeptide (IAPP, "amylin") has been proposed as having important roles in the pathogenesis of type 2 diabetes mellitus via its biological activity and by forming islet amyloid. |
| 2517 | 10036583 | The study provides evidence that an increased beta cell storage of IAPP independent of insulin may be an important factor in the early phase of the development of islet amyloid in this form of diabetes. |
| 2518 | 10064099 | Prolonged exposure of pancreatic beta cells to raised glucose concentrations results in increased cellular content of islet amyloid polypeptide precursors. |
| 2519 | 10064099 | Most non-insulin dependent diabetic patients have amyloid deposits in their pancreatic islets. |
| 2520 | 10064099 | It is not known whether chronic hyperglycaemia contributes to the formation of amyloid fibrils from the islet amyloid polypeptide that is produced by the pancreatic beta cells. |
| 2521 | 10064099 | Since islet amyloid exhibits islet amyloid polypeptide precursors immunoreactivity, we examined whether sustained in vitro exposure to raised glucose increases the abundance of these precursors in human beta cells. |
| 2522 | 10064099 | After 6 days stimulation with 20 mmol/l glucose the cellular content of insulin but not islet amyloid polypeptide was decreased leading to an increase in the ratio of the latter over insulin (3.0 +/- 0.6 vs 1.8 +/- 0.3 after 6 mmol/l glucose culture, p < 0.05). |
| 2523 | 10064099 | Western blot analysis of cellular islet amyloid polypeptide after prolonged exposure to high glucose indicated the presence of higher proportions of its precursor- and intermediate forms. |
| 2524 | 10064099 | We concluded that prolonged in vitro exposure of beta cells to raised glucose concentrations increases the relative proportion of islet amyloid polypeptide over insulin, as well as of its precursors over the mature form of islet amyloid polypeptide. |
| 2525 | 10064099 | Prolonged exposure of pancreatic beta cells to raised glucose concentrations results in increased cellular content of islet amyloid polypeptide precursors. |
| 2526 | 10064099 | Most non-insulin dependent diabetic patients have amyloid deposits in their pancreatic islets. |
| 2527 | 10064099 | It is not known whether chronic hyperglycaemia contributes to the formation of amyloid fibrils from the islet amyloid polypeptide that is produced by the pancreatic beta cells. |
| 2528 | 10064099 | Since islet amyloid exhibits islet amyloid polypeptide precursors immunoreactivity, we examined whether sustained in vitro exposure to raised glucose increases the abundance of these precursors in human beta cells. |
| 2529 | 10064099 | After 6 days stimulation with 20 mmol/l glucose the cellular content of insulin but not islet amyloid polypeptide was decreased leading to an increase in the ratio of the latter over insulin (3.0 +/- 0.6 vs 1.8 +/- 0.3 after 6 mmol/l glucose culture, p < 0.05). |
| 2530 | 10064099 | Western blot analysis of cellular islet amyloid polypeptide after prolonged exposure to high glucose indicated the presence of higher proportions of its precursor- and intermediate forms. |
| 2531 | 10064099 | We concluded that prolonged in vitro exposure of beta cells to raised glucose concentrations increases the relative proportion of islet amyloid polypeptide over insulin, as well as of its precursors over the mature form of islet amyloid polypeptide. |
| 2532 | 10064099 | Prolonged exposure of pancreatic beta cells to raised glucose concentrations results in increased cellular content of islet amyloid polypeptide precursors. |
| 2533 | 10064099 | Most non-insulin dependent diabetic patients have amyloid deposits in their pancreatic islets. |
| 2534 | 10064099 | It is not known whether chronic hyperglycaemia contributes to the formation of amyloid fibrils from the islet amyloid polypeptide that is produced by the pancreatic beta cells. |
| 2535 | 10064099 | Since islet amyloid exhibits islet amyloid polypeptide precursors immunoreactivity, we examined whether sustained in vitro exposure to raised glucose increases the abundance of these precursors in human beta cells. |
| 2536 | 10064099 | After 6 days stimulation with 20 mmol/l glucose the cellular content of insulin but not islet amyloid polypeptide was decreased leading to an increase in the ratio of the latter over insulin (3.0 +/- 0.6 vs 1.8 +/- 0.3 after 6 mmol/l glucose culture, p < 0.05). |
| 2537 | 10064099 | Western blot analysis of cellular islet amyloid polypeptide after prolonged exposure to high glucose indicated the presence of higher proportions of its precursor- and intermediate forms. |
| 2538 | 10064099 | We concluded that prolonged in vitro exposure of beta cells to raised glucose concentrations increases the relative proportion of islet amyloid polypeptide over insulin, as well as of its precursors over the mature form of islet amyloid polypeptide. |
| 2539 | 10064099 | Prolonged exposure of pancreatic beta cells to raised glucose concentrations results in increased cellular content of islet amyloid polypeptide precursors. |
| 2540 | 10064099 | Most non-insulin dependent diabetic patients have amyloid deposits in their pancreatic islets. |
| 2541 | 10064099 | It is not known whether chronic hyperglycaemia contributes to the formation of amyloid fibrils from the islet amyloid polypeptide that is produced by the pancreatic beta cells. |
| 2542 | 10064099 | Since islet amyloid exhibits islet amyloid polypeptide precursors immunoreactivity, we examined whether sustained in vitro exposure to raised glucose increases the abundance of these precursors in human beta cells. |
| 2543 | 10064099 | After 6 days stimulation with 20 mmol/l glucose the cellular content of insulin but not islet amyloid polypeptide was decreased leading to an increase in the ratio of the latter over insulin (3.0 +/- 0.6 vs 1.8 +/- 0.3 after 6 mmol/l glucose culture, p < 0.05). |
| 2544 | 10064099 | Western blot analysis of cellular islet amyloid polypeptide after prolonged exposure to high glucose indicated the presence of higher proportions of its precursor- and intermediate forms. |
| 2545 | 10064099 | We concluded that prolonged in vitro exposure of beta cells to raised glucose concentrations increases the relative proportion of islet amyloid polypeptide over insulin, as well as of its precursors over the mature form of islet amyloid polypeptide. |
| 2546 | 10064099 | Prolonged exposure of pancreatic beta cells to raised glucose concentrations results in increased cellular content of islet amyloid polypeptide precursors. |
| 2547 | 10064099 | Most non-insulin dependent diabetic patients have amyloid deposits in their pancreatic islets. |
| 2548 | 10064099 | It is not known whether chronic hyperglycaemia contributes to the formation of amyloid fibrils from the islet amyloid polypeptide that is produced by the pancreatic beta cells. |
| 2549 | 10064099 | Since islet amyloid exhibits islet amyloid polypeptide precursors immunoreactivity, we examined whether sustained in vitro exposure to raised glucose increases the abundance of these precursors in human beta cells. |
| 2550 | 10064099 | After 6 days stimulation with 20 mmol/l glucose the cellular content of insulin but not islet amyloid polypeptide was decreased leading to an increase in the ratio of the latter over insulin (3.0 +/- 0.6 vs 1.8 +/- 0.3 after 6 mmol/l glucose culture, p < 0.05). |
| 2551 | 10064099 | Western blot analysis of cellular islet amyloid polypeptide after prolonged exposure to high glucose indicated the presence of higher proportions of its precursor- and intermediate forms. |
| 2552 | 10064099 | We concluded that prolonged in vitro exposure of beta cells to raised glucose concentrations increases the relative proportion of islet amyloid polypeptide over insulin, as well as of its precursors over the mature form of islet amyloid polypeptide. |
| 2553 | 10064099 | Prolonged exposure of pancreatic beta cells to raised glucose concentrations results in increased cellular content of islet amyloid polypeptide precursors. |
| 2554 | 10064099 | Most non-insulin dependent diabetic patients have amyloid deposits in their pancreatic islets. |
| 2555 | 10064099 | It is not known whether chronic hyperglycaemia contributes to the formation of amyloid fibrils from the islet amyloid polypeptide that is produced by the pancreatic beta cells. |
| 2556 | 10064099 | Since islet amyloid exhibits islet amyloid polypeptide precursors immunoreactivity, we examined whether sustained in vitro exposure to raised glucose increases the abundance of these precursors in human beta cells. |
| 2557 | 10064099 | After 6 days stimulation with 20 mmol/l glucose the cellular content of insulin but not islet amyloid polypeptide was decreased leading to an increase in the ratio of the latter over insulin (3.0 +/- 0.6 vs 1.8 +/- 0.3 after 6 mmol/l glucose culture, p < 0.05). |
| 2558 | 10064099 | Western blot analysis of cellular islet amyloid polypeptide after prolonged exposure to high glucose indicated the presence of higher proportions of its precursor- and intermediate forms. |
| 2559 | 10064099 | We concluded that prolonged in vitro exposure of beta cells to raised glucose concentrations increases the relative proportion of islet amyloid polypeptide over insulin, as well as of its precursors over the mature form of islet amyloid polypeptide. |
| 2560 | 10064099 | Prolonged exposure of pancreatic beta cells to raised glucose concentrations results in increased cellular content of islet amyloid polypeptide precursors. |
| 2561 | 10064099 | Most non-insulin dependent diabetic patients have amyloid deposits in their pancreatic islets. |
| 2562 | 10064099 | It is not known whether chronic hyperglycaemia contributes to the formation of amyloid fibrils from the islet amyloid polypeptide that is produced by the pancreatic beta cells. |
| 2563 | 10064099 | Since islet amyloid exhibits islet amyloid polypeptide precursors immunoreactivity, we examined whether sustained in vitro exposure to raised glucose increases the abundance of these precursors in human beta cells. |
| 2564 | 10064099 | After 6 days stimulation with 20 mmol/l glucose the cellular content of insulin but not islet amyloid polypeptide was decreased leading to an increase in the ratio of the latter over insulin (3.0 +/- 0.6 vs 1.8 +/- 0.3 after 6 mmol/l glucose culture, p < 0.05). |
| 2565 | 10064099 | Western blot analysis of cellular islet amyloid polypeptide after prolonged exposure to high glucose indicated the presence of higher proportions of its precursor- and intermediate forms. |
| 2566 | 10064099 | We concluded that prolonged in vitro exposure of beta cells to raised glucose concentrations increases the relative proportion of islet amyloid polypeptide over insulin, as well as of its precursors over the mature form of islet amyloid polypeptide. |
| 2567 | 10078548 | The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles. |
| 2568 | 10078548 | Islet amyloid is derived from the locally expressed protein islet amyloid polypeptide (IAPP). |
| 2569 | 10078548 | The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles. |
| 2570 | 10078548 | Islet amyloid is derived from the locally expressed protein islet amyloid polypeptide (IAPP). |
| 2571 | 10078555 | Only four of those genes had been shown previously to be expressed at higher levels in beta-cells (insulin, islet amyloid polypeptide, neuronatin, and protein kinase A regulatory subunit [RIalpha]). |
| 2572 | 10191146 | Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in vitro. |
| 2573 | 10191146 | Pancreatic amyloidosis is characterized by the deposition of amyloid consisting of islet amyloid polypeptide (IAPP). |
| 2574 | 10191146 | Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in vitro. |
| 2575 | 10191146 | Pancreatic amyloidosis is characterized by the deposition of amyloid consisting of islet amyloid polypeptide (IAPP). |
| 2576 | 10206436 | Differences in amyloid deposition in islets of transgenic mice expressing human islet amyloid polypeptide versus human islets implanted into nude mice. |
| 2577 | 10206436 | Islet amyloid polypeptide (IAPP)-derived amyloid is frequently deposited in the islets of Langerhans in patients with chronic non-insulin-dependent diabetes mellitus (NIDDM). |
| 2578 | 10206436 | Differences in amyloid deposition in islets of transgenic mice expressing human islet amyloid polypeptide versus human islets implanted into nude mice. |
| 2579 | 10206436 | Islet amyloid polypeptide (IAPP)-derived amyloid is frequently deposited in the islets of Langerhans in patients with chronic non-insulin-dependent diabetes mellitus (NIDDM). |
| 2580 | 10233846 | Intracellular amyloidogenesis by human islet amyloid polypeptide induces apoptosis in COS-1 cells. |
| 2581 | 10233846 | Human islet amyloid polypeptide (hIAPP) is co-secreted with insulin from pancreatic islet beta cells. |
| 2582 | 10233846 | Intracellular amyloidogenesis by human islet amyloid polypeptide induces apoptosis in COS-1 cells. |
| 2583 | 10233846 | Human islet amyloid polypeptide (hIAPP) is co-secreted with insulin from pancreatic islet beta cells. |
| 2584 | 10334297 | It has as its unique component the islet beta-cell peptide islet amyloid polypeptide (IAPP), or amylin, which is cosecreted with insulin. |
| 2585 | 10334297 | In addition to this unique component, islet amyloid contains other proteins, such as apolipoprotein E and the heparan sulfate proteoglycan perlecan, which are typically observed in other forms of generalized and localized amyloid. |
| 2586 | 10334297 | It has as its unique component the islet beta-cell peptide islet amyloid polypeptide (IAPP), or amylin, which is cosecreted with insulin. |
| 2587 | 10334297 | In addition to this unique component, islet amyloid contains other proteins, such as apolipoprotein E and the heparan sulfate proteoglycan perlecan, which are typically observed in other forms of generalized and localized amyloid. |
| 2588 | 10337452 | With the respect to the trophic effect of amyloid deposits in the pancreatic islets and to a hypothetic effect of amylin increasing insulin resistance, the present results emphasize the particular usefulness of metformin in the pharmacological treatment of NIDDM. |
| 2589 | 10341286 | Despite co-secretion from islets the relative amounts of IAPP and insulin may vary. |
| 2590 | 10341286 | Since IAPP was first described as the major peptide constituent of amyloid in the islets of Langerhans of subjects with type 2 diabetes and insulinoma, many studies have been devoted to investigating the role of IAPP in formation of amyloid deposits and in diabetes pathogenesis. |
| 2591 | 10341286 | However, there is growing evidence for IAPP as an active islet hormone in addition to insulin and glucagon in glucose metabolic control. |
| 2592 | 10341286 | An inhibitory effect is seen by IAPP on gastric emptying, glycogen synthesis in skeletal muscle, islet insulin and glucagon secretion, whereas a stimulatory effect is seen on hepatic gluconeogenesis. |
| 2593 | 10362543 | Presenilin 2 was identified in primitive islet and duct cells of human foetal pancreas and in proliferating exocrine duct cells in human pancreatitis but not found in islet amyloid deposits in Type 2 diabetic subjects. |
| 2594 | 10362543 | Oral glucose tolerance tests on subjects with the presenilin 2 Met239Val mutation unaffected by early onset familial Alzheimer's disease (mean age 35 years) and on their first-degree relatives without the mutation demonstrated no evidence of glucose intolerance or increased proinsulin secretion. |
| 2595 | 10452964 | The rate of Amadori product formation in apoE in vitro was similar to that for albumin and apolipoproteins A-I and A-II. |
| 2596 | 10452964 | In contrast, glycation had no effect on the interaction of apoE with amyloid beta-peptide. |
| 2597 | 10480534 | Pancreatic amyloid proteins and their relation to clinical diabetes, with special reference to serum insulin secretion. |
| 2598 | 10495105 | Pituitary adenylate cyclase-activating polypeptide and islet amyloid polypeptide in primary sensory neurons: functional implications from plasticity in expression on nerve injury and inflammation. |
| 2599 | 10495105 | In this article, we introduce two novel members of the sensory neuropeptide family: pituitary adenylate cyclase-activating polypeptide (PACAP) and islet amyloid polypeptide (IAPP). |
| 2600 | 10495105 | Whereas PACAP, a vasoactive intestinal polypeptide-resembling peptide, predominantly occurs in neuronal elements, IAPP, which is structurally related to calcitonin gene-related peptide, is most widely known as a pancreatic beta-cell peptide; as such, it has been recognized as a constituent of amyloid deposits in type 2 diabetes. |
| 2601 | 10495105 | Pituitary adenylate cyclase-activating polypeptide and islet amyloid polypeptide in primary sensory neurons: functional implications from plasticity in expression on nerve injury and inflammation. |
| 2602 | 10495105 | In this article, we introduce two novel members of the sensory neuropeptide family: pituitary adenylate cyclase-activating polypeptide (PACAP) and islet amyloid polypeptide (IAPP). |
| 2603 | 10495105 | Whereas PACAP, a vasoactive intestinal polypeptide-resembling peptide, predominantly occurs in neuronal elements, IAPP, which is structurally related to calcitonin gene-related peptide, is most widely known as a pancreatic beta-cell peptide; as such, it has been recognized as a constituent of amyloid deposits in type 2 diabetes. |
| 2604 | 10495105 | Pituitary adenylate cyclase-activating polypeptide and islet amyloid polypeptide in primary sensory neurons: functional implications from plasticity in expression on nerve injury and inflammation. |
| 2605 | 10495105 | In this article, we introduce two novel members of the sensory neuropeptide family: pituitary adenylate cyclase-activating polypeptide (PACAP) and islet amyloid polypeptide (IAPP). |
| 2606 | 10495105 | Whereas PACAP, a vasoactive intestinal polypeptide-resembling peptide, predominantly occurs in neuronal elements, IAPP, which is structurally related to calcitonin gene-related peptide, is most widely known as a pancreatic beta-cell peptide; as such, it has been recognized as a constituent of amyloid deposits in type 2 diabetes. |
| 2607 | 10512360 | Two novel immortal pancreatic beta-cell lines expressing and secreting human islet amyloid polypeptide do not spontaneously develop islet amyloid. |
| 2608 | 10512360 | Type 2 diabetes is characterized by islet amyloid deposits, which are primarily composed of the amyloidogenic human form of islet amyloid polypeptide (IAPP, amylin). |
| 2609 | 10512360 | The mechanism of islet amyloido-genesis is not known, but other products (e.g., apolipoprotein E and perlecan) contained within islet amyloid may be necessary. |
| 2610 | 10512360 | Two novel immortal pancreatic beta-cell lines expressing and secreting human islet amyloid polypeptide do not spontaneously develop islet amyloid. |
| 2611 | 10512360 | Type 2 diabetes is characterized by islet amyloid deposits, which are primarily composed of the amyloidogenic human form of islet amyloid polypeptide (IAPP, amylin). |
| 2612 | 10512360 | The mechanism of islet amyloido-genesis is not known, but other products (e.g., apolipoprotein E and perlecan) contained within islet amyloid may be necessary. |
| 2613 | 10512360 | Two novel immortal pancreatic beta-cell lines expressing and secreting human islet amyloid polypeptide do not spontaneously develop islet amyloid. |
| 2614 | 10512360 | Type 2 diabetes is characterized by islet amyloid deposits, which are primarily composed of the amyloidogenic human form of islet amyloid polypeptide (IAPP, amylin). |
| 2615 | 10512360 | The mechanism of islet amyloido-genesis is not known, but other products (e.g., apolipoprotein E and perlecan) contained within islet amyloid may be necessary. |
| 2616 | 10517745 | C-Reactive protein, serum amyloid A protein, and coronary events. |
| 2617 | 10554571 | Last observations suggest the new potential pathogenic factors such as: cellular membrane ATP-ase and structure dysfunction changes, lipotoxicity on pancreatic beta cell, increase secretion of islet amyloid polypeptide and genetic defects. |
| 2618 | 10656810 | Identification of a penta- and hexapeptide of islet amyloid polypeptide (IAPP) with amyloidogenic and cytotoxic properties. |
| 2619 | 10656810 | Pancreatic amyloid is formed by the aggregation of islet amyloid polypeptide (hIAPP or amylin), which is a 37-residue peptide. |
| 2620 | 10656810 | Identification of a penta- and hexapeptide of islet amyloid polypeptide (IAPP) with amyloidogenic and cytotoxic properties. |
| 2621 | 10656810 | Pancreatic amyloid is formed by the aggregation of islet amyloid polypeptide (hIAPP or amylin), which is a 37-residue peptide. |
| 2622 | 10669788 | Aggregation of an amyloidogenic fragment of human islet amyloid polypeptide. |
| 2623 | 10669788 | Native human islet amyloid polypeptide (hIAPP) has been identified as the major component of amyloid plaques found in the pancreatic islets of Langerhans of persons affected by type 2 diabetes mellitus. |
| 2624 | 10669788 | Aggregation of an amyloidogenic fragment of human islet amyloid polypeptide. |
| 2625 | 10669788 | Native human islet amyloid polypeptide (hIAPP) has been identified as the major component of amyloid plaques found in the pancreatic islets of Langerhans of persons affected by type 2 diabetes mellitus. |
| 2626 | 10751203 | Islet amyloid polypeptide (amylin)-deficient mice develop a more severe form of alloxan-induced diabetes. |
| 2627 | 10751203 | To examine whether islet amyloid polypeptide (IAPP), other than through amyloid formation, may be of importance in diabetes pathogenesis, IAPP-deficient mice (IAPP(-/-)) were challenged with alloxan (day 0). |
| 2628 | 10751203 | Islet amyloid polypeptide (amylin)-deficient mice develop a more severe form of alloxan-induced diabetes. |
| 2629 | 10751203 | To examine whether islet amyloid polypeptide (IAPP), other than through amyloid formation, may be of importance in diabetes pathogenesis, IAPP-deficient mice (IAPP(-/-)) were challenged with alloxan (day 0). |
| 2630 | 10831234 | Islet amyloid polypeptide (amylin) modulates chylomicron metabolism in rats. |
| 2631 | 10831234 | Amylin is a pancreatic peptide that has been shown to be able to induce a state of peripheral insulin resistance. |
| 2632 | 10831234 | Amylin can reduce chylomicron uptake, most probably by regulating lipoprotein receptors either directly, or via modulation of insulin activity. |
| 2633 | 10853552 | The carpal tunnel syndrome is frequent in hemodialysis patients, and surgery gives the opportunity to look for beta-2-microglobulin amyloid deposits. |
| 2634 | 10889799 | Excess insulin secretion may eventually reduce beta-cell function due to amyloid deposition, leading to raised blood glucose and further deterioration of beta-cell function and insulin sensitivity via glucose toxicity. |
| 2635 | 10903851 | We have previously demonstrated that transthyretin amyloid fibrils contain four constituent protofilaments packed in a square array. |
| 2636 | 10903851 | Here, we have used cross-correlation techniques to average electron microscopy images of multiple cross-sections in order to reconstruct the sub-structure of ex vivo amyloid fibrils composed of amyloid A protein, monoclonal immunoglobulin lambda light chain, Leu60Arg variant apolipoprotein AI, and Asp67His variant lysozyme, as well as synthetic fibrils derived from a ten-residue peptide corresponding to the A-strand of transthyretin. |
| 2637 | 10903851 | We have previously demonstrated that transthyretin amyloid fibrils contain four constituent protofilaments packed in a square array. |
| 2638 | 10903851 | Here, we have used cross-correlation techniques to average electron microscopy images of multiple cross-sections in order to reconstruct the sub-structure of ex vivo amyloid fibrils composed of amyloid A protein, monoclonal immunoglobulin lambda light chain, Leu60Arg variant apolipoprotein AI, and Asp67His variant lysozyme, as well as synthetic fibrils derived from a ten-residue peptide corresponding to the A-strand of transthyretin. |
| 2639 | 10907112 | Islet amyloid polypeptide in the islets of Langerhans: friend or foe? |
| 2640 | 10907112 | Islet amyloid polypeptide (IAPP), or amylin, was originally discovered as the constituent peptide in amyloid occurring in human insulinomas and in pancreatic islets in human subjects with Type II (non-insulin-dependent) diabetes mellitus. |
| 2641 | 10907112 | Islet amyloid polypeptide in the islets of Langerhans: friend or foe? |
| 2642 | 10907112 | Islet amyloid polypeptide (IAPP), or amylin, was originally discovered as the constituent peptide in amyloid occurring in human insulinomas and in pancreatic islets in human subjects with Type II (non-insulin-dependent) diabetes mellitus. |
| 2643 | 10931181 | Processing of synthetic pro-islet amyloid polypeptide (proIAPP) 'amylin' by recombinant prohormone convertase enzymes, PC2 and PC3, in vitro. |
| 2644 | 10931181 | Islet amyloid polypeptide (IAPP), amylin, is the constituent peptide of pancreatic islet amyloid deposits which form in islets of Type 2 diabetic subjects. |
| 2645 | 10931181 | To determine the enzymes responsible for proteolysis and their activity at the potential cleavage sites, synthetic human proIAPP was incubated (0.5-16 h) with recombinant prohormone convertases, PC2 or PC3 at appropriate conditions of calcium and pH. |
| 2646 | 10931181 | PC3 was active initially at the N-terminal-IAPP junction and later at the C-terminus, whereas initial PC2 activity was at the IAPP-C-terminal junction. |
| 2647 | 10931181 | There was no evidence for substantial competition for the processing enzymes when the combined substrates proinsulin and proIAPP were incubated with both PC2 and PC3. |
| 2648 | 10931181 | As proinsulin cleavage is sequential in vivo (PC3 active at the B-chain-C-peptide junction, followed by PC2 at A chain-C-peptide junction), these data suggest that proteolysis of proIAPP and proinsulin is coincident in secretory granules and increased proinsulin secretion in diabetes could be accompanied by increased production of proIAPP. |
| 2649 | 10931181 | Processing of synthetic pro-islet amyloid polypeptide (proIAPP) 'amylin' by recombinant prohormone convertase enzymes, PC2 and PC3, in vitro. |
| 2650 | 10931181 | Islet amyloid polypeptide (IAPP), amylin, is the constituent peptide of pancreatic islet amyloid deposits which form in islets of Type 2 diabetic subjects. |
| 2651 | 10931181 | To determine the enzymes responsible for proteolysis and their activity at the potential cleavage sites, synthetic human proIAPP was incubated (0.5-16 h) with recombinant prohormone convertases, PC2 or PC3 at appropriate conditions of calcium and pH. |
| 2652 | 10931181 | PC3 was active initially at the N-terminal-IAPP junction and later at the C-terminus, whereas initial PC2 activity was at the IAPP-C-terminal junction. |
| 2653 | 10931181 | There was no evidence for substantial competition for the processing enzymes when the combined substrates proinsulin and proIAPP were incubated with both PC2 and PC3. |
| 2654 | 10931181 | As proinsulin cleavage is sequential in vivo (PC3 active at the B-chain-C-peptide junction, followed by PC2 at A chain-C-peptide junction), these data suggest that proteolysis of proIAPP and proinsulin is coincident in secretory granules and increased proinsulin secretion in diabetes could be accompanied by increased production of proIAPP. |
| 2655 | 10960722 | Parallel changes of proinsulin and islet amyloid polypeptide in glucose intolerance. |
| 2656 | 10960722 | Elevated proinsulin secretion and islet amyloid deposition are both features of Type 2 diabetes but their relationship to beta-cell dysfunction is unknown. |
| 2657 | 10960722 | To determine if islet amyloid polypeptide (IAPP) secretion is disproportionate with other beta-cell products at any stage of glucose intolerance, 116 subjects were studied. |
| 2658 | 10960722 | Parallel changes of proinsulin and islet amyloid polypeptide in glucose intolerance. |
| 2659 | 10960722 | Elevated proinsulin secretion and islet amyloid deposition are both features of Type 2 diabetes but their relationship to beta-cell dysfunction is unknown. |
| 2660 | 10960722 | To determine if islet amyloid polypeptide (IAPP) secretion is disproportionate with other beta-cell products at any stage of glucose intolerance, 116 subjects were studied. |
| 2661 | 10960722 | Parallel changes of proinsulin and islet amyloid polypeptide in glucose intolerance. |
| 2662 | 10960722 | Elevated proinsulin secretion and islet amyloid deposition are both features of Type 2 diabetes but their relationship to beta-cell dysfunction is unknown. |
| 2663 | 10960722 | To determine if islet amyloid polypeptide (IAPP) secretion is disproportionate with other beta-cell products at any stage of glucose intolerance, 116 subjects were studied. |
| 2664 | 10969830 | The c-Jun amino-terminal kinase pathway is preferentially activated by interleukin-1 and controls apoptosis in differentiating pancreatic beta-cells. |
| 2665 | 10969830 | To characterize the differentiation events that selectively target insulin-producing cells to interleukin (IL)-1beta-induced apoptosis, we studied IL-1beta signaling via mitogen-activated protein kinase (MAPK) and stress-activated protein kinase in 2 pancreatic endocrine cell lines. |
| 2666 | 10969830 | We studied the glucagon-secreting AN-glu cell line and the insulin and the islet amyloid polypeptide-producing beta-cell line (AN-ins cells), which is derived by stable transfection of AN-glu cells with the transcription factor pancreatic duodenal homeobox factor-1. |
| 2667 | 10969830 | This increased sensitivity was not associated with a more pronounced IL-l-induced nitric oxide production in AN-ins cells, but it correlated with a more marked activation of the 3 MAPKs extracellular signal-regulated kinases (ERKs)-1/2, c-Jun NH2-terminal kinase (JNK), and p38 MAPK (p38). |
| 2668 | 10969830 | This led to increased phosphorylation of the transcription factors c-Jun, Elk-1, and ATF2 and of heat shock protein 25. |
| 2669 | 10969830 | Inhibition of ERK-1/2 and p38 did not prevent but aggravated IL-1beta-induced cell death. |
| 2670 | 10969830 | Cell death could be elicited by overexpressing the catalytic domain of MAPK kinase kinase 1, a specific activator of JNK and nuclear factor-kappaB, which does not recruit ERK-1/2 or p38. |
| 2671 | 10969830 | Coactivation of ERK-1/2 with JNK did not prevent apoptosis. |
| 2672 | 10969830 | In conclusion, increased MAPK signaling in response to IL-1beta may represent a novel molecular marker of beta-cell differentiation. |
| 2673 | 10969831 | The constitutive secretory pathway is a major route for islet amyloid polypeptide secretion in neonatal but not adult rat islet cells. |
| 2674 | 10969831 | Islet amyloid polypeptide (IAPP or amylin) is a normal secretory product of the pancreatic beta-cell that is cosecreted with insulin and is the major constituent of islet amyloid deposits in individuals with type 2 diabetes or insulinomas. |
| 2675 | 10969831 | The constitutive secretory pathway is a major route for islet amyloid polypeptide secretion in neonatal but not adult rat islet cells. |
| 2676 | 10969831 | Islet amyloid polypeptide (IAPP or amylin) is a normal secretory product of the pancreatic beta-cell that is cosecreted with insulin and is the major constituent of islet amyloid deposits in individuals with type 2 diabetes or insulinomas. |
| 2677 | 10973971 | Degradation of amylin by insulin-degrading enzyme. |
| 2678 | 10973971 | A pathological feature of Type 2 diabetes is deposits in the pancreatic islets primarily composed of amylin (islet amyloid polypeptide). |
| 2679 | 10973971 | Recent reports suggest that insulin-degrading enzyme (IDE) may have specificity for amyloidogenic proteins, and therefore we sought to determine whether amylin is an IDE substrate. |
| 2680 | 10973971 | Metalloproteinase inhibitors inactivated amylin-degrading activity with a pattern consistent with the enzymatic properties of IDE, whereas inhibitors of acid and serine proteases, calpains, and the proteasome were ineffective. |
| 2681 | 10973971 | Amylin degradation was inhibited by insulin in a dose-dependent manner, whereas insulin degradation was inhibited by amylin. |
| 2682 | 10973971 | Other substrates of IDE such as atrial natriuretic peptide and glucagon also competitively inhibited amylin degradation. |
| 2683 | 10973971 | Finally, a monoclonal anti-IDE antibody immunoprecipitated both insulin- and amylin-degrading activities. |
| 2684 | 10973971 | The data strongly suggest that IDE is an amylin-degrading enzyme and plays an important role in the clearance of amylin and the prevention of islet amyloid formation. |
| 2685 | 10973971 | Degradation of amylin by insulin-degrading enzyme. |
| 2686 | 10973971 | A pathological feature of Type 2 diabetes is deposits in the pancreatic islets primarily composed of amylin (islet amyloid polypeptide). |
| 2687 | 10973971 | Recent reports suggest that insulin-degrading enzyme (IDE) may have specificity for amyloidogenic proteins, and therefore we sought to determine whether amylin is an IDE substrate. |
| 2688 | 10973971 | Metalloproteinase inhibitors inactivated amylin-degrading activity with a pattern consistent with the enzymatic properties of IDE, whereas inhibitors of acid and serine proteases, calpains, and the proteasome were ineffective. |
| 2689 | 10973971 | Amylin degradation was inhibited by insulin in a dose-dependent manner, whereas insulin degradation was inhibited by amylin. |
| 2690 | 10973971 | Other substrates of IDE such as atrial natriuretic peptide and glucagon also competitively inhibited amylin degradation. |
| 2691 | 10973971 | Finally, a monoclonal anti-IDE antibody immunoprecipitated both insulin- and amylin-degrading activities. |
| 2692 | 10973971 | The data strongly suggest that IDE is an amylin-degrading enzyme and plays an important role in the clearance of amylin and the prevention of islet amyloid formation. |
| 2693 | 10975716 | Amyloid in human islets of Langerhans: immunologic evidence that islet amyloid polypeptide is modified in amyloidogenesis. |
| 2694 | 10975716 | Amyloid derived from the beta-cell product islet amyloid polypeptide (IAPP) has been implicated for a beta-cell lesion in Type II diabetes mellitus. |
| 2695 | 10975716 | Amyloid in human islets of Langerhans: immunologic evidence that islet amyloid polypeptide is modified in amyloidogenesis. |
| 2696 | 10975716 | Amyloid derived from the beta-cell product islet amyloid polypeptide (IAPP) has been implicated for a beta-cell lesion in Type II diabetes mellitus. |
| 2697 | 11038774 | [The impact of the missense mutation-ser20gly in islet amyloid polypeptide gene on NIDDM in Chinese]. |
| 2698 | 11069207 | Islet amyloid polypeptide (IAPP) decreased to approximately 41% and approximately 24% of basal values during hypoglycemia and rapidly rose approximately 4.7-fold during the recovery period, while plasma C-peptide remained suppressed in both groups. |
| 2699 | 11072517 | The 37 amino acids 'islet amyloid polypeptide' (IAPP) was discovered in 1986 as the building block of islet amyloid. |
| 2700 | 11072517 | Islet amyloid has turned out to be a pathogenic factor, which is accompanied by death of beta-cells and reduction of the insulin producing capacity. |
| 2701 | 11072517 | The 37 amino acids 'islet amyloid polypeptide' (IAPP) was discovered in 1986 as the building block of islet amyloid. |
| 2702 | 11072517 | Islet amyloid has turned out to be a pathogenic factor, which is accompanied by death of beta-cells and reduction of the insulin producing capacity. |
| 2703 | 11094339 | Amyloidogenicity of recombinant human pro-islet amyloid polypeptide (ProIAPP). |
| 2704 | 11095107 | Pro islet amyloid polypeptide (ProIAPP) immunoreactivity in the islets of Langerhans. |
| 2705 | 11095107 | The islet amyloid fibril consists of the 37-amino-acid islet amyloid polypeptide (IAPP) but its pathogenesis is only partly understood. |
| 2706 | 11095107 | Pro islet amyloid polypeptide (ProIAPP) immunoreactivity in the islets of Langerhans. |
| 2707 | 11095107 | The islet amyloid fibril consists of the 37-amino-acid islet amyloid polypeptide (IAPP) but its pathogenesis is only partly understood. |
| 2708 | 11106586 | The domestic cat, by virtue of the fact that it is one of the few species that spontaneously develop a form of diabetes mellitus that closely resembles human type 2 diabetes, including the formation of amyloid deposits derived from islet amyloid polypeptide (IAPP), was considered to be an excellent candidate species in which to attempt to develop a nontransgenic animal model for this disease process. |
| 2709 | 11106586 | At the end of the study all 4 glipizide-treated cats had islet amyloid deposits, whereas only 1 of 4 insulin-treated cats had detectable amyloid. |
| 2710 | 11106586 | The domestic cat, by virtue of the fact that it is one of the few species that spontaneously develop a form of diabetes mellitus that closely resembles human type 2 diabetes, including the formation of amyloid deposits derived from islet amyloid polypeptide (IAPP), was considered to be an excellent candidate species in which to attempt to develop a nontransgenic animal model for this disease process. |
| 2711 | 11106586 | At the end of the study all 4 glipizide-treated cats had islet amyloid deposits, whereas only 1 of 4 insulin-treated cats had detectable amyloid. |
| 2712 | 11108954 | Receptor for advanced glycation end products (RAGE) is a multiligand member of the immunoglobulin superfamily of cell surface molecules whose repertoire of ligands includes advanced glycation end products (AGEs), amyloid fibrils, amphoterins and S100/calgranulins. |
| 2713 | 11108954 | For example, increased levels of AGEs in diabetes and renal insufficiency, amyloid fibrils in Alzheimer's disease brain, amphoterin in tumors and S100/calgranulins at sites of inflammation have been identified. |
| 2714 | 11108954 | Receptor for advanced glycation end products (RAGE) is a multiligand member of the immunoglobulin superfamily of cell surface molecules whose repertoire of ligands includes advanced glycation end products (AGEs), amyloid fibrils, amphoterins and S100/calgranulins. |
| 2715 | 11108954 | For example, increased levels of AGEs in diabetes and renal insufficiency, amyloid fibrils in Alzheimer's disease brain, amphoterin in tumors and S100/calgranulins at sites of inflammation have been identified. |
| 2716 | 11113614 | There is evidence that the reductions in the availability of both glucose/energy and insulin contribute to the formation of amyloidogenic derivatives and hyperphosphorylated tau protein. |
| 2717 | 11113614 | This may indicate that the amyloid cascade hypothesis in not valid for sporadic Alzheimer disease but that the formation of both, amyloidogenic derivatives and hyperphosphorylated tau protein is downstream the origin of this neurodegenerative disease. |
| 2718 | 11118882 | This promoter region contains sequence motifs that have been shown to be involved in beta-cell-specific expression of insulin, Pdx1 and islet amyloid polypeptide (IAPP). |
| 2719 | 11124436 | Molecular misreading was discovered in the rat vasopressin gene associated with diabetes insipidus and subsequently in human genes linked to Alzheimer's disease (AD), e.g. beta amyloid precursor protein (betaAPP) and ubiquitin-B (UBB). |
| 2720 | 11135321 | In order to further investigate islet function and secretion during early development of pancreatic cancer, we measured the concentrations of insulin, glucagon, somatostatin, and islet amyloid polypeptide (IAPP) in plasma, pancreatic tissue, and secretin-stimulated pancreatic juice at 12 and 27 weeks after the ductal-cell-specific carcinogen, BOP had been used to induce tumors in Syrian golden hamsters. |
| 2721 | 11145110 | Differential changes in islet amyloid polypeptide (amylin) and insulin mRNA expression after high-fat diet-induced insulin resistance in C57BL/6J mice. |
| 2722 | 11145110 | Islet amyloid, derived from islet amyloid polypeptide (IAPP or amylin), frequently occurs in type 2 diabetes. |
| 2723 | 11145110 | Differential changes in islet amyloid polypeptide (amylin) and insulin mRNA expression after high-fat diet-induced insulin resistance in C57BL/6J mice. |
| 2724 | 11145110 | Islet amyloid, derived from islet amyloid polypeptide (IAPP or amylin), frequently occurs in type 2 diabetes. |
| 2725 | 11145957 | Identification of a heparin binding domain in the N-terminal cleavage site of pro-islet amyloid polypeptide. |
| 2726 | 11145957 | Islet amyloid deposits are a characteristic pathologic lesion of the pancreas in type 2 diabetes and are composed primarily of the islet beta cell peptide islet amyloid polypeptide (IAPP or amylin) as well as the basement membrane heparan sulfate proteoglycan perlecan. |
| 2727 | 11145957 | Identification of a heparin binding domain in the N-terminal cleavage site of pro-islet amyloid polypeptide. |
| 2728 | 11145957 | Islet amyloid deposits are a characteristic pathologic lesion of the pancreas in type 2 diabetes and are composed primarily of the islet beta cell peptide islet amyloid polypeptide (IAPP or amylin) as well as the basement membrane heparan sulfate proteoglycan perlecan. |
| 2729 | 11147796 | The Zucker diabetic fatty (ZDF) rat is a model of type 2 diabetes and, like the human disease, has both insulin resistance (from a mutant leptin receptor causing obesity) and inadequate beta-cell compensation. |
| 2730 | 11147796 | To test for an independently inherited beta-cell defect, we examined beta-cell function in fetuses of ZDF-lean rats, which have wild-type leptin receptors. beta-Cell number and insulin content do not differ among wild-type, heterozygous, and homozygous ZDF-lean fetuses. |
| 2731 | 11147796 | This is not a generalized defect in gene expression nor an altered transfection efficiency, because the islet amyloid polypeptide promoter and viral promoters are unaffected. |
| 2732 | 11147796 | This study demonstrates that the ZDF rat carries a genetic defect in beta-cell transcription that is inherited independently from the leptin receptor mutation and insulin resistance. |
| 2733 | 11150482 | In this study, we established a polyclonal anti-RAGE antibody, and examined the immunohistochemical localization of amyloid beta protein (Abeta), AGE, and RAGE in neurons and astrocytes from patients with AD and DM. |
| 2734 | 11150482 | Abeta-, AGE-, and RAGE-positive granules were identified in the perikaryon of hippocampal neurons (especially from CA3 and CA4) in all subjects. |
| 2735 | 11193791 | Such changes include increased levels of oxidative stress, perturbed energy metabolism, and accumulation of insoluble (oxidatively modified) proteins (prominent among which are amyloid beta-peptide and tau). |
| 2736 | 11215678 | However, with sustained periods of insulin resistance, islet amyloid polypeptide (IAPP) is deposited in islets and can replace normal islet architecture, resulting in an insulin-deficient state. |
| 2737 | 11230804 | Inhibition of human pancreatic islet insulin release by receptor-selective somatostatin analogs directed to somatostatin receptor subtype 5. |
| 2738 | 11230804 | Somatostatin (SS)-14 and SS28 are produced by pancreatic D cells and gut mucosa and inhibit pancreatic islet insulin and glucagon release. |
| 2739 | 11230804 | Glucose-stimulated insulin secretion in human islets incubated for 1 hr at 20 mM glucose, and in islets cultured for 24 hr at a near-physiological (6.1 mM) glucose concentration, was inhibited (<50% of the control) by SSTR5-specific analogs and by SS14 and SS28. |
| 2740 | 11230804 | SS14, SS28, and different SSTR5 preferential analogs also inhibited islet amyloid polypeptide release during the 24-hr culture. |
| 2741 | 11230804 | On the other hand, a group of SSTR2-selective analogs failed to inhibit insulin release. |
| 2742 | 11230804 | Analysis by reverse transcription-polymerase chain reaction indicated that human islets express similar amounts of SSTR2 and SSTR5 mRNAs, while human pancreatic ductal cells express much lower levels of these mRNAs. |
| 2743 | 11230804 | In conclusion, our data suggest that SSTR5 is an important mediator of the insulin inhibitory action of SS in cultured human islets. |
| 2744 | 11246872 | The prohormone convertase enzyme 2 (PC2) is essential for processing pro-islet amyloid polypeptide at the NH2-terminal cleavage site. |
| 2745 | 11246872 | Impaired processing of pro-islet amyloid polypeptide (proIAPP), the precursor of the beta-cell peptide islet amyloid polypeptide (IAPP) (amylin), has been implicated in islet amyloid formation in type 2 diabetes. |
| 2746 | 11246872 | The prohormone convertase enzymes PC3 (also known as PC1) and PC2 are localized to beta-cell secretory granules with proIAPP and proinsulin and are responsible for proinsulin processing. |
| 2747 | 11246872 | These data indicate that PC2 is essential for processing of proIAPP at the NH2-terminal cleavage site in vivo and that PC3 is likely only capable of processing proIAPP at the COOH-terminal cleavage site. |
| 2748 | 11246872 | The prohormone convertase enzyme 2 (PC2) is essential for processing pro-islet amyloid polypeptide at the NH2-terminal cleavage site. |
| 2749 | 11246872 | Impaired processing of pro-islet amyloid polypeptide (proIAPP), the precursor of the beta-cell peptide islet amyloid polypeptide (IAPP) (amylin), has been implicated in islet amyloid formation in type 2 diabetes. |
| 2750 | 11246872 | The prohormone convertase enzymes PC3 (also known as PC1) and PC2 are localized to beta-cell secretory granules with proIAPP and proinsulin and are responsible for proinsulin processing. |
| 2751 | 11246872 | These data indicate that PC2 is essential for processing of proIAPP at the NH2-terminal cleavage site in vivo and that PC3 is likely only capable of processing proIAPP at the COOH-terminal cleavage site. |
| 2752 | 11272181 | It reviews recent studies in IAPP (islet-amyloid polypeptide, or amylin) transgenic mice developing islet amyloid deposits and hyperglycemia to suggest that the process of amyloid fibril formation impairs function early and leads to beta-cell failure and eventual death. |
| 2753 | 11272181 | Based on the known association of amyloid deposits and relative hyperproinsulinemia, it is hypothesized that fibril formation begins during impaired glucose tolerance after other factors cause the initial defects in early insulin secretion and insulin action. |
| 2754 | 11272181 | It reviews recent studies in IAPP (islet-amyloid polypeptide, or amylin) transgenic mice developing islet amyloid deposits and hyperglycemia to suggest that the process of amyloid fibril formation impairs function early and leads to beta-cell failure and eventual death. |
| 2755 | 11272181 | Based on the known association of amyloid deposits and relative hyperproinsulinemia, it is hypothesized that fibril formation begins during impaired glucose tolerance after other factors cause the initial defects in early insulin secretion and insulin action. |
| 2756 | 11272183 | Longitudinal studies in Macaca mulatta monkeys show that insulin resistance is accompanied by increased islet mass and onset of diabetes is associated with deposition of amyloid and reduction of beta-cells. |
| 2757 | 11272184 | The percentage of amyloid-infiltrated islets varied from 0.4 to 74%. beta-Cells from amyloid-containing islets still had specific Golgi proinsulin labeling. |
| 2758 | 11272184 | Proinsulin mRNA was significantly reduced in islets with amyloid deposits when compared with amyloid-free islets, but the mean reduction did not exceed 16%. |
| 2759 | 11272184 | Insulin was still present in the beta-cells of amyloid-containing islets, and its amount, estimated by measurement of the insulin-labeling optical density, was not statistically different from that in amyloid-free islets. |
| 2760 | 11272184 | In conclusion, even in amyloid-containing islets, beta-cells maintain active insulin transcription and translation and normal insulin storage. |
| 2761 | 11272184 | Taking into account that in most cases only a small proportion of islets are infiltrated by amyloid, the limited reduction in proinsulin mRNA is unlikely to play a major role in the pathogenesis of diabetes. |
| 2762 | 11272184 | The percentage of amyloid-infiltrated islets varied from 0.4 to 74%. beta-Cells from amyloid-containing islets still had specific Golgi proinsulin labeling. |
| 2763 | 11272184 | Proinsulin mRNA was significantly reduced in islets with amyloid deposits when compared with amyloid-free islets, but the mean reduction did not exceed 16%. |
| 2764 | 11272184 | Insulin was still present in the beta-cells of amyloid-containing islets, and its amount, estimated by measurement of the insulin-labeling optical density, was not statistically different from that in amyloid-free islets. |
| 2765 | 11272184 | In conclusion, even in amyloid-containing islets, beta-cells maintain active insulin transcription and translation and normal insulin storage. |
| 2766 | 11272184 | Taking into account that in most cases only a small proportion of islets are infiltrated by amyloid, the limited reduction in proinsulin mRNA is unlikely to play a major role in the pathogenesis of diabetes. |
| 2767 | 11272184 | The percentage of amyloid-infiltrated islets varied from 0.4 to 74%. beta-Cells from amyloid-containing islets still had specific Golgi proinsulin labeling. |
| 2768 | 11272184 | Proinsulin mRNA was significantly reduced in islets with amyloid deposits when compared with amyloid-free islets, but the mean reduction did not exceed 16%. |
| 2769 | 11272184 | Insulin was still present in the beta-cells of amyloid-containing islets, and its amount, estimated by measurement of the insulin-labeling optical density, was not statistically different from that in amyloid-free islets. |
| 2770 | 11272184 | In conclusion, even in amyloid-containing islets, beta-cells maintain active insulin transcription and translation and normal insulin storage. |
| 2771 | 11272184 | Taking into account that in most cases only a small proportion of islets are infiltrated by amyloid, the limited reduction in proinsulin mRNA is unlikely to play a major role in the pathogenesis of diabetes. |
| 2772 | 11272184 | The percentage of amyloid-infiltrated islets varied from 0.4 to 74%. beta-Cells from amyloid-containing islets still had specific Golgi proinsulin labeling. |
| 2773 | 11272184 | Proinsulin mRNA was significantly reduced in islets with amyloid deposits when compared with amyloid-free islets, but the mean reduction did not exceed 16%. |
| 2774 | 11272184 | Insulin was still present in the beta-cells of amyloid-containing islets, and its amount, estimated by measurement of the insulin-labeling optical density, was not statistically different from that in amyloid-free islets. |
| 2775 | 11272184 | In conclusion, even in amyloid-containing islets, beta-cells maintain active insulin transcription and translation and normal insulin storage. |
| 2776 | 11272184 | Taking into account that in most cases only a small proportion of islets are infiltrated by amyloid, the limited reduction in proinsulin mRNA is unlikely to play a major role in the pathogenesis of diabetes. |
| 2777 | 11272184 | The percentage of amyloid-infiltrated islets varied from 0.4 to 74%. beta-Cells from amyloid-containing islets still had specific Golgi proinsulin labeling. |
| 2778 | 11272184 | Proinsulin mRNA was significantly reduced in islets with amyloid deposits when compared with amyloid-free islets, but the mean reduction did not exceed 16%. |
| 2779 | 11272184 | Insulin was still present in the beta-cells of amyloid-containing islets, and its amount, estimated by measurement of the insulin-labeling optical density, was not statistically different from that in amyloid-free islets. |
| 2780 | 11272184 | In conclusion, even in amyloid-containing islets, beta-cells maintain active insulin transcription and translation and normal insulin storage. |
| 2781 | 11272184 | Taking into account that in most cases only a small proportion of islets are infiltrated by amyloid, the limited reduction in proinsulin mRNA is unlikely to play a major role in the pathogenesis of diabetes. |
| 2782 | 11272188 | Oophorectomy promotes islet amyloid formation in human islet amyloid polypeptide transgenic mice. |
| 2783 | 11291934 | High glucose concentration favors the selective secretion of islet amyloid polypeptide through a constitutive secretory pathway in human pancreatic islets. |
| 2784 | 11291934 | We studied the contribution of the constitutive and the regulated pathways to the total secretion of islet amyloid polypeptide (IAPP) in human pancreatic islets after prolonged culture at either 5.5 or 24.4 mM glucose. |
| 2785 | 11291934 | High glucose concentration favors the selective secretion of islet amyloid polypeptide through a constitutive secretory pathway in human pancreatic islets. |
| 2786 | 11291934 | We studied the contribution of the constitutive and the regulated pathways to the total secretion of islet amyloid polypeptide (IAPP) in human pancreatic islets after prolonged culture at either 5.5 or 24.4 mM glucose. |
| 2787 | 11301286 | Tumor necrosis factor (TNF)-converting enzyme (TACE) and other ADAM proteases (those that contain a disintegrin and a metalloprotease domain) have emerged as potential therapeutic targets in the areas of arthritis, cancer, diabetes and HIV cachexia. |
| 2788 | 11301286 | TACE is the first ADAM protease to process the known physiological substrate and inflammatory cytokine, membrane-bound precursor-TNF-alpha, to its mature soluble form. |
| 2789 | 11301286 | Subsequently, TACE was shown to be required for several different processing events such as tumor growth factor-alpha (TGF-alpha) precursor and amyloid precursor protein (APP) cleavage. |
| 2790 | 11318791 | The islet amyloid polypeptide (amylin) gene S20G mutation in Chinese subjects: evidence for associations with type 2 diabetes and cholesterol levels. |
| 2791 | 11327784 | Identification of a novel human islet amyloid polypeptide beta-sheet domain and factors influencing fibrillogenesis. |
| 2792 | 11327784 | Human islet amyloid polypeptide (hIAPP) accumulates as pancreatic amyloid in type 2 diabetes and readily forms fibrils in vitro. |
| 2793 | 11327784 | Identification of a novel human islet amyloid polypeptide beta-sheet domain and factors influencing fibrillogenesis. |
| 2794 | 11327784 | Human islet amyloid polypeptide (hIAPP) accumulates as pancreatic amyloid in type 2 diabetes and readily forms fibrils in vitro. |
| 2795 | 11334439 | This study examines, at the ultrastructural level, whether the fetal porcine endocrine pancreas (insulin, glucagon, somatostatin, and pancreatic polypeptide [PP]- and islet amyloid polypeptide [IAPP]-containing cells) develops normally after transplantation under the kidney capsule in athymic mice. |
| 2796 | 11350174 | Islet amyloid polypeptide: identification of long-range contacts and local order on the fibrillogenesis pathway. |
| 2797 | 11350174 | The principle component of these deposits is an insoluble fibrillar form of a normally soluble 37 residue peptide hormone, islet amyloid polypeptide. |
| 2798 | 11350174 | These are compared to a non-amyloidogenic variant of islet amyloid polypeptide from rat and N-acetyl-tyrosinamide as models of the unfolded state under matched conditions. |
| 2799 | 11350174 | Parallel assessment of fiber formation using the histological dye, ThT, indicate that ordering at the C terminus of islet amyloid polypeptide is coincident with, and thus indicative of, fiber formation. |
| 2800 | 11350174 | Islet amyloid polypeptide: identification of long-range contacts and local order on the fibrillogenesis pathway. |
| 2801 | 11350174 | The principle component of these deposits is an insoluble fibrillar form of a normally soluble 37 residue peptide hormone, islet amyloid polypeptide. |
| 2802 | 11350174 | These are compared to a non-amyloidogenic variant of islet amyloid polypeptide from rat and N-acetyl-tyrosinamide as models of the unfolded state under matched conditions. |
| 2803 | 11350174 | Parallel assessment of fiber formation using the histological dye, ThT, indicate that ordering at the C terminus of islet amyloid polypeptide is coincident with, and thus indicative of, fiber formation. |
| 2804 | 11350174 | Islet amyloid polypeptide: identification of long-range contacts and local order on the fibrillogenesis pathway. |
| 2805 | 11350174 | The principle component of these deposits is an insoluble fibrillar form of a normally soluble 37 residue peptide hormone, islet amyloid polypeptide. |
| 2806 | 11350174 | These are compared to a non-amyloidogenic variant of islet amyloid polypeptide from rat and N-acetyl-tyrosinamide as models of the unfolded state under matched conditions. |
| 2807 | 11350174 | Parallel assessment of fiber formation using the histological dye, ThT, indicate that ordering at the C terminus of islet amyloid polypeptide is coincident with, and thus indicative of, fiber formation. |
| 2808 | 11350174 | Islet amyloid polypeptide: identification of long-range contacts and local order on the fibrillogenesis pathway. |
| 2809 | 11350174 | The principle component of these deposits is an insoluble fibrillar form of a normally soluble 37 residue peptide hormone, islet amyloid polypeptide. |
| 2810 | 11350174 | These are compared to a non-amyloidogenic variant of islet amyloid polypeptide from rat and N-acetyl-tyrosinamide as models of the unfolded state under matched conditions. |
| 2811 | 11350174 | Parallel assessment of fiber formation using the histological dye, ThT, indicate that ordering at the C terminus of islet amyloid polypeptide is coincident with, and thus indicative of, fiber formation. |
| 2812 | 11395927 | Agouti signaling protein stimulates islet amyloid polypeptide (amylin) secretion in pancreatic beta-cells. |
| 2813 | 11395927 | We have shown the human homologue of agouti (agouti signaling protein; ASP) to regulate human adipocyte metabolism and lipid storage via a Ca(2+)-dependent mechanism. |
| 2814 | 11395927 | We have also demonstrated agouti expression in human pancreas, and that ASP stimulates insulin release via a similar Ca(2+)-dependent mechanism. |
| 2815 | 11395927 | Amylin is cosecreted with insulin from beta-cells, and overexpression of human amylin in beta-cells in yellow agouti mutant mice resulted in accelerated pancreatic amyloid deposition, severely impaired beta-cell function, and a diabetic phenotype. |
| 2816 | 11395927 | We report here that ASP stimulates amylin release in both the HIT-T15 beta-cell line and human pancreatic islets in the presence of a wide range of glucose concentrations (0-16.7 mmol/L), similar to its effect on insulin release; this effect was blocked by 30 mumol/L nitrendipine, confirming a Ca(2+)-dependent mechanism. |
| 2817 | 11395927 | Agouti signaling protein stimulates islet amyloid polypeptide (amylin) secretion in pancreatic beta-cells. |
| 2818 | 11395927 | We have shown the human homologue of agouti (agouti signaling protein; ASP) to regulate human adipocyte metabolism and lipid storage via a Ca(2+)-dependent mechanism. |
| 2819 | 11395927 | We have also demonstrated agouti expression in human pancreas, and that ASP stimulates insulin release via a similar Ca(2+)-dependent mechanism. |
| 2820 | 11395927 | Amylin is cosecreted with insulin from beta-cells, and overexpression of human amylin in beta-cells in yellow agouti mutant mice resulted in accelerated pancreatic amyloid deposition, severely impaired beta-cell function, and a diabetic phenotype. |
| 2821 | 11395927 | We report here that ASP stimulates amylin release in both the HIT-T15 beta-cell line and human pancreatic islets in the presence of a wide range of glucose concentrations (0-16.7 mmol/L), similar to its effect on insulin release; this effect was blocked by 30 mumol/L nitrendipine, confirming a Ca(2+)-dependent mechanism. |
| 2822 | 11445568 | Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide. |
| 2823 | 11445568 | The development of type II diabetes was shown to be associated with the formation of amyloid fibrils consisted of the islet amyloid polypeptide (IAPP or amylin). |
| 2824 | 11445568 | Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide. |
| 2825 | 11445568 | The development of type II diabetes was shown to be associated with the formation of amyloid fibrils consisted of the islet amyloid polypeptide (IAPP or amylin). |
| 2826 | 11484088 | A novel mutation in islet amyloid polypeptide (IAPP) gene promoter is associated with Type II diabetes mellitus. |
| 2827 | 11507651 | In the islets, staining intensity of both insulin and islet amyloid polypeptide (IAPP) increased slightly till 10 weeks of age and thereafter decreased rapidly. |
| 2828 | 11507651 | In contrast, the staining intensities of glucagon, somatostatin, and pancreatic polypeptide (PP) did not change. |
| 2829 | 11522748 | Islet amyloid polypeptide is not a satisfactory marker for detecting pancreatic cancer. |
| 2830 | 11546817 | We demonstrate that adipose tissue expresses a number of acute phase reactants at high levels, including serum amyloid A3 (SAA3), alphal-acid glycoprotein, the lipocalin 24p3 as well as plasminogen activator inhibitor-1 (PAI-1). |
| 2831 | 11555835 | Alterations in beta-cell function, such as formation of amyloid from excessive production of amylin and reduced expression of GLUT2, have been suggested to be possible mechanisms. |
| 2832 | 11555835 | We compared in vivo secretory responses of amylin and insulin (n = 37) and expression of GLUT2 in pancreata (n = 10) obtained at surgery between diabetic and nondiabetic patients with and without pancreatic tumors. |
| 2833 | 11679429 | These mice produce the unique amyloidogenic component of human islet amyloid, human islet amyloid polypeptide (hIAPP). |
| 2834 | 11684098 | Inhibitors can arrest the membrane activity of human islet amyloid polypeptide independently of amyloid formation. |
| 2835 | 11684098 | Human islet amyloid polypeptide (hIAPP), co-secreted with insulin from pancreatic beta cells, misfolds to form amyloid deposits in non-insulin-dependent diabetes mellitus (NIDDM). |
| 2836 | 11684098 | Inhibitors can arrest the membrane activity of human islet amyloid polypeptide independently of amyloid formation. |
| 2837 | 11684098 | Human islet amyloid polypeptide (hIAPP), co-secreted with insulin from pancreatic beta cells, misfolds to form amyloid deposits in non-insulin-dependent diabetes mellitus (NIDDM). |
| 2838 | 11720876 | High plasma amylin/islet amyloid polypeptide levels in patients with residual medullary thyroid carcinoma after total thyroidectomy. |
| 2839 | 11731221 | Islet amyloid polypeptide (IAPP, amylin) is secreted from pancreatic islet beta-cells and converted to amyloid deposits in type 2 diabetes. |
| 2840 | 11786016 | Pancreatic amyloid is formed by the aggregation of the 37-residue islet amyloid polypeptide (IAPP) in type II diabetes patients and is cytotoxic. |
| 2841 | 11791616 | Enhanced in vitro production of amyloid-like fibrils from mutant (S20G) islet amyloid polypeptide. |
| 2842 | 11834421 | Pancreas duodenum homeobox-1 (PDX-1) (also known as insulin promoter factor-1, islet/duodenum homeobox-1, somatostatin transactivating factor-1, insulin upstream factor-1 and glucose-sensitive factor) is a transcription factor encoded by a Hox-like homeodomain gene. |
| 2843 | 11834421 | In adult subjects, PDX-1 is essential for normal pancreatic islet function as suggested by its regulatory action on the expression of a number of pancreatic genes, including insulin, somatostatin, islet amyloid polypeptide, the glucose transporter type 2 and glucokinase. |
| 2844 | 11875249 | There is current data supporting the damaging role of intermediate sized toxic amyloid particles to the beta cell resulting in a beta cell defect which contributes to a relative deficiency or loss of insulin secretion. |
| 2845 | 11916915 | A tendency toward beta-cell de-differentiation was also apparent with palmitate: pyruvate carboxylase and mitochondrial glycerol 3-phosphate dehydrogenase were downregulated, whereas lactate dehydrogenase and fructose 1,6-bisphosphatases were induced. |
| 2846 | 11916915 | However, palmitate also increased expression of calcyclin and 25-kDa synaptosomal-associated protein (SNAP25), which control distal secretory processes. |
| 2847 | 11916915 | Oleate and palmitate also induced expression of chemokines (MCP-1 and GRO1 oncogene) and genes of the acute phase response (serum amyloid A3). |
| 2848 | 11916915 | Increases in transcriptional modulators such as ATF3, CCAAT/enhancer binding protein-beta (C/EBPbeta), C/EBPdelta, and c-fos were also seen. |
| 2849 | 11926832 | Islet amyloid polypeptide (IAPP) contributes to the pathogenesis of type II diabetes by depositing as cytotoxic amyloid fibers in the endocrine pancreas. |
| 2850 | 12015594 | Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis. |
| 2851 | 12015594 | The normal plasma protein serum amyloid P component (SAP) binds to fibrils in all types of amyloid deposits, and contributes to the pathogenesis of amyloidosis. |
| 2852 | 12015594 | In order to intervene in this process we have developed a drug, R-1-[6-[R-2-carboxy-pyrrolidin-1-yl]-6-oxo-hexanoyl]pyrrolidine-2-carboxylic acid, that is a competitive inhibitor of SAP binding to amyloid fibrils. |
| 2853 | 12015594 | This mechanism of drug action potently removes SAP from human amyloid deposits in the tissues and may provide a new therapeutic approach to both systemic amyloidosis and diseases associated with local amyloid, including Alzheimer's disease and type 2 diabetes. |
| 2854 | 12015594 | Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis. |
| 2855 | 12015594 | The normal plasma protein serum amyloid P component (SAP) binds to fibrils in all types of amyloid deposits, and contributes to the pathogenesis of amyloidosis. |
| 2856 | 12015594 | In order to intervene in this process we have developed a drug, R-1-[6-[R-2-carboxy-pyrrolidin-1-yl]-6-oxo-hexanoyl]pyrrolidine-2-carboxylic acid, that is a competitive inhibitor of SAP binding to amyloid fibrils. |
| 2857 | 12015594 | This mechanism of drug action potently removes SAP from human amyloid deposits in the tissues and may provide a new therapeutic approach to both systemic amyloidosis and diseases associated with local amyloid, including Alzheimer's disease and type 2 diabetes. |
| 2858 | 12015594 | Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis. |
| 2859 | 12015594 | The normal plasma protein serum amyloid P component (SAP) binds to fibrils in all types of amyloid deposits, and contributes to the pathogenesis of amyloidosis. |
| 2860 | 12015594 | In order to intervene in this process we have developed a drug, R-1-[6-[R-2-carboxy-pyrrolidin-1-yl]-6-oxo-hexanoyl]pyrrolidine-2-carboxylic acid, that is a competitive inhibitor of SAP binding to amyloid fibrils. |
| 2861 | 12015594 | This mechanism of drug action potently removes SAP from human amyloid deposits in the tissues and may provide a new therapeutic approach to both systemic amyloidosis and diseases associated with local amyloid, including Alzheimer's disease and type 2 diabetes. |
| 2862 | 12015594 | Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis. |
| 2863 | 12015594 | The normal plasma protein serum amyloid P component (SAP) binds to fibrils in all types of amyloid deposits, and contributes to the pathogenesis of amyloidosis. |
| 2864 | 12015594 | In order to intervene in this process we have developed a drug, R-1-[6-[R-2-carboxy-pyrrolidin-1-yl]-6-oxo-hexanoyl]pyrrolidine-2-carboxylic acid, that is a competitive inhibitor of SAP binding to amyloid fibrils. |
| 2865 | 12015594 | This mechanism of drug action potently removes SAP from human amyloid deposits in the tissues and may provide a new therapeutic approach to both systemic amyloidosis and diseases associated with local amyloid, including Alzheimer's disease and type 2 diabetes. |
| 2866 | 12028373 | While the disposition index promises to be a useful tool to predict individuals at high risk of developing type 2 diabetes, other factors that contribute to beta-cell dysfunction and mark disease onset and progression include impairments in proinsulin processing and insulin secretion, decreased beta-cell mass and islet amyloid deposition. |
| 2867 | 12031967 | Overexpression of c-Myc in beta-cells of transgenic mice causes proliferation and apoptosis, downregulation of insulin gene expression, and diabetes. |
| 2868 | 12031967 | To test the hypothesis that c-Myc plays an important role in beta-cell growth and differentiation, we generated transgenic mice overexpressing c-Myc in beta-cells under control of the rat insulin II promoter. |
| 2869 | 12031967 | GLUT2 mRNA was decreased, but other beta-cell-associated genes (IAPP [islet amyloid pancreatic polypeptide], PDX-1 [pancreatic and duodenal homeobox-1], and BETA2/NeuroD) were expressed at near-normal levels. |
| 2870 | 12031967 | Immunostaining for both GLUT2 and Nkx6.1 was mainly cytoplasmic. |
| 2871 | 12031967 | In conclusion, these studies demonstrate that activation of c-Myc in beta-cells leads to 1) increased proliferation and apoptosis, 2) initial hyperplasia with amorphous islet organization, and 3) selective downregulation of insulin gene expression and the development of overt diabetes. |
| 2872 | 12031974 | Yeast-2 hybrid screening identified serum amyloid A (SAA), an acute-phase inflammatory response protein, as an interacting protein of Tanis, and this was confirmed by Biacore experiments. |
| 2873 | 12039445 | These ligands include products of nonenzymatic glycation, the Advanced Glycation Endproducts (AGEs, enriched in the diabetic milieu), members of the S100/calgranulin family of proinflammatory mediators, beta-sheet fibrillar structures (characteristic of amyloid) and amphoterin (present at high levels in the tumor bed). |
| 2874 | 12049785 | We show here that these cells express islet amyloid polypeptide and prohormone convertase 1/3 (PC1/3), proteins that are not expressed by mature alpha cells, but are found in beta cells. |
| 2875 | 12049785 | PC1/3 converts proglucagon to the functionally distinct hormones glucagon-like peptide (GLP)-1 and GLP-2 rather than glucagon. |
| 2876 | 12049785 | Despite these differences, the early proglucagon-positive cells express, as do mature alpha cells, the POU domain transcription factor Brn-4, and do not express the beta cell factor pdx-1. |
| 2877 | 12054816 | Design of peptide-based inhibitors of human islet amyloid polypeptide fibrillogenesis. |
| 2878 | 12054816 | Human islet amyloid polypeptide (IAPP) is the major component of amyloid deposits found in the pancreas of over 90% of all cases of type-2 diabetes. |
| 2879 | 12054816 | Design of peptide-based inhibitors of human islet amyloid polypeptide fibrillogenesis. |
| 2880 | 12054816 | Human islet amyloid polypeptide (IAPP) is the major component of amyloid deposits found in the pancreas of over 90% of all cases of type-2 diabetes. |
| 2881 | 12084635 | For example, insulin regulates phosphorylation of tau protein, which underlies neurofibrillary lesions in the brains of AD patients. |
| 2882 | 12084635 | Insulin also affects the metabolism of beta-amyloid, the main constituent of AD amyloid pathology. |
| 2883 | 12086946 | Estrogen can prevent or reverse obesity and diabetes in mice expressing human islet amyloid polypeptide. |
| 2884 | 12086946 | Type 2 diabetes is characterized by loss of beta-cell mass and concomitant deposition of amyloid derived from islet amyloid polypeptide (IAPP). |
| 2885 | 12086946 | Estrogen can prevent or reverse obesity and diabetes in mice expressing human islet amyloid polypeptide. |
| 2886 | 12086946 | Type 2 diabetes is characterized by loss of beta-cell mass and concomitant deposition of amyloid derived from islet amyloid polypeptide (IAPP). |
| 2887 | 12110051 | Sections of paraffin-embedded tissues were evaluated for amyloid with hematoxylin and eosin (HE) and congo red (CR) staining, and using immunohistochemistry for human islet amyloid polypeptide (IAPP), calcitonin gene-related peptide (CGRP), glucagon, pancreatic polypeptide (PP), somatostatin (SS), and porcine insulin. |
| 2888 | 12110051 | Islet amyloid was positive with HE in 40 baboons, with CR in 39 baboons, and with IAPP and CGRP in 35 baboons. |
| 2889 | 12110051 | IAPP and CGRP only stained islet amyloid. |
| 2890 | 12110051 | PP, SS, glucagon, and porcine insulin did not stain amyloid. |
| 2891 | 12110051 | Sections of paraffin-embedded tissues were evaluated for amyloid with hematoxylin and eosin (HE) and congo red (CR) staining, and using immunohistochemistry for human islet amyloid polypeptide (IAPP), calcitonin gene-related peptide (CGRP), glucagon, pancreatic polypeptide (PP), somatostatin (SS), and porcine insulin. |
| 2892 | 12110051 | Islet amyloid was positive with HE in 40 baboons, with CR in 39 baboons, and with IAPP and CGRP in 35 baboons. |
| 2893 | 12110051 | IAPP and CGRP only stained islet amyloid. |
| 2894 | 12110051 | PP, SS, glucagon, and porcine insulin did not stain amyloid. |
| 2895 | 12110051 | Sections of paraffin-embedded tissues were evaluated for amyloid with hematoxylin and eosin (HE) and congo red (CR) staining, and using immunohistochemistry for human islet amyloid polypeptide (IAPP), calcitonin gene-related peptide (CGRP), glucagon, pancreatic polypeptide (PP), somatostatin (SS), and porcine insulin. |
| 2896 | 12110051 | Islet amyloid was positive with HE in 40 baboons, with CR in 39 baboons, and with IAPP and CGRP in 35 baboons. |
| 2897 | 12110051 | IAPP and CGRP only stained islet amyloid. |
| 2898 | 12110051 | PP, SS, glucagon, and porcine insulin did not stain amyloid. |
| 2899 | 12110051 | Sections of paraffin-embedded tissues were evaluated for amyloid with hematoxylin and eosin (HE) and congo red (CR) staining, and using immunohistochemistry for human islet amyloid polypeptide (IAPP), calcitonin gene-related peptide (CGRP), glucagon, pancreatic polypeptide (PP), somatostatin (SS), and porcine insulin. |
| 2900 | 12110051 | Islet amyloid was positive with HE in 40 baboons, with CR in 39 baboons, and with IAPP and CGRP in 35 baboons. |
| 2901 | 12110051 | IAPP and CGRP only stained islet amyloid. |
| 2902 | 12110051 | PP, SS, glucagon, and porcine insulin did not stain amyloid. |
| 2903 | 12110767 | Islet redox stress: the manifold toxicities of insulin resistance, metabolic syndrome and amylin derived islet amyloid in type 2 diabetes mellitus. |
| 2904 | 12124300 | We report constraints on the supramolecular structure of amyloid fibrils formed by the 40-residue beta-amyloid peptide associated with Alzheimer's disease (A beta(1-40)) obtained from solid-state nuclear magnetic resonance (NMR) measurements of intermolecular dipole-dipole couplings between (13)C labels at 11 carbon sites in residues 2 through 39. |
| 2905 | 12209476 | Amyloidogenicity and cytotoxicity of islet amyloid polypeptide. |
| 2906 | 12209476 | Insoluble amyloid formation by islet amyloid polypeptide (IAPP) in the islets of Langerhans of the pancreas is a major pathophysiological feature of noninsulin dependent diabetes mellitus (NIDDM) or type II diabetes. |
| 2907 | 12209476 | Amyloidogenicity and cytotoxicity of islet amyloid polypeptide. |
| 2908 | 12209476 | Insoluble amyloid formation by islet amyloid polypeptide (IAPP) in the islets of Langerhans of the pancreas is a major pathophysiological feature of noninsulin dependent diabetes mellitus (NIDDM) or type II diabetes. |
| 2909 | 12222959 | In this review, we discuss the context of each of these classes of ligands, including advance glycation end-products, amyloid beta peptide and the family of beta sheet fibrils, S100/calgranulins and amphoterin. |
| 2910 | 12234175 | Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes. |
| 2911 | 12234175 | Islet amyloid polypeptide (IAPP) and insulin are copackaged and cosecreted by pancreatic islet beta-cells. |
| 2912 | 12234175 | Non-insulin-dependent (type II) diabetes mellitus (NIDDM) is characterized by dysfunction and depletion of these beta-cells and also, in more than 90% of patients, amyloid plaques containing fibrillar IAPP. |
| 2913 | 12234175 | Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes. |
| 2914 | 12234175 | Islet amyloid polypeptide (IAPP) and insulin are copackaged and cosecreted by pancreatic islet beta-cells. |
| 2915 | 12234175 | Non-insulin-dependent (type II) diabetes mellitus (NIDDM) is characterized by dysfunction and depletion of these beta-cells and also, in more than 90% of patients, amyloid plaques containing fibrillar IAPP. |
| 2916 | 12234175 | Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes. |
| 2917 | 12234175 | Islet amyloid polypeptide (IAPP) and insulin are copackaged and cosecreted by pancreatic islet beta-cells. |
| 2918 | 12234175 | Non-insulin-dependent (type II) diabetes mellitus (NIDDM) is characterized by dysfunction and depletion of these beta-cells and also, in more than 90% of patients, amyloid plaques containing fibrillar IAPP. |
| 2919 | 12367525 | Identification and characterization of a novel molecular-recognition and self-assembly domain within the islet amyloid polypeptide. |
| 2920 | 12367525 | The islet amyloid polypeptide (hIAPP) is a 37 amino acid residue polypeptide that was found to accumulate as amyloid fibrils in the pancreas of individuals with type II diabetes. |
| 2921 | 12367525 | Identification and characterization of a novel molecular-recognition and self-assembly domain within the islet amyloid polypeptide. |
| 2922 | 12367525 | The islet amyloid polypeptide (hIAPP) is a 37 amino acid residue polypeptide that was found to accumulate as amyloid fibrils in the pancreas of individuals with type II diabetes. |
| 2923 | 12419183 | This correlates with tPA binding and stimulation of tPA-mediated plasminogen activation. |
| 2924 | 12419183 | Prototype amyloid peptides, including Abeta and islet amyloid polypeptide (IAPP) (associated with pancreatic beta cell toxicity in type II diabetes), have no sequence similarity to the fibrin peptides but also bind to tPA and can substitute for fibrin in plasminogen activation by tPA. |
| 2925 | 12419183 | Moreover, the induction of cross-beta structure in an otherwise globular protein (endostatin) endows it with tPA-activating potential. |
| 2926 | 12431815 | IA in both humans and cats is derived from islet amyloid polypeptide (IAPP, or amylin) which is a hormone produced and secreted along with insulin by the pancreatic beta cells. |
| 2927 | 12453678 | Receptor for Advanced Glycation Endproducts (RAGE) is a member of the immunoglobulin superfamily of cell surface molecules capable of interacting with a broad spectrum of ligands, including advanced glycation endproducts (AGEs), amyloid fibrils, S100/calgranulins and amphoterin. |
| 2928 | 12467491 | Insulin may also play a role in regulating the amyloid precursor protein and its derivative beta-amyloid (Abeta), which is associated with senile plaques, a neuropathological hallmark of Alzheimer's disease. |
| 2929 | 12467491 | It has been proposed that insulin can accelerate the intracellular trafficking of Abeta and interfere with its degradation. |
| 2930 | 12467491 | These findings are consistent with the notion that insulin abnormalities may potentially influence levels of Abeta in the brains of patients with Alzheimer's disease. |
| 2931 | 12467491 | The thiazolidinedione rosiglitazone has been shown to have a potent insulin-sensitising action that appears to be mediated through the peroxisome proliferator-activated receptor-gamma (PPAR-gamma). |
| 2932 | 12480734 | In most AD cases, Abeta peptides also form some deposits in the cerebrovasculature, leading to cerebral amyloid angiopathy and hemorrhagic stroke. |
| 2933 | 12480734 | We studied the effect of Abeta on constrictor responses elicited by endothelin-1 in isolated human cerebral arteries collected following rapid autopsies. |
| 2934 | 12480734 | We report that freshly solubilized Abeta potentiates endothelin-1-induced vasoconstriction in isolated human middle cerebral and basilar arteries. |
| 2935 | 12480734 | The vasoconstriction elicited by Abeta in these large human cerebral arteries appears to be completely antagonized by NS-398, a selective cyclooxygenase-2 inhibitor, or by SB202190, a specific p38 mitogen-activated protein kinase inhibitor, suggesting that Abeta vasoactivity is mediated via the stimulation of a proinflammatory pathway. |
| 2936 | 12481027 | We present a structural model for amyloid fibrils formed by the 40-residue beta-amyloid peptide associated with Alzheimer's disease (Abeta(1-40)), based on a set of experimental constraints from solid state NMR spectroscopy. |
| 2937 | 12515900 | Furthermore, GLP-1 can modify processing of the amyloid beta- protein precursor in cell culture and dose-dependently reduces amyloid beta-peptide levels in the brain in vivo. |
| 2938 | 12525695 | Expression of Pax4 in embryonic stem cells promotes differentiation of nestin-positive progenitor and insulin-producing cells. |
| 2939 | 12525695 | We show that constitutive expression of Pax4 (Pax4(+)), and to a lesser extent Pdx1 (Pdx1(+)), affects the differentiation of ES cells and significantly promote the development of insulin-producing cells. |
| 2940 | 12525695 | In Pax4 overexpressing R1 ES cells, isl-1, ngn3, insulin, islet amyloid polypeptide, and glucose transporter 2 (Glut-2) mRNA levels increase significantly. |
| 2941 | 12525695 | Constitutive Pax4 expression combined with selection of nestin+ cells and histotypic culture conditions give rise to spheroids containing insulin-positive granules typical of embryonal and adult beta cells. |
| 2942 | 12540610 | Transgenic mice expressing the amyloidogenic human islet amyloid polypeptide (hIAPP) in their islet beta-cells are a model of islet amyloid formation as it occurs in type 2 diabetes. |
| 2943 | 12540610 | In summary, dietary fat enhances both the prevalence and severity of islet amyloid and leads to beta-cell loss and impaired insulin secretion. |
| 2944 | 12540610 | Transgenic mice expressing the amyloidogenic human islet amyloid polypeptide (hIAPP) in their islet beta-cells are a model of islet amyloid formation as it occurs in type 2 diabetes. |
| 2945 | 12540610 | In summary, dietary fat enhances both the prevalence and severity of islet amyloid and leads to beta-cell loss and impaired insulin secretion. |
| 2946 | 12544832 | Effect of amyloid precursor protein 17mer peptide on microtubule structure and tau protein hyperphosphorylation in hippocampal neurons of experimental diabetic mice. |
| 2947 | 12544832 | The objective of this study was to investigate whether microtubular structure changes and tau protein hyperphosphorylation exist in hippocampal neurons of experimental diabetic mice, and to study the effect of amyloid precursor protein 17mer peptide. |
| 2948 | 12544832 | Effect of amyloid precursor protein 17mer peptide on microtubule structure and tau protein hyperphosphorylation in hippocampal neurons of experimental diabetic mice. |
| 2949 | 12544832 | The objective of this study was to investigate whether microtubular structure changes and tau protein hyperphosphorylation exist in hippocampal neurons of experimental diabetic mice, and to study the effect of amyloid precursor protein 17mer peptide. |
| 2950 | 12588049 | Polymorphism in intron 2 of islet amyloid polypeptide gene is associated with lower low-density lipoprotein cholesterol in nondiabetic subjects and in type 2 diabetic patients. |
| 2951 | 12588049 | The aim of this study was to investigate the presence of mutations in the islet amyloid polypeptide (IAPP) gene in a Spanish population with type 2 diabetes and gestational diabetes mellitus (GDM). |
| 2952 | 12588049 | Polymorphism in intron 2 of islet amyloid polypeptide gene is associated with lower low-density lipoprotein cholesterol in nondiabetic subjects and in type 2 diabetic patients. |
| 2953 | 12588049 | The aim of this study was to investigate the presence of mutations in the islet amyloid polypeptide (IAPP) gene in a Spanish population with type 2 diabetes and gestational diabetes mellitus (GDM). |
| 2954 | 12605343 | Islet amyloid polypeptide (amylin), cosecreted with insulin by the pancreatic beta-cells, has an important role in the regulation of islet cell hormone homeoastasis. |
| 2955 | 12606822 | Effects of free fatty acid on polymerization of islet amyloid polypeptide (IAPP) in vitro and on amyloid fibril formation in cultivated isolated islets of transgenic mice overexpressing human IAPP. |
| 2956 | 12616983 | CRP increases during oral contraceptive use were associated with changes in some other acute-phase proteins (fibrinogen, ceruloplasmin, von Willebrand factor [vWF]) originating from the liver and vessel wall, but not in others (interleukin-6 [IL-6], serum amyloid A [SAA]). |
| 2957 | 12618085 | We therefore evaluated CRP and the nearby serum amyloid P-component, APCS, which is structurally similar to CRP, as candidate diabetes susceptibility genes. |
| 2958 | 12618085 | We genotyped representative SNPs in approximately 1300 Pima samples and found a single variant in the CRP promoter (SNP 133552) that was associated with T2DM (P=0.014), as well as a common haplotype (CGCG) that was associated with both T2DM (P=0.029) and corrected insulin response, a surrogate measure of insulin secretion in non-diabetic subjects (P=0.050). |
| 2959 | 12630035 | Elevated fasting plasma level of islet amyloid polypeptide (IAPP) in chronic alcoholic pancreatitis (CAP). |
| 2960 | 12634421 | Insulin-degrading enzyme regulates the levels of insulin, amyloid beta-protein, and the beta-amyloid precursor protein intracellular domain in vivo. |
| 2961 | 12634421 | Two substrates of insulin-degrading enzyme (IDE), amyloid beta-protein (Abeta) and insulin, are critically important in the pathogenesis of Alzheimer's disease (AD) and type 2 diabetes mellitus (DM2), respectively. |
| 2962 | 12634421 | We previously identified IDE as a principal regulator of Abeta levels in neuronal and microglial cells. |
| 2963 | 12634421 | To establish whether IDE hypofunction decreases Abeta and insulin degradation in vivo and chronically increases their levels, we characterized mice with homozygous deletions of the IDE gene (IDE --). |
| 2964 | 12634421 | IDE deficiency resulted in a >50% decrease in Abeta degradation in both brain membrane fractions and primary neuronal cultures and a similar deficit in insulin degradation in liver. |
| 2965 | 12634421 | The IDE -- mice showed increased cerebral accumulation of endogenous Abeta, a hallmark of AD, and had hyperinsulinemia and glucose intolerance, hallmarks of DM2. |
| 2966 | 12634421 | Insulin-degrading enzyme regulates the levels of insulin, amyloid beta-protein, and the beta-amyloid precursor protein intracellular domain in vivo. |
| 2967 | 12634421 | Two substrates of insulin-degrading enzyme (IDE), amyloid beta-protein (Abeta) and insulin, are critically important in the pathogenesis of Alzheimer's disease (AD) and type 2 diabetes mellitus (DM2), respectively. |
| 2968 | 12634421 | We previously identified IDE as a principal regulator of Abeta levels in neuronal and microglial cells. |
| 2969 | 12634421 | To establish whether IDE hypofunction decreases Abeta and insulin degradation in vivo and chronically increases their levels, we characterized mice with homozygous deletions of the IDE gene (IDE --). |
| 2970 | 12634421 | IDE deficiency resulted in a >50% decrease in Abeta degradation in both brain membrane fractions and primary neuronal cultures and a similar deficit in insulin degradation in liver. |
| 2971 | 12634421 | The IDE -- mice showed increased cerebral accumulation of endogenous Abeta, a hallmark of AD, and had hyperinsulinemia and glucose intolerance, hallmarks of DM2. |
| 2972 | 12637985 | The effect of apolipoprotein E deficiency on islet amyloid deposition in human islet amyloid polypeptide transgenic mice. |
| 2973 | 12670620 | Islet amyloid polypeptide and type 2 diabetes. |
| 2974 | 12670620 | Islet amyloid polypeptide (IAPP; amylin), the major component of islet amyloid, is co-secreted with insulin from beta-cells. |
| 2975 | 12670620 | Islet amyloid polypeptide and type 2 diabetes. |
| 2976 | 12670620 | Islet amyloid polypeptide (IAPP; amylin), the major component of islet amyloid, is co-secreted with insulin from beta-cells. |
| 2977 | 12686466 | Postnatally disturbed pancreatic islet cell distribution in human islet amyloid polypeptide transgenic mice. |
| 2978 | 12706318 | Apolipoprotein E genotype, islet amyloid deposition and severity of Type 2 diabetes. |
| 2979 | 12706318 | Islet amyloid is found in 90% of patients with Type 2 (non-insulin-dependent) diabetes at post-mortem. |
| 2980 | 12706318 | It is unlikely that the common polymorphisms for the ApoE gene are linked to amyloid formation or progression of islet dysfunction in Type 2 diabetes. |
| 2981 | 12706318 | Apolipoprotein E genotype, islet amyloid deposition and severity of Type 2 diabetes. |
| 2982 | 12706318 | Islet amyloid is found in 90% of patients with Type 2 (non-insulin-dependent) diabetes at post-mortem. |
| 2983 | 12706318 | It is unlikely that the common polymorphisms for the ApoE gene are linked to amyloid formation or progression of islet dysfunction in Type 2 diabetes. |
| 2984 | 12706318 | Apolipoprotein E genotype, islet amyloid deposition and severity of Type 2 diabetes. |
| 2985 | 12706318 | Islet amyloid is found in 90% of patients with Type 2 (non-insulin-dependent) diabetes at post-mortem. |
| 2986 | 12706318 | It is unlikely that the common polymorphisms for the ApoE gene are linked to amyloid formation or progression of islet dysfunction in Type 2 diabetes. |
| 2987 | 12717005 | However, pairs of integral counterregulatory controllers (e.g. insulin and glucagon, or calcitonin and parathyroid hormone) cannot operate on the same controlled variable, unless there is some form of mutual inhibition. |
| 2988 | 12717005 | Our synthesis of the information pertaining to the glucose homeostat that has accumulated in the literature predicts that disruption of the flip-flop mechanism by the accumulation of amyloid in the pancreatic islets in type 2 diabetes mellitus will lead to hyperglucagonaemia, hyperinsulinaemia, insulin resistance, glucose intolerance and impaired insulin responsiveness to elevated blood glucose levels. |
| 2989 | 12719273 | Micelle formation by a fragment of human islet amyloid polypeptide. |
| 2990 | 12719273 | Human islet amyloid polypeptide (hIAPP) is the major component of amyloid plaques found in the pancreatic islets of persons with type 2 diabetes mellitus. |
| 2991 | 12719273 | Micelle formation by a fragment of human islet amyloid polypeptide. |
| 2992 | 12719273 | Human islet amyloid polypeptide (hIAPP) is the major component of amyloid plaques found in the pancreatic islets of persons with type 2 diabetes mellitus. |
| 2993 | 12729615 | They contain both amylin (islet amyloid polypeptide), the beta-cell-derived unique fibrillogenic component, and heparan sulfate proteoglycans (HSPGs). |
| 2994 | 12736442 | Evaluation of feline serum amyloid A (SAA) as an inflammatory marker. |
| 2995 | 12749025 | Glucagon-like peptide-1 decreases endogenous amyloid-beta peptide (Abeta) levels and protects hippocampal neurons from death induced by Abeta and iron. |
| 2996 | 12749025 | We report here that GLP-1 can reduce the levels of amyloid-beta peptide (Abeta) in the brain in vivo and can reduce levels of amyloid precursor protein (APP) in cultured neuronal cells. |
| 2997 | 12749025 | Moreover, GLP-1 and exendin-4 protect cultured hippocampal neurons against death induced by Abeta and iron, an oxidative insult. |
| 2998 | 12749025 | Collectively, these data suggest that GLP-1 can modify APP processing and protect against oxidative injury, two actions that suggest a novel therapeutic target for intervention in Alzheimer's disease. |
| 2999 | 12765956 | The effect of amyloid beta-peptides, 50 micromol/l Abeta(25-35) or 2 micromol/l Abeta(1-40), on mitochondrial function was also analyzed. |
| 3000 | 12766975 | The inherited amyloid neuropathies are due to mutations of three proteins: transthyretin, apolipoprotein A1, and gelsolin. |
| 3001 | 12786686 | Studies of variability in the islet amyloid polypeptide gene in relation to Type 2 diabetes. |
| 3002 | 12806128 | Amylin (islet amyloid polypeptide) is a peptide synthesized principally in the beta-cells of the pancreatic islets together with insulin and has actions as a hormone, growth factor, and modifier of behavior. |
| 3003 | 12821727 | Insulin and Alzheimer's disease: an amyloid connection. |
| 3004 | 12829636 | Replication increases beta-cell vulnerability to human islet amyloid polypeptide-induced apoptosis. |
| 3005 | 12829636 | Type 2 diabetes is characterized by a relative beta-cell deficit as a result of increased beta-cell apoptosis and islet amyloid derived from the beta-cell peptide islet amyloid polypeptide (IAPP). |
| 3006 | 12829636 | Replication increases beta-cell vulnerability to human islet amyloid polypeptide-induced apoptosis. |
| 3007 | 12829636 | Type 2 diabetes is characterized by a relative beta-cell deficit as a result of increased beta-cell apoptosis and islet amyloid derived from the beta-cell peptide islet amyloid polypeptide (IAPP). |
| 3008 | 12849365 | Cerebral autosomal dominant arteriopathy with subcortical infarcts and leucoencephalopathy (CADASIL)and some forms of cerebral amyloid angiopathy have a genetic basis. |
| 3009 | 12882918 | ES cells were evaluated for their ability to differentiate into pancreatic and islet lineage-restricted stages including pancreatic duodenal homeobox 1 (PDX1)-positive pancreatic precursor cells, early endocrine cell progenitors, and islet hormone-producing cells. |
| 3010 | 12882918 | Following growth and differentiation in nonselective medium containing serum, murine ES cells spontaneously differentiated into cells individually expressing each of the four major islet hormones: insulin, glucagon, somatostatin, and pancreatic polypeptide. |
| 3011 | 12882918 | Hormone-positive cells appeared within focal clusters of cells coexpressing PDX1 and the nonclassical hormone markers peptide YY (YY) and islet amyloid polypeptide (IAPP) in combination with the definitive hormones, characteristic of endocrine cells appearing during early pancreaticogenesis. |
| 3012 | 12941770 | In an attempt to establish the mechanism for the deficit in beta-cell mass in type 2 diabetes, we used an obese versus lean murine transgenic model for human islet amyloid polypeptide (IAPP) that develops islet pathology comparable to that in humans with type 2 diabetes. |
| 3013 | 12941771 | An insulin-degrading enzyme inhibitor decreases amylin degradation, increases amylin-induced cytotoxicity, and increases amyloid formation in insulinoma cell cultures. |
| 3014 | 12941771 | Amylin (islet amyloid polypeptide) is the chief component of the islet amyloid found in type 2 diabetes, and amylin fibril precursors may be cytotoxic to pancreatic beta-cells. |
| 3015 | 12941771 | We investigated the role of insulin-degrading enzyme (IDE) in amylin degradation, amyloid deposition, and cytotoxicity in RIN-m5F insulinoma cells. |
| 3016 | 12941771 | The IDE inhibitor bacitracin inhibited amylin degradation by 78% and insulin degradation by 100%. |
| 3017 | 12941771 | IDE inhibition by bacitracin impaired amylin degradation, increased amyloid formation, and increased amylin-induced cytotoxicity, suggesting a role for IDE in amylin clearance and the prevention of amylin aggregation. |
| 3018 | 12941771 | An insulin-degrading enzyme inhibitor decreases amylin degradation, increases amylin-induced cytotoxicity, and increases amyloid formation in insulinoma cell cultures. |
| 3019 | 12941771 | Amylin (islet amyloid polypeptide) is the chief component of the islet amyloid found in type 2 diabetes, and amylin fibril precursors may be cytotoxic to pancreatic beta-cells. |
| 3020 | 12941771 | We investigated the role of insulin-degrading enzyme (IDE) in amylin degradation, amyloid deposition, and cytotoxicity in RIN-m5F insulinoma cells. |
| 3021 | 12941771 | The IDE inhibitor bacitracin inhibited amylin degradation by 78% and insulin degradation by 100%. |
| 3022 | 12941771 | IDE inhibition by bacitracin impaired amylin degradation, increased amyloid formation, and increased amylin-induced cytotoxicity, suggesting a role for IDE in amylin clearance and the prevention of amylin aggregation. |
| 3023 | 12941771 | An insulin-degrading enzyme inhibitor decreases amylin degradation, increases amylin-induced cytotoxicity, and increases amyloid formation in insulinoma cell cultures. |
| 3024 | 12941771 | Amylin (islet amyloid polypeptide) is the chief component of the islet amyloid found in type 2 diabetes, and amylin fibril precursors may be cytotoxic to pancreatic beta-cells. |
| 3025 | 12941771 | We investigated the role of insulin-degrading enzyme (IDE) in amylin degradation, amyloid deposition, and cytotoxicity in RIN-m5F insulinoma cells. |
| 3026 | 12941771 | The IDE inhibitor bacitracin inhibited amylin degradation by 78% and insulin degradation by 100%. |
| 3027 | 12941771 | IDE inhibition by bacitracin impaired amylin degradation, increased amyloid formation, and increased amylin-induced cytotoxicity, suggesting a role for IDE in amylin clearance and the prevention of amylin aggregation. |
| 3028 | 12941771 | An insulin-degrading enzyme inhibitor decreases amylin degradation, increases amylin-induced cytotoxicity, and increases amyloid formation in insulinoma cell cultures. |
| 3029 | 12941771 | Amylin (islet amyloid polypeptide) is the chief component of the islet amyloid found in type 2 diabetes, and amylin fibril precursors may be cytotoxic to pancreatic beta-cells. |
| 3030 | 12941771 | We investigated the role of insulin-degrading enzyme (IDE) in amylin degradation, amyloid deposition, and cytotoxicity in RIN-m5F insulinoma cells. |
| 3031 | 12941771 | The IDE inhibitor bacitracin inhibited amylin degradation by 78% and insulin degradation by 100%. |
| 3032 | 12941771 | IDE inhibition by bacitracin impaired amylin degradation, increased amyloid formation, and increased amylin-induced cytotoxicity, suggesting a role for IDE in amylin clearance and the prevention of amylin aggregation. |
| 3033 | 12952363 | Using reverse transcriptase-polymerase chain reaction, no differences in mRNA expression levels were found for insulin, islet amyloid polypeptide (IAPP), and the prohormone convertase (PC) 1 and PC2 between 6-week-old untreated ZDF rats and 19-week-old sham- and phlorizin-treated ZDF rats. |
| 3034 | 12962700 | Glycosaminoglycans (GAG) and the pentraxin protein, serum amyloid P (SAP) component, are universal non-fibrillar constituents of amyloid deposits that contribute to fibrillogenesis. |
| 3035 | 12962700 | We review potential therapies for amyloidosis, which include measures to reduce the production of amyloidogenic precursor proteins, interference with fibrillogenesis, and enhancement of amyloid clearance, either by active or passive immunisation or by destabilising deposits through removal of serum amyloid P component. |
| 3036 | 12962700 | Glycosaminoglycans (GAG) and the pentraxin protein, serum amyloid P (SAP) component, are universal non-fibrillar constituents of amyloid deposits that contribute to fibrillogenesis. |
| 3037 | 12962700 | We review potential therapies for amyloidosis, which include measures to reduce the production of amyloidogenic precursor proteins, interference with fibrillogenesis, and enhancement of amyloid clearance, either by active or passive immunisation or by destabilising deposits through removal of serum amyloid P component. |
| 3038 | 12974632 | The human islet amyloid polypeptide forms transient membrane-active prefibrillar assemblies. |
| 3039 | 12974632 | The formation of amyloid fibrils by the human islet amyloid polypeptide is associated with type II diabetes. |
| 3040 | 12974632 | Here, we specifically studied the membrane interaction activity of soluble and insoluble islet amyloid polypeptide assemblies at high temporal resolution. |
| 3041 | 12974632 | The human islet amyloid polypeptide forms transient membrane-active prefibrillar assemblies. |
| 3042 | 12974632 | The formation of amyloid fibrils by the human islet amyloid polypeptide is associated with type II diabetes. |
| 3043 | 12974632 | Here, we specifically studied the membrane interaction activity of soluble and insoluble islet amyloid polypeptide assemblies at high temporal resolution. |
| 3044 | 12974632 | The human islet amyloid polypeptide forms transient membrane-active prefibrillar assemblies. |
| 3045 | 12974632 | The formation of amyloid fibrils by the human islet amyloid polypeptide is associated with type II diabetes. |
| 3046 | 12974632 | Here, we specifically studied the membrane interaction activity of soluble and insoluble islet amyloid polypeptide assemblies at high temporal resolution. |
| 3047 | 13807843 | Nephrogenic diabetes insipidus caused by amyloid disease. |
| 3048 | 14565847 | Pancreatic beta-cell granule peptides form heteromolecular complexes which inhibit islet amyloid polypeptide fibril formation. |
| 3049 | 14565847 | Islet amyloid polypeptide (IAPP), or 'amylin', is co-stored with insulin in secretory granules of pancreatic islet beta-cells. |
| 3050 | 14565847 | Since rIAPP and hIAPP form complexes with insulin (and each other), this could explain the lack of amyloid fibrils in transgenic mice expressing hIAPP. |
| 3051 | 14565847 | Pancreatic beta-cell granule peptides form heteromolecular complexes which inhibit islet amyloid polypeptide fibril formation. |
| 3052 | 14565847 | Islet amyloid polypeptide (IAPP), or 'amylin', is co-stored with insulin in secretory granules of pancreatic islet beta-cells. |
| 3053 | 14565847 | Since rIAPP and hIAPP form complexes with insulin (and each other), this could explain the lack of amyloid fibrils in transgenic mice expressing hIAPP. |
| 3054 | 14565847 | Pancreatic beta-cell granule peptides form heteromolecular complexes which inhibit islet amyloid polypeptide fibril formation. |
| 3055 | 14565847 | Islet amyloid polypeptide (IAPP), or 'amylin', is co-stored with insulin in secretory granules of pancreatic islet beta-cells. |
| 3056 | 14565847 | Since rIAPP and hIAPP form complexes with insulin (and each other), this could explain the lack of amyloid fibrils in transgenic mice expressing hIAPP. |
| 3057 | 14573810 | Surviving beta cells were found to synthesize little insulin, although islet amyloid polypeptide was detected and glucagon synthesis in alpha cells appeared normal or enhanced. |
| 3058 | 14578281 | Using algorithms to predict nonameric beta-cell peptides that would bind to the common HLA allele, HLA-A*0201, we identified a potential epitope from the leader sequence of islet amyloid polypeptide (human islet amyloid polypeptide [IAPP] precursor protein [preproIAPP] 5-13: KLQVFLIVL). |
| 3059 | 14578294 | Islet amyloid has been suggested to be an important link between insulin resistance and beta-cell dysfunction in type 2 diabetes. |
| 3060 | 14578294 | These findings suggest that islet amyloid deposits reflect greater insulin resistance and islet failure in a subgroup of type 2 diabetic patients. |
| 3061 | 14578294 | Islet amyloid has been suggested to be an important link between insulin resistance and beta-cell dysfunction in type 2 diabetes. |
| 3062 | 14578294 | These findings suggest that islet amyloid deposits reflect greater insulin resistance and islet failure in a subgroup of type 2 diabetic patients. |
| 3063 | 14613923 | Extended life span is associated with insulin resistance in a transgenic mouse model of insulinoma secreting human islet amyloid polypeptide. |
| 3064 | 14613923 | To study mechanisms of islet amyloidogenesis, we produced transgenic mice expressing the unique component of human islet amyloid, human islet amyloid polypeptide (hIAPP). |
| 3065 | 14613923 | This increase in life span in hIAPPxRIP-Tag was positively correlated with body weight (r = 0.48, P < 0.05) and was associated with decreased insulin sensitivity compared with RIP-Tag mice. hIAPPxRIP-Tag mice did not develop amyloid during their 4-mo life span, suggesting that increased hIAPP secretion is insufficient for islet amyloid formation within such a short time. |
| 3066 | 14613923 | Extended life span is associated with insulin resistance in a transgenic mouse model of insulinoma secreting human islet amyloid polypeptide. |
| 3067 | 14613923 | To study mechanisms of islet amyloidogenesis, we produced transgenic mice expressing the unique component of human islet amyloid, human islet amyloid polypeptide (hIAPP). |
| 3068 | 14613923 | This increase in life span in hIAPPxRIP-Tag was positively correlated with body weight (r = 0.48, P < 0.05) and was associated with decreased insulin sensitivity compared with RIP-Tag mice. hIAPPxRIP-Tag mice did not develop amyloid during their 4-mo life span, suggesting that increased hIAPP secretion is insufficient for islet amyloid formation within such a short time. |
| 3069 | 14613923 | Extended life span is associated with insulin resistance in a transgenic mouse model of insulinoma secreting human islet amyloid polypeptide. |
| 3070 | 14613923 | To study mechanisms of islet amyloidogenesis, we produced transgenic mice expressing the unique component of human islet amyloid, human islet amyloid polypeptide (hIAPP). |
| 3071 | 14613923 | This increase in life span in hIAPPxRIP-Tag was positively correlated with body weight (r = 0.48, P < 0.05) and was associated with decreased insulin sensitivity compared with RIP-Tag mice. hIAPPxRIP-Tag mice did not develop amyloid during their 4-mo life span, suggesting that increased hIAPP secretion is insufficient for islet amyloid formation within such a short time. |
| 3072 | 14624021 | Relationship between testosterone, sex hormone binding globulin and plasma amyloid beta peptide 40 in older men with subjective memory loss or dementia. |
| 3073 | 14624021 | In a group of 28 older men with either subjective memory loss or dementia, serum total testosterone and sex hormone binding globulin (SHBG) correlated inversely with plasma levels of amyloid beta peptide 40 (Abeta40, r=-0.5, P=0.01 and r=-0.4, P=0.04, respectively). |
| 3074 | 14624021 | Relationship between testosterone, sex hormone binding globulin and plasma amyloid beta peptide 40 in older men with subjective memory loss or dementia. |
| 3075 | 14624021 | In a group of 28 older men with either subjective memory loss or dementia, serum total testosterone and sex hormone binding globulin (SHBG) correlated inversely with plasma levels of amyloid beta peptide 40 (Abeta40, r=-0.5, P=0.01 and r=-0.4, P=0.04, respectively). |
| 3076 | 14659752 | The mechanism of insulin action on islet amyloid polypeptide fiber formation. |
| 3077 | 14659752 | The main component of these deposits, islet amyloid polypeptide (IAPP), is a hormone involved in glucose metabolism and is normally co-secreted with insulin by the beta-cells of the pancreas. |
| 3078 | 14659752 | The mechanism of insulin action on islet amyloid polypeptide fiber formation. |
| 3079 | 14659752 | The main component of these deposits, islet amyloid polypeptide (IAPP), is a hormone involved in glucose metabolism and is normally co-secreted with insulin by the beta-cells of the pancreas. |
| 3080 | 14659754 | We report solid state nuclear magnetic resonance (NMR) measurements that probe the supramolecular organization of beta-sheets in the cross-beta motif of amyloid fibrils formed by residues 11-25 of the beta-amyloid peptide associated with Alzheimer's disease (Abeta(11-25)). |
| 3081 | 14693708 | Role of beta-cell prohormone convertase (PC)1/3 in processing of pro-islet amyloid polypeptide. |
| 3082 | 14693708 | Islet amyloid polypeptide (IAPP) (amylin), the major component of islet amyloid, is produced by cleavage at the COOH- and NH(2)-termini of its precursor, proIAPP, likely by the beta-cell prohormone convertases (PC) 1/3 and PC2. |
| 3083 | 14693708 | Mice lacking PC2 can process proIAPP at its COOH- but not its NH(2)-terminal cleavage site, suggesting that PC1/3 is capable of initiating proIAPP cleavage at its COOH-terminus. |
| 3084 | 14693708 | Next, GH3 cells that do not normally express proIAPP or detectable levels of PC1/3 or PC2 were cotransduced with adenoviruses expressing rat proIAPP and either PC2 or PC1/3. |
| 3085 | 14693708 | Coexpression of proIAPP and PC2 resulted in production of mature IAPP, whereas in cells that coexpressed proIAPP and PC1/3 only a 6-kDa intermediate was produced. |
| 3086 | 14693708 | We conclude that PC1/3 is important for processing of proIAPP at the COOH-terminus, but in its absence, PC2 can initiate complete processing of proIAPP to IAPP by cleaving the precursor at either its NH(2)- or COOH-terminal cleavage sites. |
| 3087 | 14693708 | Role of beta-cell prohormone convertase (PC)1/3 in processing of pro-islet amyloid polypeptide. |
| 3088 | 14693708 | Islet amyloid polypeptide (IAPP) (amylin), the major component of islet amyloid, is produced by cleavage at the COOH- and NH(2)-termini of its precursor, proIAPP, likely by the beta-cell prohormone convertases (PC) 1/3 and PC2. |
| 3089 | 14693708 | Mice lacking PC2 can process proIAPP at its COOH- but not its NH(2)-terminal cleavage site, suggesting that PC1/3 is capable of initiating proIAPP cleavage at its COOH-terminus. |
| 3090 | 14693708 | Next, GH3 cells that do not normally express proIAPP or detectable levels of PC1/3 or PC2 were cotransduced with adenoviruses expressing rat proIAPP and either PC2 or PC1/3. |
| 3091 | 14693708 | Coexpression of proIAPP and PC2 resulted in production of mature IAPP, whereas in cells that coexpressed proIAPP and PC1/3 only a 6-kDa intermediate was produced. |
| 3092 | 14693708 | We conclude that PC1/3 is important for processing of proIAPP at the COOH-terminus, but in its absence, PC2 can initiate complete processing of proIAPP to IAPP by cleaving the precursor at either its NH(2)- or COOH-terminal cleavage sites. |
| 3093 | 14711882 | The term myofibrillar myopathy (MFM) was proposed in 1996 as a non-committal term for a pathological pattern of myofibrillar dissolution associated with accumulation of myofibrillar degradation products and ectopic expression of multiple proteins that include desmin, alphaB-crystallin (alphaBC), dystrophin and congophilic amyloid material. |
| 3094 | 14711882 | Semiquantitative analysis in each case indicates that among the abnormal fibres, an average of 90, 75, 75, 70 and 70% abnormally express myotilin, desmin, alphaBC, dystrophin and beta-amyloid precursor protein, respectively. |
| 3095 | 14711882 | In all patients, we searched for mutations in desmin and alphaBC, as well as in telethonin, a Z-disk-associated protein, or in syncoilin, which together with plectin links desmin to the Z-disk. |
| 3096 | 14711882 | Two of the 63 patients carry truncation mutations in the C-terminal domain of alphaBC, four carry missense mutations in the head or tail region of desmin, and none carries a mutation in syncoilin or telethonin. |
| 3097 | 14722650 | Islet amyloid polypeptide is a 37 amino-acid, beta-cell peptide which is co-stored and co-released with insulin. |
| 3098 | 14722650 | Human islet amyloid polypeptide refolds to a beta-conformation and oligomerises to form insoluble fibrils; proline substitutions in rodent islet amyloid polypeptide prevent this molecular transition. |
| 3099 | 14722650 | Pro-islet amyloid polypeptide (67 amino acids in man) is processed in secretory granules. |
| 3100 | 14722650 | Refolding of islet amyloid polypeptide may be prevented by intragranular heterodimer formation with insulin (but not proinsulin). |
| 3101 | 14722650 | Diabetes-associated abnormal proinsulin processing could contribute to de-stabilisation of granular islet amyloid polypeptide. |
| 3102 | 14722650 | Increased pro-islet amyloid polypeptide secretion as a consequence of islet dysfunction could promote fibrillogenesis; the propeptide forms fibrils and binds to basement membrane glycosamino-glycans. |
| 3103 | 14722650 | Islet amyloid polypeptide gene polymorphisms are not universally associated with Type 2 diabetes. |
| 3104 | 14722650 | Transgenic mice expressing human islet amyloid polypeptide gene have increased islet amyloid polypeptide concentrations but develop islet amyloid only against a background of obesity and/or high fat diet. |
| 3105 | 14722650 | Islet amyloid polypeptide is a 37 amino-acid, beta-cell peptide which is co-stored and co-released with insulin. |
| 3106 | 14722650 | Human islet amyloid polypeptide refolds to a beta-conformation and oligomerises to form insoluble fibrils; proline substitutions in rodent islet amyloid polypeptide prevent this molecular transition. |
| 3107 | 14722650 | Pro-islet amyloid polypeptide (67 amino acids in man) is processed in secretory granules. |
| 3108 | 14722650 | Refolding of islet amyloid polypeptide may be prevented by intragranular heterodimer formation with insulin (but not proinsulin). |
| 3109 | 14722650 | Diabetes-associated abnormal proinsulin processing could contribute to de-stabilisation of granular islet amyloid polypeptide. |
| 3110 | 14722650 | Increased pro-islet amyloid polypeptide secretion as a consequence of islet dysfunction could promote fibrillogenesis; the propeptide forms fibrils and binds to basement membrane glycosamino-glycans. |
| 3111 | 14722650 | Islet amyloid polypeptide gene polymorphisms are not universally associated with Type 2 diabetes. |
| 3112 | 14722650 | Transgenic mice expressing human islet amyloid polypeptide gene have increased islet amyloid polypeptide concentrations but develop islet amyloid only against a background of obesity and/or high fat diet. |
| 3113 | 14722650 | Islet amyloid polypeptide is a 37 amino-acid, beta-cell peptide which is co-stored and co-released with insulin. |
| 3114 | 14722650 | Human islet amyloid polypeptide refolds to a beta-conformation and oligomerises to form insoluble fibrils; proline substitutions in rodent islet amyloid polypeptide prevent this molecular transition. |
| 3115 | 14722650 | Pro-islet amyloid polypeptide (67 amino acids in man) is processed in secretory granules. |
| 3116 | 14722650 | Refolding of islet amyloid polypeptide may be prevented by intragranular heterodimer formation with insulin (but not proinsulin). |
| 3117 | 14722650 | Diabetes-associated abnormal proinsulin processing could contribute to de-stabilisation of granular islet amyloid polypeptide. |
| 3118 | 14722650 | Increased pro-islet amyloid polypeptide secretion as a consequence of islet dysfunction could promote fibrillogenesis; the propeptide forms fibrils and binds to basement membrane glycosamino-glycans. |
| 3119 | 14722650 | Islet amyloid polypeptide gene polymorphisms are not universally associated with Type 2 diabetes. |
| 3120 | 14722650 | Transgenic mice expressing human islet amyloid polypeptide gene have increased islet amyloid polypeptide concentrations but develop islet amyloid only against a background of obesity and/or high fat diet. |
| 3121 | 14722650 | Islet amyloid polypeptide is a 37 amino-acid, beta-cell peptide which is co-stored and co-released with insulin. |
| 3122 | 14722650 | Human islet amyloid polypeptide refolds to a beta-conformation and oligomerises to form insoluble fibrils; proline substitutions in rodent islet amyloid polypeptide prevent this molecular transition. |
| 3123 | 14722650 | Pro-islet amyloid polypeptide (67 amino acids in man) is processed in secretory granules. |
| 3124 | 14722650 | Refolding of islet amyloid polypeptide may be prevented by intragranular heterodimer formation with insulin (but not proinsulin). |
| 3125 | 14722650 | Diabetes-associated abnormal proinsulin processing could contribute to de-stabilisation of granular islet amyloid polypeptide. |
| 3126 | 14722650 | Increased pro-islet amyloid polypeptide secretion as a consequence of islet dysfunction could promote fibrillogenesis; the propeptide forms fibrils and binds to basement membrane glycosamino-glycans. |
| 3127 | 14722650 | Islet amyloid polypeptide gene polymorphisms are not universally associated with Type 2 diabetes. |
| 3128 | 14722650 | Transgenic mice expressing human islet amyloid polypeptide gene have increased islet amyloid polypeptide concentrations but develop islet amyloid only against a background of obesity and/or high fat diet. |
| 3129 | 14722650 | Islet amyloid polypeptide is a 37 amino-acid, beta-cell peptide which is co-stored and co-released with insulin. |
| 3130 | 14722650 | Human islet amyloid polypeptide refolds to a beta-conformation and oligomerises to form insoluble fibrils; proline substitutions in rodent islet amyloid polypeptide prevent this molecular transition. |
| 3131 | 14722650 | Pro-islet amyloid polypeptide (67 amino acids in man) is processed in secretory granules. |
| 3132 | 14722650 | Refolding of islet amyloid polypeptide may be prevented by intragranular heterodimer formation with insulin (but not proinsulin). |
| 3133 | 14722650 | Diabetes-associated abnormal proinsulin processing could contribute to de-stabilisation of granular islet amyloid polypeptide. |
| 3134 | 14722650 | Increased pro-islet amyloid polypeptide secretion as a consequence of islet dysfunction could promote fibrillogenesis; the propeptide forms fibrils and binds to basement membrane glycosamino-glycans. |
| 3135 | 14722650 | Islet amyloid polypeptide gene polymorphisms are not universally associated with Type 2 diabetes. |
| 3136 | 14722650 | Transgenic mice expressing human islet amyloid polypeptide gene have increased islet amyloid polypeptide concentrations but develop islet amyloid only against a background of obesity and/or high fat diet. |
| 3137 | 14722650 | Islet amyloid polypeptide is a 37 amino-acid, beta-cell peptide which is co-stored and co-released with insulin. |
| 3138 | 14722650 | Human islet amyloid polypeptide refolds to a beta-conformation and oligomerises to form insoluble fibrils; proline substitutions in rodent islet amyloid polypeptide prevent this molecular transition. |
| 3139 | 14722650 | Pro-islet amyloid polypeptide (67 amino acids in man) is processed in secretory granules. |
| 3140 | 14722650 | Refolding of islet amyloid polypeptide may be prevented by intragranular heterodimer formation with insulin (but not proinsulin). |
| 3141 | 14722650 | Diabetes-associated abnormal proinsulin processing could contribute to de-stabilisation of granular islet amyloid polypeptide. |
| 3142 | 14722650 | Increased pro-islet amyloid polypeptide secretion as a consequence of islet dysfunction could promote fibrillogenesis; the propeptide forms fibrils and binds to basement membrane glycosamino-glycans. |
| 3143 | 14722650 | Islet amyloid polypeptide gene polymorphisms are not universally associated with Type 2 diabetes. |
| 3144 | 14722650 | Transgenic mice expressing human islet amyloid polypeptide gene have increased islet amyloid polypeptide concentrations but develop islet amyloid only against a background of obesity and/or high fat diet. |
| 3145 | 14722650 | Islet amyloid polypeptide is a 37 amino-acid, beta-cell peptide which is co-stored and co-released with insulin. |
| 3146 | 14722650 | Human islet amyloid polypeptide refolds to a beta-conformation and oligomerises to form insoluble fibrils; proline substitutions in rodent islet amyloid polypeptide prevent this molecular transition. |
| 3147 | 14722650 | Pro-islet amyloid polypeptide (67 amino acids in man) is processed in secretory granules. |
| 3148 | 14722650 | Refolding of islet amyloid polypeptide may be prevented by intragranular heterodimer formation with insulin (but not proinsulin). |
| 3149 | 14722650 | Diabetes-associated abnormal proinsulin processing could contribute to de-stabilisation of granular islet amyloid polypeptide. |
| 3150 | 14722650 | Increased pro-islet amyloid polypeptide secretion as a consequence of islet dysfunction could promote fibrillogenesis; the propeptide forms fibrils and binds to basement membrane glycosamino-glycans. |
| 3151 | 14722650 | Islet amyloid polypeptide gene polymorphisms are not universally associated with Type 2 diabetes. |
| 3152 | 14722650 | Transgenic mice expressing human islet amyloid polypeptide gene have increased islet amyloid polypeptide concentrations but develop islet amyloid only against a background of obesity and/or high fat diet. |
| 3153 | 14722650 | Islet amyloid polypeptide is a 37 amino-acid, beta-cell peptide which is co-stored and co-released with insulin. |
| 3154 | 14722650 | Human islet amyloid polypeptide refolds to a beta-conformation and oligomerises to form insoluble fibrils; proline substitutions in rodent islet amyloid polypeptide prevent this molecular transition. |
| 3155 | 14722650 | Pro-islet amyloid polypeptide (67 amino acids in man) is processed in secretory granules. |
| 3156 | 14722650 | Refolding of islet amyloid polypeptide may be prevented by intragranular heterodimer formation with insulin (but not proinsulin). |
| 3157 | 14722650 | Diabetes-associated abnormal proinsulin processing could contribute to de-stabilisation of granular islet amyloid polypeptide. |
| 3158 | 14722650 | Increased pro-islet amyloid polypeptide secretion as a consequence of islet dysfunction could promote fibrillogenesis; the propeptide forms fibrils and binds to basement membrane glycosamino-glycans. |
| 3159 | 14722650 | Islet amyloid polypeptide gene polymorphisms are not universally associated with Type 2 diabetes. |
| 3160 | 14722650 | Transgenic mice expressing human islet amyloid polypeptide gene have increased islet amyloid polypeptide concentrations but develop islet amyloid only against a background of obesity and/or high fat diet. |
| 3161 | 14729343 | Structural characterisation of islet amyloid polypeptide fibrils. |
| 3162 | 14729343 | Amyloid fibrils found deposited in the pancreatic islets are composed of a 37-residue peptide, known as islet amyloid polypeptide (IAPP) (also known as amylin) and are similar to those found in other amyloid diseases. |
| 3163 | 14729343 | Structural characterisation of islet amyloid polypeptide fibrils. |
| 3164 | 14729343 | Amyloid fibrils found deposited in the pancreatic islets are composed of a 37-residue peptide, known as islet amyloid polypeptide (IAPP) (also known as amylin) and are similar to those found in other amyloid diseases. |
| 3165 | 14747300 | Alzheimer disease and type 2 diabetes are characterized by increased prevalence with aging, a genetic predisposition, and comparable pathological features in the islet and brain (amyloid derived from amyloid beta protein in the brain in Alzheimer disease and islet amyloid derived from islet amyloid polypeptide in the pancreas in type 2 diabetes). |
| 3166 | 14973422 | In this paper some of the peptides or low molecular weight proteins along with some analogues which have been employed in experimental studies and in humans are reviewed, with major emphasis on amyloid seekers, insulin and leptin. |
| 3167 | 14976144 | Glucose-induced expression of the cyclin-dependent protein kinase 5 activator p35 involved in Alzheimer's disease regulates insulin gene transcription in pancreatic beta-cells. |
| 3168 | 14976144 | The deposition of amyloid within the insulin-producing islets of Langerhans in the pancreas is a common pathological finding in patients with type 2 diabetes. |
| 3169 | 14976144 | Overactivity of CDK5 occurs by proteolytic cleavage and cellular mislocalization of its activator, p35. |
| 3170 | 14976144 | These alterations in p35/CDK5 signaling pathway may mediate, at least in part, the functional abnormalities characteristic of Alzheimer's disease. |
| 3171 | 14976144 | In this study we report that both the p35 and CDK5 genes are expressed in insulin-producing beta-cells of the pancreas. |
| 3172 | 14976144 | We detect in beta-cells the formation of an active p35/CDK5 complex with specific kinase activity. |
| 3173 | 14976144 | Notably, elevations of the extracellular concentration of glucose result in increases in p35 mRNA and protein levels that parallel elevations of p35/CDK5 activity. |
| 3174 | 14976144 | Functional studies show that p35 stimulates the activity of the insulin promoter and that the stimulation requires CDK5 because stimulation is blocked by roscovitine, an inhibitor of CDK5 activity, a dominant negative form of CDK5, and small interfering RNAs against p35. |
| 3175 | 14976144 | Our findings indicate that the expression of p35 and CDK5 in insulin-producing beta-cells ensembles a new signaling pathway, the activity of which is controlled by glucose, and its functional role may comprise the regulation of various biological processes in beta-cells, such as is the case for expression of the insulin gene. |
| 3176 | 14983239 | Cardiovascular risk profile, serum albumin, serum amyloid A (SAA) and fibrinogen were obtained at baseline, and patients were followed for median 21 months (interquartile range 12 to 25) for the occurrence of major adverse cardiac events (MACE: myocardial infarction, percutaneous coronary interventions, coronary artery bypass graft, and death). |
| 3177 | 14983239 | Low albumin predicted MACE independently of SAA and fibrinogen. |
| 3178 | 14986904 | Recent data on experimental atherosclerosis in mice show that (a) insulin administration reduces the number and the size of atherosclerotic lesions in apolipoprotein E null mice; and (b) in insulin receptor substrate-2 null mice, the interruption in insulin signal transduction results in enhanced atherogenicity. |
| 3179 | 14986904 | The authors' most recent data show that a low-dose infusion of insulin in patients with AMI induces a reduction in inflammation (C-reactive protein and serum amyloid A) and oxidative stress and may have a role in myocardial protection. |
| 3180 | 15025802 | Serum amyloid A, C-reactive protein and remnant-like lipoprotein particle cholesterol in type 2 diabetic patients with coronary heart disease. |
| 3181 | 15028942 | The transcription factor pancreatic duodenal homeobox 1 (PDX-1) is uniformly expressed in early pancreatic buds of embryos as well as the beta and delta cells of the islets of Langerhans. |
| 3182 | 15028942 | It has been shown that PDX-1 is required for maintaining the pancreatic islet functions by activating gene transcriptions including insulin, somatostatin (SST), islet amyloid polypeptide, glucose transporter type 2, and glucokinase. |
| 3183 | 15033922 | We found that diet-induced insulin resistance promoted amyloidogenic beta-amyloid (Abeta) Abeta1-40 and Abeta1-42 peptide generation in the brain that corresponded with increased gamma-secretase activities and decreased insulin degrading enzyme (IDE) activities. |
| 3184 | 15033922 | Moreover, increased Abeta production also coincided with increased AD-type amyloid plaque burden in the brain and impaired performance in a spatial water maze task. |
| 3185 | 15033922 | Further exploration of the apparent interrelationship of insulin resistance to brain amyloidosis revealed a functional decrease in insulin receptor (IR)-mediated signal transduction in the brain, as suggested by decreased IR beta-subunit (IRbeta) Y1162/1163 autophosphorylation and reduced phosphatidylinositol 3 (PI3)-kinase/pS473-AKT/Protein kinase (PK)-B in these same brain regions. |
| 3186 | 15033922 | This latter finding is of particular interest given the known inhibitory role of AKT/PKB on glycogen synthase kinase (GSK)-3alpha activity, which has previously been shown to promote Abeta peptide generation. |
| 3187 | 15033922 | Most interestingly, we found that decreased pS21-GSK-3alpha and pS9-GSK-3beta phosphorylation, which is an index of GSK activation, positively correlated with the generation of brain C-terminal fragment (CTF)-gamma cleavage product of amyloid precursor protein, an index of gamma-secretase activity, in the brain of insulin-resistant relative to normoglycemic Tg2576 mice. |
| 3188 | 15033922 | Our study is consistent with the hypothesis that insulin resistance may be an underlying mechanism responsible for the observed increased relative risk for AD neuropathology, and presents the first evidence to suggest that IR signaling can influence Abeta production in the brain. |
| 3189 | 15033922 | We found that diet-induced insulin resistance promoted amyloidogenic beta-amyloid (Abeta) Abeta1-40 and Abeta1-42 peptide generation in the brain that corresponded with increased gamma-secretase activities and decreased insulin degrading enzyme (IDE) activities. |
| 3190 | 15033922 | Moreover, increased Abeta production also coincided with increased AD-type amyloid plaque burden in the brain and impaired performance in a spatial water maze task. |
| 3191 | 15033922 | Further exploration of the apparent interrelationship of insulin resistance to brain amyloidosis revealed a functional decrease in insulin receptor (IR)-mediated signal transduction in the brain, as suggested by decreased IR beta-subunit (IRbeta) Y1162/1163 autophosphorylation and reduced phosphatidylinositol 3 (PI3)-kinase/pS473-AKT/Protein kinase (PK)-B in these same brain regions. |
| 3192 | 15033922 | This latter finding is of particular interest given the known inhibitory role of AKT/PKB on glycogen synthase kinase (GSK)-3alpha activity, which has previously been shown to promote Abeta peptide generation. |
| 3193 | 15033922 | Most interestingly, we found that decreased pS21-GSK-3alpha and pS9-GSK-3beta phosphorylation, which is an index of GSK activation, positively correlated with the generation of brain C-terminal fragment (CTF)-gamma cleavage product of amyloid precursor protein, an index of gamma-secretase activity, in the brain of insulin-resistant relative to normoglycemic Tg2576 mice. |
| 3194 | 15033922 | Our study is consistent with the hypothesis that insulin resistance may be an underlying mechanism responsible for the observed increased relative risk for AD neuropathology, and presents the first evidence to suggest that IR signaling can influence Abeta production in the brain. |
| 3195 | 15039230 | Partial loss-of-function mutations in insulin-degrading enzyme that induce diabetes also impair degradation of amyloid beta-protein. |
| 3196 | 15039230 | The causes of cerebral accumulation of amyloid beta-protein (Abeta) in most cases of Alzheimer's disease (AD) remain unknown. |
| 3197 | 15039230 | We recently found that homozygous deletion of the insulin-degrading enzyme (IDE) gene in mice results in an early and marked elevation of cerebral Abeta. |
| 3198 | 15039230 | For IDE to remain a valid candidate gene for late-onset AD on functional grounds, it must be shown that partial loss of function of IDE can still alter Abeta degradation, but without causing early, severe elevation of brain Abeta. |
| 3199 | 15039230 | Here, we show that naturally occurring IDE missense mutations in a well-characterized rat model of type 2 diabetes mellitus (DM2) result in decreased catalytic efficiency and a significant approximately 15 to 30% deficit in the degradation of both insulin and Abeta. |
| 3200 | 15039230 | Endogenously secreted Abeta(40) and Abeta(42) are significantly elevated in primary neuronal cultures from animals with the IDE mutations, but there is no increase in steady-state levels of rodent Abeta in the brain up to age 14 months. |
| 3201 | 15039230 | We conclude that naturally occurring, partial loss-of-function mutations in IDE sufficient to cause DM2 also impair neuronal regulation of Abeta levels, but the brain can apparently compensate for the partial deficit during the life span of the rat. |
| 3202 | 15039230 | Partial loss-of-function mutations in insulin-degrading enzyme that induce diabetes also impair degradation of amyloid beta-protein. |
| 3203 | 15039230 | The causes of cerebral accumulation of amyloid beta-protein (Abeta) in most cases of Alzheimer's disease (AD) remain unknown. |
| 3204 | 15039230 | We recently found that homozygous deletion of the insulin-degrading enzyme (IDE) gene in mice results in an early and marked elevation of cerebral Abeta. |
| 3205 | 15039230 | For IDE to remain a valid candidate gene for late-onset AD on functional grounds, it must be shown that partial loss of function of IDE can still alter Abeta degradation, but without causing early, severe elevation of brain Abeta. |
| 3206 | 15039230 | Here, we show that naturally occurring IDE missense mutations in a well-characterized rat model of type 2 diabetes mellitus (DM2) result in decreased catalytic efficiency and a significant approximately 15 to 30% deficit in the degradation of both insulin and Abeta. |
| 3207 | 15039230 | Endogenously secreted Abeta(40) and Abeta(42) are significantly elevated in primary neuronal cultures from animals with the IDE mutations, but there is no increase in steady-state levels of rodent Abeta in the brain up to age 14 months. |
| 3208 | 15039230 | We conclude that naturally occurring, partial loss-of-function mutations in IDE sufficient to cause DM2 also impair neuronal regulation of Abeta levels, but the brain can apparently compensate for the partial deficit during the life span of the rat. |
| 3209 | 15071491 | We investigated the hypothesis that low-penetrance mutations in genes (TNFRSF1A, MEFV and NALP3/CIAS1) associated with hereditary periodic fever syndromes (HPFs) might be risk factors for AA amyloidosis among patients with chronic inflammatory disorders, including rheumatoid arthritis (RA), juvenile idiopathic arthritis (JIA), Crohn's disease, undiagnosed recurrent fevers and HPFs themselves. |
| 3210 | 15071491 | Four of 67 patients with RA plus amyloidosis had MEFV variants compared with none of 34 RA patients without amyloid (P value=0.03). |
| 3211 | 15071491 | The E148Q variant of MEFV was present in two of the three patients with TNF receptor-associated periodic syndrome (TRAPS) complicated by amyloid in two separate multiplex TRAPS families containing 5 and 16 affected members respectively, and the single patient with Muckle-Wells syndrome who had amyloidosis was homozygous for this variant. |
| 3212 | 15071491 | Although allelic variants in HPFs genes are not major susceptibility factors for AA amyloidosis in chronic inflammatory disease, low-penetrance variants of MEFV and TNFRSF1A may have clinically significant proinflammatory effects. |
| 3213 | 15071491 | We investigated the hypothesis that low-penetrance mutations in genes (TNFRSF1A, MEFV and NALP3/CIAS1) associated with hereditary periodic fever syndromes (HPFs) might be risk factors for AA amyloidosis among patients with chronic inflammatory disorders, including rheumatoid arthritis (RA), juvenile idiopathic arthritis (JIA), Crohn's disease, undiagnosed recurrent fevers and HPFs themselves. |
| 3214 | 15071491 | Four of 67 patients with RA plus amyloidosis had MEFV variants compared with none of 34 RA patients without amyloid (P value=0.03). |
| 3215 | 15071491 | The E148Q variant of MEFV was present in two of the three patients with TNF receptor-associated periodic syndrome (TRAPS) complicated by amyloid in two separate multiplex TRAPS families containing 5 and 16 affected members respectively, and the single patient with Muckle-Wells syndrome who had amyloidosis was homozygous for this variant. |
| 3216 | 15071491 | Although allelic variants in HPFs genes are not major susceptibility factors for AA amyloidosis in chronic inflammatory disease, low-penetrance variants of MEFV and TNFRSF1A may have clinically significant proinflammatory effects. |
| 3217 | 15094077 | Clinical studies have corroborated findings that patients with Alzheimer's disease are more likely than healthy older adults to have reduced insulin sensitivity, and further suggest that apolipoprotein E genotype may modulate the effects of insulin on glucose disposal, memory facilitation, and amyloid precursor protein processing. |
| 3218 | 15094078 | In early-onset familial Alzheimer disease, the inhibition of neuronal insulin receptor function may be due to competitive binding of amyloid beta (Abeta) to the insulin receptor. |
| 3219 | 15094078 | The consequences of the inhibition of neuronal insulin signal transduction may be largely identical to those of disturbances of oxidative energy metabolism and related metabolism, and of hyperphosphorylation of tau-protein. |
| 3220 | 15094078 | As far as the metabolism of amyloid precursor protein (APP) in late-onset sporadic Alzheimer disease is concerned, neuronal insulin receptor dysfunction may result in the intracellular accumulation of Abeta and in subsequent cellular damage. |
| 3221 | 15094078 | In early-onset familial Alzheimer disease, the inhibition of neuronal insulin receptor function may be due to competitive binding of amyloid beta (Abeta) to the insulin receptor. |
| 3222 | 15094078 | The consequences of the inhibition of neuronal insulin signal transduction may be largely identical to those of disturbances of oxidative energy metabolism and related metabolism, and of hyperphosphorylation of tau-protein. |
| 3223 | 15094078 | As far as the metabolism of amyloid precursor protein (APP) in late-onset sporadic Alzheimer disease is concerned, neuronal insulin receptor dysfunction may result in the intracellular accumulation of Abeta and in subsequent cellular damage. |
| 3224 | 15110389 | In the hippocampus, neuronal and, to an extent, glial expression was more marked in CA3 and CA4 than in CA1 and CA2. |
| 3225 | 15110389 | In AD, CML was found to be coexpressed with tau protein, showing the similar neurofibrillary tangle shape, as well as in neuritic plaques but not in the core of amyloid plaques. |
| 3226 | 15161755 | Diabetes due to a progressive defect in beta-cell mass in rats transgenic for human islet amyloid polypeptide (HIP Rat): a new model for type 2 diabetes. |
| 3227 | 15161755 | Also, islets in type 2 diabetes often contain deposits of islet amyloid derived from islet amyloid polypeptide (IAPP), a 37-amino acid protein cosecreted with insulin by beta-cells. |
| 3228 | 15161755 | Diabetes due to a progressive defect in beta-cell mass in rats transgenic for human islet amyloid polypeptide (HIP Rat): a new model for type 2 diabetes. |
| 3229 | 15161755 | Also, islets in type 2 diabetes often contain deposits of islet amyloid derived from islet amyloid polypeptide (IAPP), a 37-amino acid protein cosecreted with insulin by beta-cells. |
| 3230 | 15163543 | On the other hand, arsenite has high affinity for sulfhydryl groups and thus can form covalent bonds with the disulfide bridges in the molecules of insulin, insulin receptors, glucose transporters (GLUTs), and enzymes involved in glucose metabolism (e.g., pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase). |
| 3231 | 15163543 | Recent studies have shown that, in subjects with chronic arsenic exposure, oxidative stress is increased and the expression of tumor necrosis factor alpha (TNFalpha) and interleukin-6 (IL-6) is upregulated. |
| 3232 | 15163543 | Arsenite at physiologically relevant concentration also shows inhibitory effect on the expression of peroxisome proliferator-activated receptor gamma (PPARgamma), a nuclear hormone receptor important for activating insulin action. |
| 3233 | 15163543 | Oxidative stress has been suggested as a major pathogenic link to both insulin resistance and beta cell dysfunction through mechanisms involving activation of nuclear factor-kappaB (NF-kappaB), which is also activated by low levels of arsenic. |
| 3234 | 15163543 | Although without supportive data, superoxide production induced by arsenic exposure can theoretically impair insulin secretion by interaction with uncoupling protein 2 (UCP2), and oxidative stress can also cause amyloid formation in the pancreas, which could progressively destroy the insulin-secreting beta cells. |
| 3235 | 15176482 | The major neuropathological lesions defining Alzheimer's disease (AD) include neurofibrillary tangles and amyloid plaques, which are mainly composed of abnormally phosphorylated tau and amyloid-beta (A beta), respectively. |
| 3236 | 15176482 | Cerebral ischemia, chronically up-regulates expression of the amyloid precursor protein (APP), which is the precursor to the amyloid beta peptide and damages the blood-brain barrier (BBB), affecting A beta peptide clearance from the brain. |
| 3237 | 15176482 | The major neuropathological lesions defining Alzheimer's disease (AD) include neurofibrillary tangles and amyloid plaques, which are mainly composed of abnormally phosphorylated tau and amyloid-beta (A beta), respectively. |
| 3238 | 15176482 | Cerebral ischemia, chronically up-regulates expression of the amyloid precursor protein (APP), which is the precursor to the amyloid beta peptide and damages the blood-brain barrier (BBB), affecting A beta peptide clearance from the brain. |
| 3239 | 15181049 | We have recently demonstrated a potent antiinflammatory effect of troglitazone, an agonist of peroxisome proliferator-activated receptor gamma (PPARgamma) and a partial agonist of PPARalpha in both the nondiabetic obese and diabetic obese subjects. |
| 3240 | 15181049 | Nuclear factor kappaB (NFkappaB)-binding activity in mononuclear cells, plasma monocyte chemoattractant protein-1 (MCP-1), TNF-alpha, soluble intercellular adhesion molecule-1, C-reactive protein (CRP), and serum amyloid A (SAA) were measured. |
| 3241 | 15181049 | Rosiglitazone treatment resulted in a reduction in plasma MCP-1 and CRP in both groups (P < 0.05). |
| 3242 | 15181049 | Plasma TNF-alpha and SAA concentrations were inhibited significantly in the obese group (P < 0.05) but not in the obese diabetic subjects. |
| 3243 | 15181049 | NFkappaB-binding activity and plasma MCP-1, CRP, SAA, and TNF-alpha did not change in the obese and obese diabetic control groups. |
| 3244 | 15220196 | Specifically, the mBMDS cells expressed multiple genes related to pancreatic beta-cell development and function (insulin I and II, Glut2, glucose kinase, islet amyloid polypeptide, nestin, pancreatic duodenal homeobox-1 [PDX-1], and Pax6). |
| 3245 | 15243700 | Mutation at position -132 in the islet amyloid polypeptide ( IAPP) gene promoter enhances basal transcriptional activity through a new CRE-like binding site. |
| 3246 | 15259000 | Glycosylphosphatidylinositol-specific phospholipase D immunoreactivity is present in islet amyloid in type 2 diabetes. |
| 3247 | 15259000 | Since GPI-PLD is synthesized by, and secreted from, pancreatic islet beta cells, the present study examined the hypothesis that GPI-PLD associates with islet amyloid. |
| 3248 | 15259000 | Fibril formation from human islet amyloid polypeptide was determined in the absence or presence of GPI-PLD. |
| 3249 | 15259000 | In non-diabetics, GPI-PLD immunoreactivity was present and co-localized with insulin, as opposed to co-localizing with amyloid in diabetics. |
| 3250 | 15259000 | No immunoreactivity for apolipoprotein A-I was present in islet cells or islet amyloid. |
| 3251 | 15259000 | Heparan sulphate proteoglycan, which is commonly present in most amyloid, bound GPI-PLD in vitro. |
| 3252 | 15259000 | GPI-PLD inhibited the formation of amyloid fibrils from synthetic islet amyloid polypeptide in vitro. |
| 3253 | 15259000 | GPI-PLD is therefore present in islet amyloid and appears to derive from local production from islets. |
| 3254 | 15259000 | Since GPI-PLD also inhibited islet amyloid polypeptide fibril formation in vitro, it is concluded that GPI-PLD may play a role in islet amyloid formation in type 2 diabetes. |
| 3255 | 15259000 | Glycosylphosphatidylinositol-specific phospholipase D immunoreactivity is present in islet amyloid in type 2 diabetes. |
| 3256 | 15259000 | Since GPI-PLD is synthesized by, and secreted from, pancreatic islet beta cells, the present study examined the hypothesis that GPI-PLD associates with islet amyloid. |
| 3257 | 15259000 | Fibril formation from human islet amyloid polypeptide was determined in the absence or presence of GPI-PLD. |
| 3258 | 15259000 | In non-diabetics, GPI-PLD immunoreactivity was present and co-localized with insulin, as opposed to co-localizing with amyloid in diabetics. |
| 3259 | 15259000 | No immunoreactivity for apolipoprotein A-I was present in islet cells or islet amyloid. |
| 3260 | 15259000 | Heparan sulphate proteoglycan, which is commonly present in most amyloid, bound GPI-PLD in vitro. |
| 3261 | 15259000 | GPI-PLD inhibited the formation of amyloid fibrils from synthetic islet amyloid polypeptide in vitro. |
| 3262 | 15259000 | GPI-PLD is therefore present in islet amyloid and appears to derive from local production from islets. |
| 3263 | 15259000 | Since GPI-PLD also inhibited islet amyloid polypeptide fibril formation in vitro, it is concluded that GPI-PLD may play a role in islet amyloid formation in type 2 diabetes. |
| 3264 | 15259000 | Glycosylphosphatidylinositol-specific phospholipase D immunoreactivity is present in islet amyloid in type 2 diabetes. |
| 3265 | 15259000 | Since GPI-PLD is synthesized by, and secreted from, pancreatic islet beta cells, the present study examined the hypothesis that GPI-PLD associates with islet amyloid. |
| 3266 | 15259000 | Fibril formation from human islet amyloid polypeptide was determined in the absence or presence of GPI-PLD. |
| 3267 | 15259000 | In non-diabetics, GPI-PLD immunoreactivity was present and co-localized with insulin, as opposed to co-localizing with amyloid in diabetics. |
| 3268 | 15259000 | No immunoreactivity for apolipoprotein A-I was present in islet cells or islet amyloid. |
| 3269 | 15259000 | Heparan sulphate proteoglycan, which is commonly present in most amyloid, bound GPI-PLD in vitro. |
| 3270 | 15259000 | GPI-PLD inhibited the formation of amyloid fibrils from synthetic islet amyloid polypeptide in vitro. |
| 3271 | 15259000 | GPI-PLD is therefore present in islet amyloid and appears to derive from local production from islets. |
| 3272 | 15259000 | Since GPI-PLD also inhibited islet amyloid polypeptide fibril formation in vitro, it is concluded that GPI-PLD may play a role in islet amyloid formation in type 2 diabetes. |
| 3273 | 15259000 | Glycosylphosphatidylinositol-specific phospholipase D immunoreactivity is present in islet amyloid in type 2 diabetes. |
| 3274 | 15259000 | Since GPI-PLD is synthesized by, and secreted from, pancreatic islet beta cells, the present study examined the hypothesis that GPI-PLD associates with islet amyloid. |
| 3275 | 15259000 | Fibril formation from human islet amyloid polypeptide was determined in the absence or presence of GPI-PLD. |
| 3276 | 15259000 | In non-diabetics, GPI-PLD immunoreactivity was present and co-localized with insulin, as opposed to co-localizing with amyloid in diabetics. |
| 3277 | 15259000 | No immunoreactivity for apolipoprotein A-I was present in islet cells or islet amyloid. |
| 3278 | 15259000 | Heparan sulphate proteoglycan, which is commonly present in most amyloid, bound GPI-PLD in vitro. |
| 3279 | 15259000 | GPI-PLD inhibited the formation of amyloid fibrils from synthetic islet amyloid polypeptide in vitro. |
| 3280 | 15259000 | GPI-PLD is therefore present in islet amyloid and appears to derive from local production from islets. |
| 3281 | 15259000 | Since GPI-PLD also inhibited islet amyloid polypeptide fibril formation in vitro, it is concluded that GPI-PLD may play a role in islet amyloid formation in type 2 diabetes. |
| 3282 | 15259000 | Glycosylphosphatidylinositol-specific phospholipase D immunoreactivity is present in islet amyloid in type 2 diabetes. |
| 3283 | 15259000 | Since GPI-PLD is synthesized by, and secreted from, pancreatic islet beta cells, the present study examined the hypothesis that GPI-PLD associates with islet amyloid. |
| 3284 | 15259000 | Fibril formation from human islet amyloid polypeptide was determined in the absence or presence of GPI-PLD. |
| 3285 | 15259000 | In non-diabetics, GPI-PLD immunoreactivity was present and co-localized with insulin, as opposed to co-localizing with amyloid in diabetics. |
| 3286 | 15259000 | No immunoreactivity for apolipoprotein A-I was present in islet cells or islet amyloid. |
| 3287 | 15259000 | Heparan sulphate proteoglycan, which is commonly present in most amyloid, bound GPI-PLD in vitro. |
| 3288 | 15259000 | GPI-PLD inhibited the formation of amyloid fibrils from synthetic islet amyloid polypeptide in vitro. |
| 3289 | 15259000 | GPI-PLD is therefore present in islet amyloid and appears to derive from local production from islets. |
| 3290 | 15259000 | Since GPI-PLD also inhibited islet amyloid polypeptide fibril formation in vitro, it is concluded that GPI-PLD may play a role in islet amyloid formation in type 2 diabetes. |
| 3291 | 15259000 | Glycosylphosphatidylinositol-specific phospholipase D immunoreactivity is present in islet amyloid in type 2 diabetes. |
| 3292 | 15259000 | Since GPI-PLD is synthesized by, and secreted from, pancreatic islet beta cells, the present study examined the hypothesis that GPI-PLD associates with islet amyloid. |
| 3293 | 15259000 | Fibril formation from human islet amyloid polypeptide was determined in the absence or presence of GPI-PLD. |
| 3294 | 15259000 | In non-diabetics, GPI-PLD immunoreactivity was present and co-localized with insulin, as opposed to co-localizing with amyloid in diabetics. |
| 3295 | 15259000 | No immunoreactivity for apolipoprotein A-I was present in islet cells or islet amyloid. |
| 3296 | 15259000 | Heparan sulphate proteoglycan, which is commonly present in most amyloid, bound GPI-PLD in vitro. |
| 3297 | 15259000 | GPI-PLD inhibited the formation of amyloid fibrils from synthetic islet amyloid polypeptide in vitro. |
| 3298 | 15259000 | GPI-PLD is therefore present in islet amyloid and appears to derive from local production from islets. |
| 3299 | 15259000 | Since GPI-PLD also inhibited islet amyloid polypeptide fibril formation in vitro, it is concluded that GPI-PLD may play a role in islet amyloid formation in type 2 diabetes. |
| 3300 | 15259000 | Glycosylphosphatidylinositol-specific phospholipase D immunoreactivity is present in islet amyloid in type 2 diabetes. |
| 3301 | 15259000 | Since GPI-PLD is synthesized by, and secreted from, pancreatic islet beta cells, the present study examined the hypothesis that GPI-PLD associates with islet amyloid. |
| 3302 | 15259000 | Fibril formation from human islet amyloid polypeptide was determined in the absence or presence of GPI-PLD. |
| 3303 | 15259000 | In non-diabetics, GPI-PLD immunoreactivity was present and co-localized with insulin, as opposed to co-localizing with amyloid in diabetics. |
| 3304 | 15259000 | No immunoreactivity for apolipoprotein A-I was present in islet cells or islet amyloid. |
| 3305 | 15259000 | Heparan sulphate proteoglycan, which is commonly present in most amyloid, bound GPI-PLD in vitro. |
| 3306 | 15259000 | GPI-PLD inhibited the formation of amyloid fibrils from synthetic islet amyloid polypeptide in vitro. |
| 3307 | 15259000 | GPI-PLD is therefore present in islet amyloid and appears to derive from local production from islets. |
| 3308 | 15259000 | Since GPI-PLD also inhibited islet amyloid polypeptide fibril formation in vitro, it is concluded that GPI-PLD may play a role in islet amyloid formation in type 2 diabetes. |
| 3309 | 15259000 | Glycosylphosphatidylinositol-specific phospholipase D immunoreactivity is present in islet amyloid in type 2 diabetes. |
| 3310 | 15259000 | Since GPI-PLD is synthesized by, and secreted from, pancreatic islet beta cells, the present study examined the hypothesis that GPI-PLD associates with islet amyloid. |
| 3311 | 15259000 | Fibril formation from human islet amyloid polypeptide was determined in the absence or presence of GPI-PLD. |
| 3312 | 15259000 | In non-diabetics, GPI-PLD immunoreactivity was present and co-localized with insulin, as opposed to co-localizing with amyloid in diabetics. |
| 3313 | 15259000 | No immunoreactivity for apolipoprotein A-I was present in islet cells or islet amyloid. |
| 3314 | 15259000 | Heparan sulphate proteoglycan, which is commonly present in most amyloid, bound GPI-PLD in vitro. |
| 3315 | 15259000 | GPI-PLD inhibited the formation of amyloid fibrils from synthetic islet amyloid polypeptide in vitro. |
| 3316 | 15259000 | GPI-PLD is therefore present in islet amyloid and appears to derive from local production from islets. |
| 3317 | 15259000 | Since GPI-PLD also inhibited islet amyloid polypeptide fibril formation in vitro, it is concluded that GPI-PLD may play a role in islet amyloid formation in type 2 diabetes. |
| 3318 | 15259000 | Glycosylphosphatidylinositol-specific phospholipase D immunoreactivity is present in islet amyloid in type 2 diabetes. |
| 3319 | 15259000 | Since GPI-PLD is synthesized by, and secreted from, pancreatic islet beta cells, the present study examined the hypothesis that GPI-PLD associates with islet amyloid. |
| 3320 | 15259000 | Fibril formation from human islet amyloid polypeptide was determined in the absence or presence of GPI-PLD. |
| 3321 | 15259000 | In non-diabetics, GPI-PLD immunoreactivity was present and co-localized with insulin, as opposed to co-localizing with amyloid in diabetics. |
| 3322 | 15259000 | No immunoreactivity for apolipoprotein A-I was present in islet cells or islet amyloid. |
| 3323 | 15259000 | Heparan sulphate proteoglycan, which is commonly present in most amyloid, bound GPI-PLD in vitro. |
| 3324 | 15259000 | GPI-PLD inhibited the formation of amyloid fibrils from synthetic islet amyloid polypeptide in vitro. |
| 3325 | 15259000 | GPI-PLD is therefore present in islet amyloid and appears to derive from local production from islets. |
| 3326 | 15259000 | Since GPI-PLD also inhibited islet amyloid polypeptide fibril formation in vitro, it is concluded that GPI-PLD may play a role in islet amyloid formation in type 2 diabetes. |
| 3327 | 15279557 | In a similar way, the glycation rate of hemoglobin, isolated from diabetic blood and of beta-2-microglobulin isolated from amyloid plaques from uremic patients was determined. |
| 3328 | 15285718 | Alternative translation initiation generates a novel isoform of insulin-degrading enzyme targeted to mitochondria. |
| 3329 | 15285718 | IDE (insulin-degrading enzyme) is a widely expressed zinc-metallopeptidase that has been shown to regulate both cerebral amyloid beta-peptide and plasma insulin levels in vivo. |
| 3330 | 15286457 | On the other hand, the macrophage migration inhibitory factor (MIF) is a cytokine with multiple biological activities, including the ability to act as potent amyloid beta (A-beta)-binding protein. |
| 3331 | 15286457 | Two common polymorphisms have been recently detected in the genes encoding for CRP and MIF and have been associated with significant modifications of plasma levels and activity of the corresponding proteins. |
| 3332 | 15286457 | Following these observations, we hypothesized that CRP and MIF gene polymorphisms might contribute to the development and progression of neurodegenerative disorders and evaluated their association with AD. |
| 3333 | 15286457 | CRP and MIF gene polymorphisms were examined by polymerase chain reaction and restriction enzyme analysis in 116 Italian subjects affected by probable AD and 184 age- and sex-matched controls. |
| 3334 | 15286457 | We did not find a statistically significant difference in the distribution of CRP and MIF genotypes and alleles between AD subjects and controls. |
| 3335 | 15286457 | Although these data need further confirmation, they indicate that CRP and MIF gene polymorphisms are not associated with AD. |
| 3336 | 15292167 | Amyloidogenicity and cytotoxicity of recombinant mature human islet amyloid polypeptide (rhIAPP). |
| 3337 | 15292167 | Pancreatic amyloid plaques formed by the pancreatic islet amyloid polypeptide (IAPP) are present in more than 95% of type II diabetes mellitus patients, and their abundance correlates with the severity of the disease. |
| 3338 | 15292167 | Amyloidogenicity and cytotoxicity of recombinant mature human islet amyloid polypeptide (rhIAPP). |
| 3339 | 15292167 | Pancreatic amyloid plaques formed by the pancreatic islet amyloid polypeptide (IAPP) are present in more than 95% of type II diabetes mellitus patients, and their abundance correlates with the severity of the disease. |
| 3340 | 15292279 | Islet amyloid deposition is a pathogenic feature of type 2 diabetes, and these deposits contain the unique amyloidogenic peptide islet amyloid polypeptide. |
| 3341 | 15292279 | Furthermore, the extent of amyloid deposition is associated with both loss of beta-cell mass and impairment in insulin secretion and glucose metabolism, suggesting a causative role for islet amyloid in the islet lesion of type 2 diabetes. |
| 3342 | 15292279 | These animal studies have also shown that beta-cell dysfunction seems to be an important prerequisite for islet amyloid formation, with increased secretory demand from obesity and/or insulin resistance acting to further increase islet amyloid deposition. |
| 3343 | 15292279 | Recent in vitro studies suggest that the cytotoxic species responsible for islet amyloid-induced beta-cell death are formed during the very early stages of islet amyloid formation, when islet amyloid polypeptide aggregation commences. |
| 3344 | 15292279 | Islet amyloid deposition is a pathogenic feature of type 2 diabetes, and these deposits contain the unique amyloidogenic peptide islet amyloid polypeptide. |
| 3345 | 15292279 | Furthermore, the extent of amyloid deposition is associated with both loss of beta-cell mass and impairment in insulin secretion and glucose metabolism, suggesting a causative role for islet amyloid in the islet lesion of type 2 diabetes. |
| 3346 | 15292279 | These animal studies have also shown that beta-cell dysfunction seems to be an important prerequisite for islet amyloid formation, with increased secretory demand from obesity and/or insulin resistance acting to further increase islet amyloid deposition. |
| 3347 | 15292279 | Recent in vitro studies suggest that the cytotoxic species responsible for islet amyloid-induced beta-cell death are formed during the very early stages of islet amyloid formation, when islet amyloid polypeptide aggregation commences. |
| 3348 | 15292279 | Islet amyloid deposition is a pathogenic feature of type 2 diabetes, and these deposits contain the unique amyloidogenic peptide islet amyloid polypeptide. |
| 3349 | 15292279 | Furthermore, the extent of amyloid deposition is associated with both loss of beta-cell mass and impairment in insulin secretion and glucose metabolism, suggesting a causative role for islet amyloid in the islet lesion of type 2 diabetes. |
| 3350 | 15292279 | These animal studies have also shown that beta-cell dysfunction seems to be an important prerequisite for islet amyloid formation, with increased secretory demand from obesity and/or insulin resistance acting to further increase islet amyloid deposition. |
| 3351 | 15292279 | Recent in vitro studies suggest that the cytotoxic species responsible for islet amyloid-induced beta-cell death are formed during the very early stages of islet amyloid formation, when islet amyloid polypeptide aggregation commences. |
| 3352 | 15292279 | Islet amyloid deposition is a pathogenic feature of type 2 diabetes, and these deposits contain the unique amyloidogenic peptide islet amyloid polypeptide. |
| 3353 | 15292279 | Furthermore, the extent of amyloid deposition is associated with both loss of beta-cell mass and impairment in insulin secretion and glucose metabolism, suggesting a causative role for islet amyloid in the islet lesion of type 2 diabetes. |
| 3354 | 15292279 | These animal studies have also shown that beta-cell dysfunction seems to be an important prerequisite for islet amyloid formation, with increased secretory demand from obesity and/or insulin resistance acting to further increase islet amyloid deposition. |
| 3355 | 15292279 | Recent in vitro studies suggest that the cytotoxic species responsible for islet amyloid-induced beta-cell death are formed during the very early stages of islet amyloid formation, when islet amyloid polypeptide aggregation commences. |
| 3356 | 15321714 | Islet amyloid polypeptide (IAPP) is a 37-residue hormone that forms cytotoxic amyloid fibers in the endocrine pancreas of patients with type II diabetes (NIDDM). |
| 3357 | 15358791 | Identifying structural features of fibrillar islet amyloid polypeptide using site-directed spin labeling. |
| 3358 | 15358791 | Pancreatic amyloid deposits, composed primarily of the 37-residue islet amyloid polypeptide (IAPP), are a characteristic feature found in more than 90% of patients with type II diabetes. |
| 3359 | 15358791 | Identifying structural features of fibrillar islet amyloid polypeptide using site-directed spin labeling. |
| 3360 | 15358791 | Pancreatic amyloid deposits, composed primarily of the 37-residue islet amyloid polypeptide (IAPP), are a characteristic feature found in more than 90% of patients with type II diabetes. |
| 3361 | 15464829 | The SAMP8 mouse, a model of Alzheimer's disease, has an age-related impairment in learning and memory and an increase in brain levels of amyloid precursor protein (APP) and amyloid beta protein (Abeta). |
| 3362 | 15527771 | Islet amyloid polypeptide-induced membrane leakage involves uptake of lipids by forming amyloid fibers. |
| 3363 | 15527771 | Fibril formation of islet amyloid polypeptide (IAPP) is associated with cell death of the insulin-producing pancreatic beta-cells in patients with Type 2 Diabetes Mellitus. |
| 3364 | 15527771 | Islet amyloid polypeptide-induced membrane leakage involves uptake of lipids by forming amyloid fibers. |
| 3365 | 15527771 | Fibril formation of islet amyloid polypeptide (IAPP) is associated with cell death of the insulin-producing pancreatic beta-cells in patients with Type 2 Diabetes Mellitus. |
| 3366 | 15533050 | Inhibition of islet amyloid polypeptide fibril formation: a potential role for heteroaromatic interactions. |
| 3367 | 15533050 | Here, we demonstrate efficient inhibition of amyloid formation of the type 2 diabetes-related human islet amyloid polypeptide (hIAPP) by a modified aromatic peptide fragment and a small aromatic polyphenol molecule. |
| 3368 | 15533050 | Inhibition of islet amyloid polypeptide fibril formation: a potential role for heteroaromatic interactions. |
| 3369 | 15533050 | Here, we demonstrate efficient inhibition of amyloid formation of the type 2 diabetes-related human islet amyloid polypeptide (hIAPP) by a modified aromatic peptide fragment and a small aromatic polyphenol molecule. |
| 3370 | 15570177 | The objective of this study was to find out which N-terminal segment/s of amyloid precursor protein (APP) has any neurotrophic properties, since soluble APP-alpha (sAPP-alpha) has neurotrophic effects. |
| 3371 | 15590928 | Insulin-degrading enzyme as a downstream target of insulin receptor signaling cascade: implications for Alzheimer's disease intervention. |
| 3372 | 15590928 | Insulin-degrading enzyme (IDE) is one of the proteins that has been demonstrated to play a key role in degrading beta-amyloid (Abeta) monomer in vitro and in vivo, raising the possibility of upregulating IDE as an approach to reduce Abeta. |
| 3373 | 15590928 | Because one of the main functions of IDE is to degrade insulin, we hypothesized that there is a negative feedback mechanism whereby stimulation of insulin receptor-mediated signaling upregulates IDE to prevent chronic activation of the pathway. |
| 3374 | 15590928 | We show that treatment of primary hippocampal neurons with insulin increased IDE protein levels by approximately 25%. |
| 3375 | 15590928 | Insulin treatment also led to phosphatidylinositol-3 (PI3) kinase activation evidenced by Akt phosphorylation, which was blocked by PI3 kinase inhibitors, wortmannin and LY 294002. |
| 3376 | 15590928 | Inhibition of PI3 kinase abolished the IDE upregulation by insulin, indicating a cause-effect relationship between insulin signaling and IDE upregulation. |
| 3377 | 15590928 | Further support for this link was provided by the findings that deficient insulin signaling (decreased PI3 kinase subunit P85) was correlated with reduced IDE in Alzheimer's disease (AD) brains and in Tg2576 Swedish amyloid precursor protein transgenic mice fed a safflower oil-enriched ("Bad") diet used to accelerate pathogenesis. |
| 3378 | 15590928 | Consistent with IDE function in the degradation of Abeta monomer, the IDE decrease in the Bad diet-fed Tg2576 mice was associated with increased Abeta monomer levels. |
| 3379 | 15590928 | These in vitro and in vivo analyses validate the use of enhanced CNS insulin signaling as a potential strategy for AD intervention to correct the IDE defects occurring in AD. |
| 3380 | 15618358 | Role of carboxypeptidase E in processing of pro-islet amyloid polypeptide in {beta}-cells. |
| 3381 | 15618358 | Islet amyloid polypeptide (IAPP; amylin) is a peptide hormone that is cosecreted with insulin from beta-cells. |
| 3382 | 15618358 | In this study, we investigated the role of carboxypeptidase E (CPE) in the processing of proIAPP using mice lacking active CPE (Cpe(fat)/Cpe(fat)) and NIT-2 cells, a beta-cell line derived from their islets. |
| 3383 | 15618358 | Impaired proIAPP processing was associated with a decrease in PC2 (but not PC1/3) and both the 21- and 27-kDa forms of the PC2 chaperone protein 7B2, suggesting that PC2-mediated processing of proIAPP at its NH(2) terminus was impaired in the absence of CPE. |
| 3384 | 15618358 | We conclude that lack of CPE in islet beta-cells results in a marked decrease in processing of proIAPP at its NH(2) (but not COOH) terminus that is associated with attenuated levels of PC2 and (pro)7B2 and a great reduction in formation of mature amidated IAPP. |
| 3385 | 15618358 | Role of carboxypeptidase E in processing of pro-islet amyloid polypeptide in {beta}-cells. |
| 3386 | 15618358 | Islet amyloid polypeptide (IAPP; amylin) is a peptide hormone that is cosecreted with insulin from beta-cells. |
| 3387 | 15618358 | In this study, we investigated the role of carboxypeptidase E (CPE) in the processing of proIAPP using mice lacking active CPE (Cpe(fat)/Cpe(fat)) and NIT-2 cells, a beta-cell line derived from their islets. |
| 3388 | 15618358 | Impaired proIAPP processing was associated with a decrease in PC2 (but not PC1/3) and both the 21- and 27-kDa forms of the PC2 chaperone protein 7B2, suggesting that PC2-mediated processing of proIAPP at its NH(2) terminus was impaired in the absence of CPE. |
| 3389 | 15618358 | We conclude that lack of CPE in islet beta-cells results in a marked decrease in processing of proIAPP at its NH(2) (but not COOH) terminus that is associated with attenuated levels of PC2 and (pro)7B2 and a great reduction in formation of mature amidated IAPP. |
| 3390 | 15710403 | Neutron diffraction reveals sequence-specific membrane insertion of pre-fibrillar islet amyloid polypeptide and inhibition by rifampicin. |
| 3391 | 15710403 | Human islet amyloid polypeptide (hIAPP) forms amyloid deposits in non-insulin-dependent diabetes mellitus (NIDDM). |
| 3392 | 15710403 | Neutron diffraction reveals sequence-specific membrane insertion of pre-fibrillar islet amyloid polypeptide and inhibition by rifampicin. |
| 3393 | 15710403 | Human islet amyloid polypeptide (hIAPP) forms amyloid deposits in non-insulin-dependent diabetes mellitus (NIDDM). |
| 3394 | 15750215 | Impaired insulin and insulin-like growth factor expression and signaling mechanisms in Alzheimer's disease--is this type 3 diabetes? |
| 3395 | 15750215 | The present work demonstrates extensive abnormalities in insulin and insulin-like growth factor type I and II (IGF-I and IGF-II) signaling mechanisms in brains with AD, and shows that while each of the corresponding growth factors is normally made in central nervous system (CNS) neurons, the expression levels are markedly reduced in AD. |
| 3396 | 15750215 | These abnormalities were associated with reduced levels of insulin receptor substrate (IRS) mRNA, tau mRNA, IRS-associated phosphotidylinositol 3-kinase, and phospho-Akt (activated), and increased glycogen synthase kinase-3beta activity and amyloid precursor protein mRNA expression. |
| 3397 | 15750215 | The strikingly reduced CNS expression of genes encoding insulin, IGF-I, and IGF-II, as well as the insulin and IGF-I receptors, suggests that AD may represent a neuro-endocrine disorder that resembles, yet is distinct from diabetes mellitus. |
| 3398 | 15755688 | Insulin protects against amyloid beta-peptide toxicity in brain mitochondria of diabetic rats. |
| 3399 | 15755688 | We observed that STZ-induced diabetes promoted a significant decrease in mitochondrial CoQ9, ATPase activity, and a lower capacity of mitochondria to accumulate Ca2+ when compared with control and insulin-treated diabetic rats. |
| 3400 | 15755688 | However, in the presence of amyloid beta-peptide, insulin seems to prevent the decline in mitochondrial oxidative phosphorylation efficiency and avoids an increase in oxidative stress, improving or preserving the function of neurons under adverse conditions, such as Alzheimer's disease. |
| 3401 | 15755688 | Insulin protects against amyloid beta-peptide toxicity in brain mitochondria of diabetic rats. |
| 3402 | 15755688 | We observed that STZ-induced diabetes promoted a significant decrease in mitochondrial CoQ9, ATPase activity, and a lower capacity of mitochondria to accumulate Ca2+ when compared with control and insulin-treated diabetic rats. |
| 3403 | 15755688 | However, in the presence of amyloid beta-peptide, insulin seems to prevent the decline in mitochondrial oxidative phosphorylation efficiency and avoids an increase in oxidative stress, improving or preserving the function of neurons under adverse conditions, such as Alzheimer's disease. |
| 3404 | 15778964 | Molecular dynamics simulation of the aggregation of the core-recognition motif of the islet amyloid polypeptide in explicit water. |
| 3405 | 15778964 | Here, we used molecular dynamics simulations to study the initial self-assembly stages of the NH2-NFGAIL-COOH peptide, the core-recognition motif of the type II diabetes associated islet amyloid polypeptide. |
| 3406 | 15778964 | Molecular dynamics simulation of the aggregation of the core-recognition motif of the islet amyloid polypeptide in explicit water. |
| 3407 | 15778964 | Here, we used molecular dynamics simulations to study the initial self-assembly stages of the NH2-NFGAIL-COOH peptide, the core-recognition motif of the type II diabetes associated islet amyloid polypeptide. |
| 3408 | 15784251 | Transthyretin is an amyloidogenic protein which is involved in familial amyloid polyneuropathy, the most common form of systemic amyloid disease. |
| 3409 | 15791482 | Transversal sections of head, body and tail segments were stained with synaptophysin combined with Congo red to map/quantify islet tissue and amyloid. |
| 3410 | 15802374 | Processing of pro-islet amyloid polypeptide in the constitutive and regulated secretory pathways of beta cells. |
| 3411 | 15802374 | Islet amyloid is a pathologic characteristic of the pancreas in type 2 diabetes comprised mainly of the beta-cell peptide islet amyloid polypeptide (IAPP; amylin). |
| 3412 | 15802374 | We conclude that normal processing of proIAPP is a two-step process initiated by cleavage at its COOH terminus (likely by prohormone convertase 1/3 in the TGN) followed by cleavage at its NH2 terminus (by prohormone convertase 2 in granules) to form IAPP. |
| 3413 | 15802374 | Processing of pro-islet amyloid polypeptide in the constitutive and regulated secretory pathways of beta cells. |
| 3414 | 15802374 | Islet amyloid is a pathologic characteristic of the pancreas in type 2 diabetes comprised mainly of the beta-cell peptide islet amyloid polypeptide (IAPP; amylin). |
| 3415 | 15802374 | We conclude that normal processing of proIAPP is a two-step process initiated by cleavage at its COOH terminus (likely by prohormone convertase 1/3 in the TGN) followed by cleavage at its NH2 terminus (by prohormone convertase 2 in granules) to form IAPP. |
| 3416 | 15803463 | Template-directed self-assembly and growth of insulin amyloid fibrils. |
| 3417 | 15803463 | In the present work, we developed a novel, synthetic amyloid template by attaching amyloid seeds covalently onto an N-hydroxysuccinimide-activated surface, where insulin was chosen as a model amyloidogenic protein. |
| 3418 | 15803463 | According to ex situ atomic force microscopy observations, insulin monomers in solution were deposited onto the synthetic amyloid template to form fibrils, like hair growth. |
| 3419 | 15803463 | The amyloid deposition rate followed saturation kinetics with respect to insulin concentration in the solution. |
| 3420 | 15803463 | Template-directed self-assembly and growth of insulin amyloid fibrils. |
| 3421 | 15803463 | In the present work, we developed a novel, synthetic amyloid template by attaching amyloid seeds covalently onto an N-hydroxysuccinimide-activated surface, where insulin was chosen as a model amyloidogenic protein. |
| 3422 | 15803463 | According to ex situ atomic force microscopy observations, insulin monomers in solution were deposited onto the synthetic amyloid template to form fibrils, like hair growth. |
| 3423 | 15803463 | The amyloid deposition rate followed saturation kinetics with respect to insulin concentration in the solution. |
| 3424 | 15803463 | Template-directed self-assembly and growth of insulin amyloid fibrils. |
| 3425 | 15803463 | In the present work, we developed a novel, synthetic amyloid template by attaching amyloid seeds covalently onto an N-hydroxysuccinimide-activated surface, where insulin was chosen as a model amyloidogenic protein. |
| 3426 | 15803463 | According to ex situ atomic force microscopy observations, insulin monomers in solution were deposited onto the synthetic amyloid template to form fibrils, like hair growth. |
| 3427 | 15803463 | The amyloid deposition rate followed saturation kinetics with respect to insulin concentration in the solution. |
| 3428 | 15803463 | Template-directed self-assembly and growth of insulin amyloid fibrils. |
| 3429 | 15803463 | In the present work, we developed a novel, synthetic amyloid template by attaching amyloid seeds covalently onto an N-hydroxysuccinimide-activated surface, where insulin was chosen as a model amyloidogenic protein. |
| 3430 | 15803463 | According to ex situ atomic force microscopy observations, insulin monomers in solution were deposited onto the synthetic amyloid template to form fibrils, like hair growth. |
| 3431 | 15803463 | The amyloid deposition rate followed saturation kinetics with respect to insulin concentration in the solution. |
| 3432 | 15823385 | Several mechanisms have been proposed, including increased non-esterified fatty acids, inflammatory cytokines, adipokines, and mitochondrial dysfunction for insulin resistance, and glucotoxicity, lipotoxicity, and amyloid formation for beta-cell dysfunction. |
| 3433 | 15823385 | Moreover, the disease has a strong genetic component, but only a handful of genes have been identified so far: genes for calpain 10, potassium inward-rectifier 6.2, peroxisome proliferator-activated receptor gamma, insulin receptor substrate-1, and others. |
| 3434 | 15823718 | AD is characterized pathologically by the presence of senile plaques and neurofibrillary tangles (NFTs), the major constituents of which are the amyloid beta protein (Abeta) and tau protein, respectively. |
| 3435 | 15823718 | Glycation of Abeta markedly enhances its aggregation in vitro, and the glycation of tau, in addition to hyperphosphorylation, appears to enhance the formation of paired helical filaments. |
| 3436 | 15826250 | In type 2 diabetes, beta islet cells die by cytotoxic effects of smaller amylin (islet amyloid polypeptide, IAPP) aggregates, and the interstitial space created by the necrotic beta cells is replaced by larger IAPP aggregates, to form complex, polymerized islet amyloid. |
| 3437 | 15843464 | In vivo fragmentation of heparan sulfate by heparanase overexpression renders mice resistant to amyloid protein A amyloidosis. |
| 3438 | 15843464 | We have generated transgenic mice that overexpress human heparanase and have tested their susceptibility to amyloid induction. |
| 3439 | 15843464 | By contrast, the spleens of transgenic mice that failed to significantly overexpress heparanase contained heparan sulfate chains similar in size to those of control spleen and remained susceptible to amyloid deposition. |
| 3440 | 15843464 | In vivo fragmentation of heparan sulfate by heparanase overexpression renders mice resistant to amyloid protein A amyloidosis. |
| 3441 | 15843464 | We have generated transgenic mice that overexpress human heparanase and have tested their susceptibility to amyloid induction. |
| 3442 | 15843464 | By contrast, the spleens of transgenic mice that failed to significantly overexpress heparanase contained heparan sulfate chains similar in size to those of control spleen and remained susceptible to amyloid deposition. |
| 3443 | 15843464 | In vivo fragmentation of heparan sulfate by heparanase overexpression renders mice resistant to amyloid protein A amyloidosis. |
| 3444 | 15843464 | We have generated transgenic mice that overexpress human heparanase and have tested their susceptibility to amyloid induction. |
| 3445 | 15843464 | By contrast, the spleens of transgenic mice that failed to significantly overexpress heparanase contained heparan sulfate chains similar in size to those of control spleen and remained susceptible to amyloid deposition. |
| 3446 | 15850385 | Alternative splicing of human insulin-degrading enzyme yields a novel isoform with a decreased ability to degrade insulin and amyloid beta-protein. |
| 3447 | 15850385 | Deletion of insulin-degrading enzyme (IDE) in mice causes accumulation of cerebral amyloid beta-protein (Abeta), hyperinsulinemia, and glucose intolerance. |
| 3448 | 15850385 | Here, we systematically characterize human IDE mRNAs, identify a novel splice form, and compare its subcellular distribution, kinetic properties, and ability to degrade Abeta to the known isoform. |
| 3449 | 15850385 | The apparent K(m) values of recombinant 15b-IDE for both insulin and Abeta are significantly higher and the k(cat) and catalytic efficiency markedly lower than those of 15a-IDE. |
| 3450 | 15850385 | Alternative splicing of human insulin-degrading enzyme yields a novel isoform with a decreased ability to degrade insulin and amyloid beta-protein. |
| 3451 | 15850385 | Deletion of insulin-degrading enzyme (IDE) in mice causes accumulation of cerebral amyloid beta-protein (Abeta), hyperinsulinemia, and glucose intolerance. |
| 3452 | 15850385 | Here, we systematically characterize human IDE mRNAs, identify a novel splice form, and compare its subcellular distribution, kinetic properties, and ability to degrade Abeta to the known isoform. |
| 3453 | 15850385 | The apparent K(m) values of recombinant 15b-IDE for both insulin and Abeta are significantly higher and the k(cat) and catalytic efficiency markedly lower than those of 15a-IDE. |
| 3454 | 15878744 | Islet amyloid polypeptide gene promoter polymorphisms are not associated with Type 2 diabetes or with the severity of islet amyloidosis. |
| 3455 | 15878744 | The over-expression of the islet amyloid polypeptide (IAPP) gene could be a causal factor for islet amyloidosis and beta-cell destruction in Type 2 diabetes (T2DM). |
| 3456 | 15878744 | Islet amyloid polypeptide gene promoter polymorphisms are not associated with Type 2 diabetes or with the severity of islet amyloidosis. |
| 3457 | 15878744 | The over-expression of the islet amyloid polypeptide (IAPP) gene could be a causal factor for islet amyloidosis and beta-cell destruction in Type 2 diabetes (T2DM). |
| 3458 | 15896716 | beta-cells die by apoptosis in type 1 diabetes as a result of autoimmune attack mediated by cytokines, and in type 2 diabetes by various perpetrators including human islet amyloid polypeptide (hIAPP). |
| 3459 | 15896716 | Both proliferating and growth-arrested cells expressing p35 manifested increased resistance to cytokines and hIAPP, compared with control cells, as judged by cell viability, DNA fragmentation, and caspase-3 activity assays. p35 was significantly more protective in growth-arrested, compared with proliferating, cells. |
| 3460 | 15896716 | No significant differences were observed in proliferation and insulin content between cells expressing p35 and control cells. |
| 3461 | 15896716 | In contrast, p35 manifested a perturbing effect on glucose-induced insulin secretion. |
| 3462 | 15917096 | Plasma amyloid beta protein 42 in non-demented persons aged 75 years: effects of concomitant medication and medial temporal lobe atrophy. |
| 3463 | 15917096 | In the multiple regression analysis considering possible interactions between various medications statin users showed a significant decrease of Abeta42; insulin users had again significantly higher and long-term gingko biloba users lower plasma Abeta42 levels. |
| 3464 | 15929864 | Aggregation of the beta-cell product islet amyloid polypeptide (IAPP) is believed to be an important event in the development of the beta-cell lesion in type 2 diabetes. |
| 3465 | 15938041 | In 74 patients with type 2 diabetes (23 normoalbuminuric, 30 microalbuminuric, and 21 proteinuric) fibrinogen, serum amyloid A protein (SAA), C-reactive protein (CRP), and IL-6 were determined. |
| 3466 | 15938041 | CRP, fibrinogen, SAA, and IL-6 differed among groups, with proteinuric patients having the highest levels. |
| 3467 | 15938041 | In patients with increased GBM width (> 396 nm), CRP, SAA, and IL-6 were higher than in patients with normal GBM width (P < 0.003, P < 0.004, and P < 0.0004, respectively). |
| 3468 | 15939073 | Urinary 15-keto-dihydro-PGF(2alpha) (a major metabolite of PGF(2alpha)), serum interleukin-6 (IL-6) and high sensitivity C-reactive protein (hsCRP), serum amyloid protein A (SAA), urinary 8-iso-PGF(2alpha) (an F(2)-isoprostane, indicator of oxidative stress), and serum alpha-tocopherol were quantified in a population-based sample (n = 642) of 77-year old men without diabetes. |
| 3469 | 15975085 | Why diabetes would increase the likelihood of Alzheimer's disease is not immediately clear, although recent studies have demonstrated an impact of insulin abnormalities, insulin resistance and advanced glycation end products on both the development of neural amyloid plaques and neurofibrillary tangles. |
| 3470 | 15983213 | The amyloid present in the islets of Langerhans in type 2 diabetes is polymerized islet amyloid polypeptide (IAPP). |
| 3471 | 15983213 | This step is performed by the prohormone convertases PC2 and PC1/3. |
| 3472 | 15983213 | PC2 processes proIAPP preferably at the NH2-terminal processing site, and PC1/3 processes proIAPP exclusively at the COOH-terminal site. |
| 3473 | 15983213 | Additionally, h-proIAPP was transfected into three different pituitary-derived cell lines with different prohormone convertase profiles: AtT-20 cells (deficient in PC2), GH3 cells (deficient in PC1/3), and GH4C1 cells (deficient in both convertases). |
| 3474 | 15983227 | Long-term treatment with rosiglitazone and metformin reduces the extent of, but does not prevent, islet amyloid deposition in mice expressing the gene for human islet amyloid polypeptide. |
| 3475 | 15983227 | Rosiglitazone and metformin act by different mechanisms to improve insulin sensitivity and thereby reduce beta-cell secretory demand, resulting in decreased release of insulin and islet amyloid polypeptide (IAPP), the unique constituent of islet amyloid deposits. |
| 3476 | 15983227 | At the end of the study, islet amyloid prevalence (percent islets containing amyloid) and severity (percent islet area occupied by amyloid), islet mass, beta-cell mass, and insulin release were determined. |
| 3477 | 15983227 | Long-term treatment with rosiglitazone and metformin reduces the extent of, but does not prevent, islet amyloid deposition in mice expressing the gene for human islet amyloid polypeptide. |
| 3478 | 15983227 | Rosiglitazone and metformin act by different mechanisms to improve insulin sensitivity and thereby reduce beta-cell secretory demand, resulting in decreased release of insulin and islet amyloid polypeptide (IAPP), the unique constituent of islet amyloid deposits. |
| 3479 | 15983227 | At the end of the study, islet amyloid prevalence (percent islets containing amyloid) and severity (percent islet area occupied by amyloid), islet mass, beta-cell mass, and insulin release were determined. |
| 3480 | 15983227 | Long-term treatment with rosiglitazone and metformin reduces the extent of, but does not prevent, islet amyloid deposition in mice expressing the gene for human islet amyloid polypeptide. |
| 3481 | 15983227 | Rosiglitazone and metformin act by different mechanisms to improve insulin sensitivity and thereby reduce beta-cell secretory demand, resulting in decreased release of insulin and islet amyloid polypeptide (IAPP), the unique constituent of islet amyloid deposits. |
| 3482 | 15983227 | At the end of the study, islet amyloid prevalence (percent islets containing amyloid) and severity (percent islet area occupied by amyloid), islet mass, beta-cell mass, and insulin release were determined. |
| 3483 | 16006679 | Type 2 diabetes mellitus can be defined as a conformational disease because a constituent beta cell protein, islet amyloid polypeptide, undergoes a change in tertiary structure followed by self-association and tissue deposition. |
| 3484 | 16006679 | As the cell's quality control system becomes overwhelmed, conformational changes occur to islet amyloid polypeptide intermediates, generating stable oligomers with an anti-parallel crossed beta-pleated sheet structure that eventually accumulate as space-occupying lesions within the islets. |
| 3485 | 16006679 | Type 2 diabetes mellitus can be defined as a conformational disease because a constituent beta cell protein, islet amyloid polypeptide, undergoes a change in tertiary structure followed by self-association and tissue deposition. |
| 3486 | 16006679 | As the cell's quality control system becomes overwhelmed, conformational changes occur to islet amyloid polypeptide intermediates, generating stable oligomers with an anti-parallel crossed beta-pleated sheet structure that eventually accumulate as space-occupying lesions within the islets. |
| 3487 | 16018852 | Relation of left ventricular concentric remodeling to levels of C-reactive protein and serum amyloid A in patients with essential hypertension. |
| 3488 | 16018852 | In this study, we investigated possible relations between left ventricular (LV) concentric remodeling and plasma levels of high-sensitivity C-reactive protein (hs-CRP) and serum amyloid-A (SAA) in subjects who had essential hypertension; 65 consecutive subjects who had hypertension, did not have diabetes, and had normal LV mass were categorized as those whose LV relative wall thickness was <0.44 (n = 41) and those whose relative wall thickness was > or =0.44. |
| 3489 | 16018852 | In conclusion, alterations in LV geometry are associated with increased serum CRP and SAA levels in patients who are newly diagnosed with essential hypertension. |
| 3490 | 16026359 | There is also evidence for a link between pro-inflammatory cytokines and impairment of insulin-signalling pathways in the beta-cell, and the potential role of islet amyloid deposition in beta-cell deterioration continues to be a subject for debate. |
| 3491 | 16036356 | This study investigated the longitudinal association between serum selenium (s-Se) and a golden standard indicator of oxidative stress in vivo (8-iso-prostaglandin F2alpha, a major F2-isoprostane), an indicator of cyclooxygenase (COX)-mediated inflammation (prostaglandin F2alpha), high sensitive C-reactive protein (hsCRP), interleukin-6 (IL-6) and serum amyloid A protein (SAA) in a follow-up study of 27 years. |
| 3492 | 16036356 | The status of oxidative stress and inflammation was evaluated in a re-investigation 27 years later by quantification of urinary 8-iso-PGF2alpha and 15-keto-dihydro-PGF2alpha (a major metabolite of PGF2alpha) and serum hsCRP, SAA and IL-6. |
| 3493 | 16036356 | The s-Se was not associated with hsCRP, SAA or IL-6 at follow-up. |
| 3494 | 16039527 | The pathogenesis of type II diabetes is associated with the aggregation of the 37-residue human islet amyloid polypeptide (hIAPP) into cytotoxic beta sheet aggregates and fibrils. |
| 3495 | 16060675 | Parallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p. |
| 3496 | 16060675 | We report the results of solid-state nuclear magnetic resonance (NMR) and atomic force microscopy measurements on amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p (Ure2p(10)(-)(39)). |
| 3497 | 16060675 | Parallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p. |
| 3498 | 16060675 | We report the results of solid-state nuclear magnetic resonance (NMR) and atomic force microscopy measurements on amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p (Ure2p(10)(-)(39)). |
| 3499 | 16142909 | Lipid membranes modulate the structure of islet amyloid polypeptide. |
| 3500 | 16142909 | The 37-residue islet amyloid polypeptide (IAPP) is thought to play an important role in the pathogenesis of type II diabetes. |
| 3501 | 16142909 | Lipid membranes modulate the structure of islet amyloid polypeptide. |
| 3502 | 16142909 | The 37-residue islet amyloid polypeptide (IAPP) is thought to play an important role in the pathogenesis of type II diabetes. |
| 3503 | 16149573 | [Islet amyloid polypeptide (IAPP)]. |
| 3504 | 16156481 | Statins inhibit enzymes involved in the endogenous synthesis of cholesterol and evidence is mounting that they also affect enzymes in Abeta metabolism i.e. beta-secretase. |
| 3505 | 16156481 | This normalises the breakdown of the precursor of Abeta, amyloid precursor protein, thereby promoting the nonamyloidogenic pathway. |
| 3506 | 16186174 | Connective tissue growth factor (CTGF) expression in the brain is a downstream effector of insulin resistance- associated promotion of Alzheimer's disease beta-amyloid neuropathology. |
| 3507 | 16186174 | With this evidence we continued to explore the regulation of CTGF in postmortem AD brain tissue and found that CTGF expression correlated with the progression of AD clinical dementia and amyloid neuritic plaque (NP) neuropathology, but not neurofibrillary tangle (NFT) deposition. |
| 3508 | 16186174 | Consistent with this evidence, we also found that exposure of Tg2576 mice (a model AD-type amyloid neuropathology) to a diabetogenic diet that promotes IR results in a ~2-fold elevation in CTGF steady-state levels in the brain, coincident with a commensurate promotion of AD-type amyloid plaque burden. |
| 3509 | 16186174 | Finally, using in vitro cellular models of amyloid precursor protein (APP)-processing and Abeta generation/clearance, we confirmed that human recombinant (hr)CTGF may increase Abeta1-40 and Abeta1-42 peptide steady-state levels, possibly through a mechanism that involves gamma-secretase activation and decreased insulin-degrading enzyme (IDE) steady-state levels in a MAP kinase (MAPK)/ phosphatidylinositol 3-kinase (PI-3K)/protein kinase-B (AKT)1-dependent manner. |
| 3510 | 16186174 | Connective tissue growth factor (CTGF) expression in the brain is a downstream effector of insulin resistance- associated promotion of Alzheimer's disease beta-amyloid neuropathology. |
| 3511 | 16186174 | With this evidence we continued to explore the regulation of CTGF in postmortem AD brain tissue and found that CTGF expression correlated with the progression of AD clinical dementia and amyloid neuritic plaque (NP) neuropathology, but not neurofibrillary tangle (NFT) deposition. |
| 3512 | 16186174 | Consistent with this evidence, we also found that exposure of Tg2576 mice (a model AD-type amyloid neuropathology) to a diabetogenic diet that promotes IR results in a ~2-fold elevation in CTGF steady-state levels in the brain, coincident with a commensurate promotion of AD-type amyloid plaque burden. |
| 3513 | 16186174 | Finally, using in vitro cellular models of amyloid precursor protein (APP)-processing and Abeta generation/clearance, we confirmed that human recombinant (hr)CTGF may increase Abeta1-40 and Abeta1-42 peptide steady-state levels, possibly through a mechanism that involves gamma-secretase activation and decreased insulin-degrading enzyme (IDE) steady-state levels in a MAP kinase (MAPK)/ phosphatidylinositol 3-kinase (PI-3K)/protein kinase-B (AKT)1-dependent manner. |
| 3514 | 16186174 | Connective tissue growth factor (CTGF) expression in the brain is a downstream effector of insulin resistance- associated promotion of Alzheimer's disease beta-amyloid neuropathology. |
| 3515 | 16186174 | With this evidence we continued to explore the regulation of CTGF in postmortem AD brain tissue and found that CTGF expression correlated with the progression of AD clinical dementia and amyloid neuritic plaque (NP) neuropathology, but not neurofibrillary tangle (NFT) deposition. |
| 3516 | 16186174 | Consistent with this evidence, we also found that exposure of Tg2576 mice (a model AD-type amyloid neuropathology) to a diabetogenic diet that promotes IR results in a ~2-fold elevation in CTGF steady-state levels in the brain, coincident with a commensurate promotion of AD-type amyloid plaque burden. |
| 3517 | 16186174 | Finally, using in vitro cellular models of amyloid precursor protein (APP)-processing and Abeta generation/clearance, we confirmed that human recombinant (hr)CTGF may increase Abeta1-40 and Abeta1-42 peptide steady-state levels, possibly through a mechanism that involves gamma-secretase activation and decreased insulin-degrading enzyme (IDE) steady-state levels in a MAP kinase (MAPK)/ phosphatidylinositol 3-kinase (PI-3K)/protein kinase-B (AKT)1-dependent manner. |
| 3518 | 16191216 | In addition, amyloid beta protein appears directly involved in the degeneration of both the larger perforating arterial vessels as well as cerebral capillaries, which represent the blood-brain barrier. |
| 3519 | 16198619 | Peroxisome proliferator-activated receptor-gamma (PPARgamma) is a nuclear transcription factor that comprises the primary molecular target for thiazolidinedione (TZD) insulin-sensitizing drugs. |
| 3520 | 16198619 | Thus, TZDs have been shown to reduce plasma levels of the chemokine, monocyte chemotactic protein-1 (MCP-1), the anti-fibrinolytic protein, plasminogen activator inhibitor-1 (PAI-1), the endothelial cell adhesion molecules, e-selectin and inter-cellular adhesion molecule-1 (ICAM-1), the leucocyte-activating molecule, CD40L, and the tissue-remodeling enzyme, matrix metalloproteinase-9 (MMP-9). |
| 3521 | 16198619 | Further tangible evidence of a reduction by TZDs of systemic inflammation in patients with the classical metabolic syndrome stems from falls in the white blood cell count, P-selectin-positive platelets and in the acute-phase inflammatory proteins, C-reactive protein, serum amyloid A and fibrinogen. |
| 3522 | 16198619 | Here, these drugs improve insulin sensitivity for glucose metabolism, reduce hyperinsulinemia, hepatic steatosis, inflammation and fibrosis, and lower the circulating levels of liver transaminases (ALT, AST), alkaline phosphatase and gamma glutamyl transferase. |
| 3523 | 16204373 | Activation of peroxisome proliferator-activated receptor-gamma by rosiglitazone protects human islet cells against human islet amyloid polypeptide toxicity by a phosphatidylinositol 3'-kinase-dependent pathway. |
| 3524 | 16225463 | White adipose tissue is secreting several hormones, particularly leptin and adiponectin, and a variety of other protein signals: the adipocytokines. |
| 3525 | 16225463 | A growing list of adipocytokines involved in inflammation (IL-1beta, IL-6, IL-8, IL-10, TNF-alpha, TGF-beta,) and the acute-phase response (serum amyloid A, PAI-1) have been found to be increased in the metabolic syndrome. |
| 3526 | 16246041 | Increased risk of Alzheimer's disease in Type II diabetes: insulin resistance of the brain or insulin-induced amyloid pathology? |
| 3527 | 16246041 | Insulin also regulates the metabolism of beta-amyloid and tau, the building blocks of amyloid plaques and neurofibrillary tangles, the neuropathological hallmarks of Alzheimer's disease. |
| 3528 | 16246041 | Increased risk of Alzheimer's disease in Type II diabetes: insulin resistance of the brain or insulin-induced amyloid pathology? |
| 3529 | 16246041 | Insulin also regulates the metabolism of beta-amyloid and tau, the building blocks of amyloid plaques and neurofibrillary tangles, the neuropathological hallmarks of Alzheimer's disease. |
| 3530 | 16303136 | Islet amyloid polypeptide (IAPP; amylin) is responsible for amyloid formation in type-2 diabetes. |
| 3531 | 16331989 | The role of His-18 in amyloid formation by human islet amyloid polypeptide. |
| 3532 | 16331989 | The 37-residue islet amyloid polypeptide (IAPP) is the major protein component of the amyloid deposits found in type-II diabetes. |
| 3533 | 16331989 | The role of His-18 in amyloid formation by human islet amyloid polypeptide. |
| 3534 | 16331989 | The 37-residue islet amyloid polypeptide (IAPP) is the major protein component of the amyloid deposits found in type-II diabetes. |
| 3535 | 16332384 | The predominating theory on the pathophysiology of Alzheimer's disease (AD) concerns the mis-metabolism of amyloid precursor protein (APP). |
| 3536 | 16332384 | Statins may not only inhibit enzymes involved in the endogenous synthesis of cholesterol but also affect enzymes involved in Abeta metabolism, i.e., alpha-secretase and beta-secretase. |
| 3537 | 16340082 | Plasma levels of insulin and amyloid beta 42 are correlated in patients with amnestic Mild Cognitive Impairment. |
| 3538 | 16340082 | Epidemiological and experimental data suggest that type 2 diabetes (DM2) and sporadic late-onset Alzheimer's disease (AD) share a common mechanism, that is able to produce accumulation of insulin and amyloid beta 42 (Abeta42), the major pathogenic events respectively of the two conditions. |
| 3539 | 16340082 | Plasma levels of insulin and amyloid beta 42 are correlated in patients with amnestic Mild Cognitive Impairment. |
| 3540 | 16340082 | Epidemiological and experimental data suggest that type 2 diabetes (DM2) and sporadic late-onset Alzheimer's disease (AD) share a common mechanism, that is able to produce accumulation of insulin and amyloid beta 42 (Abeta42), the major pathogenic events respectively of the two conditions. |
| 3541 | 16340083 | Insulin and insulin-like growth factor expression and function deteriorate with progression of Alzheimer's disease: link to brain reductions in acetylcholine. |
| 3542 | 16340083 | Glucose utilization and energy metabolism are regulated by insulin and insulin-like growth factor I (IGF-I), and correspondingly, studies have shown that cognitive impairment may be improved by glucose or insulin administration. |
| 3543 | 16340083 | Recently, we demonstrated significantly reduced levels of insulin and IGF-I polypeptide genes and their corresponding receptors in advanced AD relative to aged control brains. |
| 3544 | 16340083 | Realtime quantitative RT-PCR analysis of frontal lobe tissue demonstrated that increasing AD Braak Stage was associated with progressively reduced levels of mRNA corresponding to insulin, IGF-I, and IGF-II polypeptides and their receptors, tau, which is regulated by insulin and IGF-I, and the Hu D neuronal RNA binding protein. |
| 3545 | 16340083 | In contrast, progressively increased levels of amyloid beta protein precursor (AbetaPP), glial fibrillary acidic protein, and the IBA1/AIF1 microglial mRNA transcripts were detected with increasing AD Braak Stage. |
| 3546 | 16340083 | Impairments in growth factor and growth factor receptor expression and function were associated with increasing AD Braak stage dependent reductions in insulin, IGF-I, and IGF-II receptor binding, ATP levels, and choline acetyltransferase (ChAT) expression. |
| 3547 | 16340083 | Further studies demonstrated that: 1) ChAT expression increases with insulin or IGF-I stimulation; 2) ChAT is expressed in insulin and IGF-I receptor-positive cortical neurons; and 3) ChAT co-localization in insulin or IGF-I receptor-positive neurons is reduced in AD. |
| 3548 | 16361024 | The findings of mechanistic studies suggest that vascular disease and alterations in glucose, insulin, and amyloid metabolism underlie the pathophysiology, but which of these mechanisms are clinically relevant is unclear. |
| 3549 | 16403520 | Islet amyloid polypeptide inserts into phospholipid monolayers as monomer. |
| 3550 | 16403520 | It is hypothesized that beta-cell death is related to interaction of the 37 amino acid residue human islet amyloid polypeptide (hIAPP), the major constituent of islet amyloid, with cellular membranes. |
| 3551 | 16403520 | Islet amyloid polypeptide inserts into phospholipid monolayers as monomer. |
| 3552 | 16403520 | It is hypothesized that beta-cell death is related to interaction of the 37 amino acid residue human islet amyloid polypeptide (hIAPP), the major constituent of islet amyloid, with cellular membranes. |
| 3553 | 16415763 | Several abnormalities in islet beta-cell and insulin secretion were also pointed out in elderly people such as increased amyloid deposition and decreased amylin secretion, impaired insulin secretion pulsatility, decreased insulin sensitivity of pancreatic beta-cells to insulinotropic gut hormones and diminished insulin response to non-glucose stimuli such as arginine. |
| 3554 | 16467158 | Design of a mimic of nonamyloidogenic and bioactive human islet amyloid polypeptide (IAPP) as nanomolar affinity inhibitor of IAPP cytotoxic fibrillogenesis. |
| 3555 | 16467158 | Aggregation of human islet amyloid polypeptide (IAPP) into pancreatic amyloid is strongly associated with the pathogenesis of type II diabetes. |
| 3556 | 16467158 | Design of a mimic of nonamyloidogenic and bioactive human islet amyloid polypeptide (IAPP) as nanomolar affinity inhibitor of IAPP cytotoxic fibrillogenesis. |
| 3557 | 16467158 | Aggregation of human islet amyloid polypeptide (IAPP) into pancreatic amyloid is strongly associated with the pathogenesis of type II diabetes. |
| 3558 | 16505860 | Formation of small, dense HDL particles with attenuated antiatherogenic activity can be mechanistically related to HDL enrichment in triglycerides and in serum amyloid A, depletion of cholesteryl esters, covalent modification of HDL apolipoproteins and attenuated antiatherogenic function of apolipoprotein AI. |
| 3559 | 16510295 | The receptor for advanced glycation endproducts (RAGE) is a multiligand receptor that binds a variety of structurally and functionally unrelated ligands, including advanced glycation endproducts (AGEs), amyloid fibrils, amphoterin, and members of the S100 family of proteins. |
| 3560 | 16565054 | We report investigations of the morphology and molecular structure of amyloid fibrils comprised of residues 10-40 of the Alzheimer's beta-amyloid peptide (Abeta(10-40)), prepared under various solution conditions and degrees of agitation. |
| 3561 | 16565054 | Omission of residues 1-9 from the full-length Alzheimer's beta-amyloid peptide (Abeta(1-40)) did not prevent the peptide from forming amyloid fibrils or eliminate fibril polymorphism. |
| 3562 | 16565054 | We report investigations of the morphology and molecular structure of amyloid fibrils comprised of residues 10-40 of the Alzheimer's beta-amyloid peptide (Abeta(10-40)), prepared under various solution conditions and degrees of agitation. |
| 3563 | 16565054 | Omission of residues 1-9 from the full-length Alzheimer's beta-amyloid peptide (Abeta(1-40)) did not prevent the peptide from forming amyloid fibrils or eliminate fibril polymorphism. |
| 3564 | 16570161 | Intracellular amyloid-like deposits contain unprocessed pro-islet amyloid polypeptide (proIAPP) in beta cells of transgenic mice overexpressing the gene for human IAPP and transplanted human islets. |
| 3565 | 16574064 | The C-terminal domain of human insulin degrading enzyme is required for dimerization and substrate recognition. |
| 3566 | 16574064 | Insulin degrading enzyme (IDE), a zinc metalloprotease, can specifically recognize and degrade insulin, as well as several amyloidogenic peptides such as amyloid beta (Abeta) and amylin. |
| 3567 | 16574064 | The disruption of IDE function in rodents leads to glucose intolerance and cerebral Abeta accumulation, hallmarks of type 2 diabetes and Alzheimer's disease, respectively. |
| 3568 | 16574064 | Fluorescence polarization assays using labeled insulin reveal that IDE-N has reduced affinity to insulin relative to wild type IDE. |
| 3569 | 16627931 | More recently, studies with human postmortem brain tissue linked many of the characteristic molecular and pathological features of AD to reduced expression of the insulin and insulin-like growth factor (IGF) genes and their corresponding receptors. |
| 3570 | 16627931 | The ic-STZ-injected rats did not have elevated blood glucose levels, and pancreatic architecture and insulin immunoreactivity were similar to control, yet their brains were reduced in size and exhibited neurodegeneration associated with cell loss, gliosis, and increased immunoreactivity for p53, active glycogen synthase kinase 3beta, phospho-tau, ubiquitin, and amyloid-beta. |
| 3571 | 16627931 | Real time quantitative RT-PCR studies demonstrated that the ic-STZ-treated brains had significantly reduced expression of genes corresponding to neurons, oligodendroglia, and choline acetyltransferase, and increased expression of genes encoding glial fibrillary acidic protein, microglia-specific proteins, acetylcholinesterase, tau, and amyloid precursor protein. |
| 3572 | 16627931 | These abnormalities were associated reduced expression of genes encoding insulin, IGF-II, insulin receptor, IGF-I receptor, and insulin receptor substrate-1, and reduced ligand binding to the insulin and IGF-II receptors. |
| 3573 | 16754744 | Two of these genes were serum amyloid A (SAA) and transmembrane 4 L six family member 1 (TM4SF1). |
| 3574 | 16754744 | Real-time RT-PCR analysis of SAA and TM4SF1 expression in adipocytes from seven subjects revealed 19-fold and 22-fold higher expression in the large cells, respectively, and a correlation between adipocyte size and both SAA and TM4SF1 expression. |
| 3575 | 16754744 | In comparison with 17 other human tissues and cell types by microarray, large adipocytes displayed by far the highest SAA and TM4SF1 expression. |
| 3576 | 16772049 | Solid-state nuclear magnetic resonance (NMR) measurements have made major contributions to our understanding of the molecular structures of amyloid fibrils, including fibrils formed by the beta-amyloid peptide associated with Alzheimer's disease, by proteins associated with fungal prions, and by a variety of other polypeptides. |
| 3577 | 16774767 | Insulin is a small, predominantly alpha-helical protein consisting of 51 residues in two disulfide-linked polypeptide chains that readily assembles into amyloid fibrils under conditions of low pH and elevated temperature. |
| 3578 | 16774767 | We demonstrate here that both the A-chain and the B-chain of insulin are capable of forming amyloid fibrils in isolation under similar conditions, with fibrillar morphologies that differ from those composed of intact insulin. |
| 3579 | 16774767 | Insulin is a small, predominantly alpha-helical protein consisting of 51 residues in two disulfide-linked polypeptide chains that readily assembles into amyloid fibrils under conditions of low pH and elevated temperature. |
| 3580 | 16774767 | We demonstrate here that both the A-chain and the B-chain of insulin are capable of forming amyloid fibrils in isolation under similar conditions, with fibrillar morphologies that differ from those composed of intact insulin. |
| 3581 | 16786033 | ApoE has roles in cholesterol metabolism and Abeta clearance, both of which are thought to be significant in AD pathogenesis. |
| 3582 | 16786033 | A diversity of topics is covered, including cholesterol metabolism, glucose regulation, diabetes, insulin, ApoE function, amyloid precursor protein metabolism, and in particular their relevance to AD. |
| 3583 | 16787929 | In this study, we explored whether proteases capable of degrading soluble Abeta (sAbeta) could degrade fAbeta as well. |
| 3584 | 16787929 | Only MMP-9 digests contained fragments (Abeta(1-20) and Abeta(1-30)) from fAbeta(1-42) substrate; the corresponding cleavage sites are thought to be important for beta-pleated sheet formation. |
| 3585 | 16787929 | To determine whether MMP-9 can degrade plaques formed in vivo, fresh brain slices from aged APP/PS1 mice were incubated with proteases. |
| 3586 | 16787929 | Consistent with a role for endogenous MMP-9 in this process in vivo, MMP-9 immunoreactivity was detected in astrocytes surrounding amyloid plaques in the brains of aged APP/PS1 and APPsw mice, and increased MMP activity was selectively observed in compact ThS-positive plaques. |
| 3587 | 16788249 | Two of the serum biomarkers matched with islet amyloid polypeptide and resistin in the SWISS-PROT knowledgebase. |
| 3588 | 16804082 | Beta-cell deficit due to increased apoptosis in the human islet amyloid polypeptide transgenic (HIP) rat recapitulates the metabolic defects present in type 2 diabetes. |
| 3589 | 16804082 | The islet anatomy in IFG and type 2 diabetes reveals an approximately 50 and 65% deficit in beta-cell mass, with increased beta-cell apoptosis and islet amyloid derived from islet amyloid polypeptide (IAPP). |
| 3590 | 16804082 | Beta-cell deficit due to increased apoptosis in the human islet amyloid polypeptide transgenic (HIP) rat recapitulates the metabolic defects present in type 2 diabetes. |
| 3591 | 16804082 | The islet anatomy in IFG and type 2 diabetes reveals an approximately 50 and 65% deficit in beta-cell mass, with increased beta-cell apoptosis and islet amyloid derived from islet amyloid polypeptide (IAPP). |
| 3592 | 16804197 | Islet amyloid polypeptide (IAPP) transgenic rodents as models for type 2 diabetes. |
| 3593 | 16804197 | The islet in type 2 diabetes mellitus (T2D) has deficient beta-cell mass due to increased beta-cell apoptosis and islet amyloid derived from islet amyloid polypeptide (IAPP). |
| 3594 | 16804197 | Islet amyloid polypeptide (IAPP) transgenic rodents as models for type 2 diabetes. |
| 3595 | 16804197 | The islet in type 2 diabetes mellitus (T2D) has deficient beta-cell mass due to increased beta-cell apoptosis and islet amyloid derived from islet amyloid polypeptide (IAPP). |
| 3596 | 16804198 | These features include age of onset of FDM in middle age, association with obesity, residual but declining insulin secretion, development of islet amyloid deposits, loss of approximately 50% of beta-cell mass, and development of complications in several organ systems including peripheral polyneuropathy and retinopathy. |
| 3597 | 16804200 | Initially there is hyperplasia of the islets with abundant insulin production typically followed by replacement of islets with islet-associated amyloid. |
| 3598 | 16823976 | Multiplexed affinity retrieval devices and methodology were developed to simultaneously target retinol binding protein, C-reactive protein, serum amyloid P component, as well as an added exogenous internal reference standard (staphylococcal enterotoxin B) for subsequent MALDI-TOF MS analysis. |
| 3599 | 16823976 | This approach allows for semiquantitative analysis of both retinol binding protein and serum amyloid P component while performing absolute quantitative measurements of C-reactive protein. |
| 3600 | 16823976 | Multiplexed affinity retrieval devices and methodology were developed to simultaneously target retinol binding protein, C-reactive protein, serum amyloid P component, as well as an added exogenous internal reference standard (staphylococcal enterotoxin B) for subsequent MALDI-TOF MS analysis. |
| 3601 | 16823976 | This approach allows for semiquantitative analysis of both retinol binding protein and serum amyloid P component while performing absolute quantitative measurements of C-reactive protein. |
| 3602 | 16842191 | The receptor for advanced glycation end products (RAGE) is a cell-bound receptor of the immunoglobulin superfamily which may be activated by a variety of proinflammatory ligands including advanced glycoxidation end products, S100/calgranulins, high mobility group box 1, and amyloid beta-peptide. |
| 3603 | 16849627 | Type 2 diabetes mellitus (T2DM) is characterized by an approximately 60% deficit in beta-cell mass, increased beta-cell apoptosis, and islet amyloid derived from islet amyloid polypeptide (IAPP). |
| 3604 | 16866369 | Characterization of the heparin binding site in the N-terminus of human pro-islet amyloid polypeptide: implications for amyloid formation. |
| 3605 | 16866369 | Islet amyloid polypeptide (IAPP), also referred to as amylin, aggregates in the islet extracellular space to form amyloid deposits in up to 95% of patients with the disease. |
| 3606 | 16866369 | IAPP is stored with insulin in beta-islet cells and is processed in parallel by subtilisin-like prohormone convertases prior to secretion. |
| 3607 | 16866369 | Immunohistochemical studies implicate the presence of the heparan sulfate proteoglycan (HSPG) perlecan in islet amyloid deposits, suggesting a role for HSPGs in mediating amyloid deposition in type 2 diabetes and implicating a binding domain in the N-terminus of proIAPP. |
| 3608 | 16866369 | Characterization of the heparin binding site in the N-terminus of human pro-islet amyloid polypeptide: implications for amyloid formation. |
| 3609 | 16866369 | Islet amyloid polypeptide (IAPP), also referred to as amylin, aggregates in the islet extracellular space to form amyloid deposits in up to 95% of patients with the disease. |
| 3610 | 16866369 | IAPP is stored with insulin in beta-islet cells and is processed in parallel by subtilisin-like prohormone convertases prior to secretion. |
| 3611 | 16866369 | Immunohistochemical studies implicate the presence of the heparan sulfate proteoglycan (HSPG) perlecan in islet amyloid deposits, suggesting a role for HSPGs in mediating amyloid deposition in type 2 diabetes and implicating a binding domain in the N-terminus of proIAPP. |
| 3612 | 16866369 | Characterization of the heparin binding site in the N-terminus of human pro-islet amyloid polypeptide: implications for amyloid formation. |
| 3613 | 16866369 | Islet amyloid polypeptide (IAPP), also referred to as amylin, aggregates in the islet extracellular space to form amyloid deposits in up to 95% of patients with the disease. |
| 3614 | 16866369 | IAPP is stored with insulin in beta-islet cells and is processed in parallel by subtilisin-like prohormone convertases prior to secretion. |
| 3615 | 16866369 | Immunohistochemical studies implicate the presence of the heparan sulfate proteoglycan (HSPG) perlecan in islet amyloid deposits, suggesting a role for HSPGs in mediating amyloid deposition in type 2 diabetes and implicating a binding domain in the N-terminus of proIAPP. |
| 3616 | 16873681 | Impaired NH2-terminal processing of human proislet amyloid polypeptide by the prohormone convertase PC2 leads to amyloid formation and cell death. |
| 3617 | 16873681 | Islet amyloid, formed by aggregation of islet amyloid polypeptide (IAPP; amylin), is a pathological characteristic of the pancreas in type 2 diabetes and may contribute to the progressive loss of beta-cells in this disease. |
| 3618 | 16873681 | GH3 cells lacking the prohormone convertase 1/3 (PC1/3) and IAPP and with very low levels of prohormone convertase 2 (PC2) were transduced with adenovirus (Ad) expressing human or rat (control) proIAPP linked to green fluorescent protein, with or without Ad-PC2 or Ad-PC1/3. |
| 3619 | 16873681 | COOH-terminal processing of human proIAPP by PC1/3 increased (hIAPP+PC1/3 10.4 +/- 0.7%; P < 0.05), whereas NH(2)-terminal processing of proIAPP by addition of PC2 markedly decreased (hIAPP+PC2 5.5 +/- 0.5%; P < 0.05) the number of apoptotic GH3 cells. |
| 3620 | 16873681 | Islets from mice lacking PC2 and with beta-cell expression of human proIAPP (hIAPP(+/+)/PC2(-/-)) developed amyloid associated with beta-cell death during 2-week culture. |
| 3621 | 16873681 | Rescue of PC2 expression by ex vivo transduction with Ad-PC2 restored NH(2)-terminal processing to mature IAPP and decreased both the extent of amyloid formation and the number of TUNEL-positive cells (-PC2 26.5 +/- 4.1% vs. |
| 3622 | 16873681 | Impaired NH2-terminal processing of human proislet amyloid polypeptide by the prohormone convertase PC2 leads to amyloid formation and cell death. |
| 3623 | 16873681 | Islet amyloid, formed by aggregation of islet amyloid polypeptide (IAPP; amylin), is a pathological characteristic of the pancreas in type 2 diabetes and may contribute to the progressive loss of beta-cells in this disease. |
| 3624 | 16873681 | GH3 cells lacking the prohormone convertase 1/3 (PC1/3) and IAPP and with very low levels of prohormone convertase 2 (PC2) were transduced with adenovirus (Ad) expressing human or rat (control) proIAPP linked to green fluorescent protein, with or without Ad-PC2 or Ad-PC1/3. |
| 3625 | 16873681 | COOH-terminal processing of human proIAPP by PC1/3 increased (hIAPP+PC1/3 10.4 +/- 0.7%; P < 0.05), whereas NH(2)-terminal processing of proIAPP by addition of PC2 markedly decreased (hIAPP+PC2 5.5 +/- 0.5%; P < 0.05) the number of apoptotic GH3 cells. |
| 3626 | 16873681 | Islets from mice lacking PC2 and with beta-cell expression of human proIAPP (hIAPP(+/+)/PC2(-/-)) developed amyloid associated with beta-cell death during 2-week culture. |
| 3627 | 16873681 | Rescue of PC2 expression by ex vivo transduction with Ad-PC2 restored NH(2)-terminal processing to mature IAPP and decreased both the extent of amyloid formation and the number of TUNEL-positive cells (-PC2 26.5 +/- 4.1% vs. |
| 3628 | 16873681 | Impaired NH2-terminal processing of human proislet amyloid polypeptide by the prohormone convertase PC2 leads to amyloid formation and cell death. |
| 3629 | 16873681 | Islet amyloid, formed by aggregation of islet amyloid polypeptide (IAPP; amylin), is a pathological characteristic of the pancreas in type 2 diabetes and may contribute to the progressive loss of beta-cells in this disease. |
| 3630 | 16873681 | GH3 cells lacking the prohormone convertase 1/3 (PC1/3) and IAPP and with very low levels of prohormone convertase 2 (PC2) were transduced with adenovirus (Ad) expressing human or rat (control) proIAPP linked to green fluorescent protein, with or without Ad-PC2 or Ad-PC1/3. |
| 3631 | 16873681 | COOH-terminal processing of human proIAPP by PC1/3 increased (hIAPP+PC1/3 10.4 +/- 0.7%; P < 0.05), whereas NH(2)-terminal processing of proIAPP by addition of PC2 markedly decreased (hIAPP+PC2 5.5 +/- 0.5%; P < 0.05) the number of apoptotic GH3 cells. |
| 3632 | 16873681 | Islets from mice lacking PC2 and with beta-cell expression of human proIAPP (hIAPP(+/+)/PC2(-/-)) developed amyloid associated with beta-cell death during 2-week culture. |
| 3633 | 16873681 | Rescue of PC2 expression by ex vivo transduction with Ad-PC2 restored NH(2)-terminal processing to mature IAPP and decreased both the extent of amyloid formation and the number of TUNEL-positive cells (-PC2 26.5 +/- 4.1% vs. |
| 3634 | 16873681 | Impaired NH2-terminal processing of human proislet amyloid polypeptide by the prohormone convertase PC2 leads to amyloid formation and cell death. |
| 3635 | 16873681 | Islet amyloid, formed by aggregation of islet amyloid polypeptide (IAPP; amylin), is a pathological characteristic of the pancreas in type 2 diabetes and may contribute to the progressive loss of beta-cells in this disease. |
| 3636 | 16873681 | GH3 cells lacking the prohormone convertase 1/3 (PC1/3) and IAPP and with very low levels of prohormone convertase 2 (PC2) were transduced with adenovirus (Ad) expressing human or rat (control) proIAPP linked to green fluorescent protein, with or without Ad-PC2 or Ad-PC1/3. |
| 3637 | 16873681 | COOH-terminal processing of human proIAPP by PC1/3 increased (hIAPP+PC1/3 10.4 +/- 0.7%; P < 0.05), whereas NH(2)-terminal processing of proIAPP by addition of PC2 markedly decreased (hIAPP+PC2 5.5 +/- 0.5%; P < 0.05) the number of apoptotic GH3 cells. |
| 3638 | 16873681 | Islets from mice lacking PC2 and with beta-cell expression of human proIAPP (hIAPP(+/+)/PC2(-/-)) developed amyloid associated with beta-cell death during 2-week culture. |
| 3639 | 16873681 | Rescue of PC2 expression by ex vivo transduction with Ad-PC2 restored NH(2)-terminal processing to mature IAPP and decreased both the extent of amyloid formation and the number of TUNEL-positive cells (-PC2 26.5 +/- 4.1% vs. |
| 3640 | 16873699 | Immunological parameters at baseline included high-sensitivity C-reactive protein (CRP), serum amyloid A, interleukin-6, regulated on activation normal T-cell expressed and secreted (RANTES), macrophage migration inhibitory factor (MIF), and soluble intercellular adhesion molecule. |
| 3641 | 16873699 | In the intervention group, progression to type 2 diabetes was significantly higher in subjects with the highest RANTES concentrations and was lower in subjects with the highest MIF levels. |
| 3642 | 16873699 | Ratios of RANTES to MIF in the upper tertile were highly predictive of incident type 2 diabetes in the intervention group (P = 0.006), whereas the association was less pronounced in the control group (P = 0.088). |
| 3643 | 16878984 | Conserved and cooperative assembly of membrane-bound alpha-helical states of islet amyloid polypeptide. |
| 3644 | 16878984 | In this work, we investigate these phenomena in islet amyloid polypeptide (IAPP). |
| 3645 | 16878984 | Conserved and cooperative assembly of membrane-bound alpha-helical states of islet amyloid polypeptide. |
| 3646 | 16878984 | In this work, we investigate these phenomena in islet amyloid polypeptide (IAPP). |
| 3647 | 16894402 | Insulin resistance and dysregulation of the degradation of neurotoxic amyloid and insulin appear at the core of the links between Alzheimer's disease and diabetes. |
| 3648 | 16894402 | Functions and expression of insulysin, an enzyme involved in the degradation of neurotoxic amyloid peptides and insulin, are usually impaired or reduced in Alzheimer's disease and diabetes. |
| 3649 | 16894402 | The increased occurrence of insulin resistance in Alzheimer's disease suggests that improving insulin effectiveness and insulysin activity may have therapeutic value in Alzheimer's disease patients and therefore is worth intensive investigation. |
| 3650 | 16894402 | Insulin resistance and dysregulation of the degradation of neurotoxic amyloid and insulin appear at the core of the links between Alzheimer's disease and diabetes. |
| 3651 | 16894402 | Functions and expression of insulysin, an enzyme involved in the degradation of neurotoxic amyloid peptides and insulin, are usually impaired or reduced in Alzheimer's disease and diabetes. |
| 3652 | 16894402 | The increased occurrence of insulin resistance in Alzheimer's disease suggests that improving insulin effectiveness and insulysin activity may have therapeutic value in Alzheimer's disease patients and therefore is worth intensive investigation. |
| 3653 | 16909327 | Venous blood samples were analyzed for lipid subfractions and novel cardiovascular risk factors such as lipoprotein (a), homocysteine, fibrinogen, high-sensitivity C-reactive protein (hs-CRP), and serum amyloid A (SAA) levels. |
| 3654 | 16909327 | No significant difference was found between the groups regarding family history of premature CAD, blood pressure, body mass index, lipoprotein (a), homocysteine, fibrinogen, SAA, apoprotein A-1 and B levels. |
| 3655 | 16916504 | Establishment of an in-house ELISA and the reference range for serum amyloid A (SAA): complementarity between SAA and C-reactive protein as markers of inflammation. |
| 3656 | 16920151 | Quaternary structure of a mature amyloid fibril from Alzheimer's Abeta(1-40) peptide. |
| 3657 | 16920151 | Using a range of biophysical techniques including electron microscopy we have analysed the quaternary structure of a mature amyloid fibril formed from the Abeta(1-40) peptide from Alzheimer's disease. |
| 3658 | 16920151 | Quaternary structure of a mature amyloid fibril from Alzheimer's Abeta(1-40) peptide. |
| 3659 | 16920151 | Using a range of biophysical techniques including electron microscopy we have analysed the quaternary structure of a mature amyloid fibril formed from the Abeta(1-40) peptide from Alzheimer's disease. |
| 3660 | 16930758 | Severe insulin resistance associated with subcutaneous amyloid deposition. |
| 3661 | 16930758 | It is suggested that the granulomas were the source of an insulin-degrading enzyme (IDE) which simultaneously degraded amyloidogenic precursors into localized amyloid deposits. |
| 3662 | 16930758 | Severe insulin resistance associated with subcutaneous amyloid deposition. |
| 3663 | 16930758 | It is suggested that the granulomas were the source of an insulin-degrading enzyme (IDE) which simultaneously degraded amyloidogenic precursors into localized amyloid deposits. |
| 3664 | 16935948 | Phenol red exhibits modest inhibition toward fibril formation of human Islet amyloid polypeptide (hIAPP) and its toxicity, which is associated with type II diabetes mellitus. |
| 3665 | 16950544 | Diabetes Mellitus type 2 (DM2) is a group of metabolic disorders characterized by defective insulin action or secretion or both with a 10.6% incidence in Mexican Mestizo population, DM2 is also classified within the localized misfolding diseases due to the amyloid pancreatic deposits found in 90% of the DM2 necropsies. |
| 3666 | 16950544 | The pancreatic amyloid main component is a protein known as human islet amyloid polypeptide (hIAPP) or amylin, the most common mutation is the S20G in Asian population with a polymorphic frequency in DM2 Asian patients. |
| 3667 | 16950544 | Diabetes Mellitus type 2 (DM2) is a group of metabolic disorders characterized by defective insulin action or secretion or both with a 10.6% incidence in Mexican Mestizo population, DM2 is also classified within the localized misfolding diseases due to the amyloid pancreatic deposits found in 90% of the DM2 necropsies. |
| 3668 | 16950544 | The pancreatic amyloid main component is a protein known as human islet amyloid polypeptide (hIAPP) or amylin, the most common mutation is the S20G in Asian population with a polymorphic frequency in DM2 Asian patients. |
| 3669 | 16968152 | Glucagon-like peptide-1 differentiation of primate embryonic stem cells into insulin-producing cells. |
| 3670 | 16968152 | The present study was performed to determine whether glucagon-like peptide-1 (GLP-1) stimulates differentiation of nestin-selected embryonic stem cells into insulin-producing cells. |
| 3671 | 16968152 | These cells differentiated into insulin-producing cells after addition of GLP-1. |
| 3672 | 16968152 | These nestin-positive cell-derived ICCs expressed numerous beta-cell lineage genes, including insulin; Glut-2; pancreatic duodenal homebox-1 protein (PDX-1); islet amyloid polypeptide (IAPP); neurogenin 3 (ngn3); and alpha, gamma, and delta cell gene markers. |
| 3673 | 16968152 | In addition, ICCs were characterized by coexpression of nestin/insulin and nestin/PDX-1. |
| 3674 | 16968152 | The levels of pancreas-related gene and protein expression and insulin secretion in the GLP-1 group were stronger than those in the normal controls. |
| 3675 | 16968152 | GLP-1 has been shown to be involved in stimulating the signaling pathways downstream of the transcription factor PDX-1, by increasing its protein and messenger RNA levels. |
| 3676 | 16968152 | We concluded that GLP-1 induced differentiation of nestin-positive progenitor embryonic stem cells into insulin-producing cells, which was achieved by upregulation of PDX-1 expression. |
| 3677 | 16968945 | Indeed, formation of HDL particles with attenuated antiatherogenic activity is mechanistically related to core lipid enrichment in triglycerides and cholesteryl ester depletion, altered apolipoprotein A-I (apoA-I) conformation, replacement of apoA-I by serum amyloid A, and covalent modification of HDL protein components by oxidation and glycation. |
| 3678 | 16982850 | There is a lack of agreement on the distribution of islet amyloid polypeptide (IAPP) in the pancreases of healthy and diabetic subjects. |
| 3679 | 16982850 | Therefore, a detailed morphometrical and immunohistochemical study was performed to obtain information on the distribution of cells expressing insulin, glucagon, somatostatin, pancreatic polypeptide (PP), and IAPP in the pancreases of non-diabetic (n=4) and diabetic individuals (n=6). |
| 3680 | 17010615 | Glycogen synthase kinase-3alpha (GSK-3alpha) was recently found to be an attractive target for the treatment of Alzheimer's disease due to its dual action in the formation of both amyloid plaques and neurofibrillary tangles. |
| 3681 | 17027526 | The central theme of this chapter is that human adipose tissue is a potent source of inflammatory interleukins plus other cytokines and that the majority of this release is due to the nonfat cells in the adipose tissue except for leptin and adiponectin that are primarily secreted by adipocytes. |
| 3682 | 17027526 | Human adipocytes secrete at least as much plasminogen activator inhibitor-1 (PAI-1), MCP-1, interleukin-8 (IL-8), and IL-6 in vitro as they do leptin but the nonfat cells of adipose tissue secrete even more of these proteins. |
| 3683 | 17027526 | The amount of serum amyloid A proteins 1 & 2 (SAA 1 & 2), haptoglobin, nerve growth factor (NGF), macrophage migration inhibitory factor (MIF), and PAI-1 secreted by the adipocytes derived from a gram of adipose tissue is 144%, 75%, 72%, 37%, and 23%, respectively, of that by the nonfat cells derived from the same amount of human adipose tissue. |
| 3684 | 17027526 | However, the release of IL-8, MCP-1, vascular endothelial growth factor (VEGF), TGF-beta1, IL-6, PGE(2), TNF-alpha, cathepsin S, hepatocyte growth factor (HGF), IL-1beta, IL-10, resistin, C-reactive protein (CRP), and interleukin-1 receptor antagonist (IL-1Ra) by adipocytes is less than 12% of that by the nonfat cells present in human adipose tissue. |
| 3685 | 17027526 | Obesity markedly elevates the total release of TNF-alpha, IL-6, and IL-8 by adipose tissue but only that of TNF-alpha is enhanced in adipocytes. |
| 3686 | 17027526 | Visceral adipose tissue also releases more VEGF, resistin, IL-6, PAI-1, TGF-beta1, IL-8, and IL-10 per gram of tissue than does abdominal subcutaneous adipose tissue. |
| 3687 | 17027526 | In conclusion, there is an increasing recognition that adipose tissue is an endocrine organ that secretes leptin and adiponectin along with a host of other paracrine and endocrine factors in addition to free fatty acids. |
| 3688 | 17065343 | In an effort to identify novel epitopes, we used matrix-assisted algorithms to predict peptides of glial fibrillary acidic protein (GFAP), prepro-islet amyloid polypeptide (ppIAPP), and islet-specific glucose-6-phosphatase catalytic subunit-related protein (IGRP) that likely bind to HLA-A*0201 with a strong affinity and contain a COOH-terminal proteasomal cleavage site. |
| 3689 | 17065343 | Seven peptides stabilized HLA-A*0201 expression in binding assays and were used to stimulate peripheral blood mononuclear cells and were evaluated for granzyme B secretion. |
| 3690 | 17065343 | Other peptides recognized by type 1 diabetic or antibody-positive subjects included GFAP(143-151), IGRP(152-160), and GFAP(214-222). |
| 3691 | 17065343 | These data implicate peptides of ppIAPP, GFAP, and IGRP as CTL epitopes for a heterogenous CD8(+) T-cell response in type 1 subjects and antibody-positive relatives. |
| 3692 | 17065344 | To identify additional epitopes, HLA class I peptide affinity algorithms were used to identify a panel of peptides derived from the beta-cell proteins islet amyloid polypeptide (IAPP), islet-specific glucose-6-phosphatase catalytic subunit-related protein (IGRP), insulin, insulinoma-associated antigen 2 (IA-2), and phogrin that were predicted to bind HLA-A*0201. |
| 3693 | 17065344 | We identified peptides IAPP9-17, IGRP215-223, IGRP152-160, islet IA-2(172-180), and IA-2(482-490) as novel HLA-A*0201-restricted T-cell epitopes in type 1 diabetic patients. |
| 3694 | 17066144 | Insulin resistance and dysregulation of the degradation of neurotoxic amyloid and insulin appear at the core of the links between Alzheimer's disease and diabetes. |
| 3695 | 17066144 | Functions and expression of insulysin, an enzyme involved in the degradation of neurotoxic amyloid peptides and insulin, are usually impaired or reduced in Alzheimer's disease and diabetes. |
| 3696 | 17066144 | The increased occurrence of insulin resistance in Alzheimer's disease suggests that improving insulin effectiveness and insulysin activity may have therapeutic value in Alzheimer's disease patients and therefore is worth intensive investigation. |
| 3697 | 17066144 | Insulin resistance and dysregulation of the degradation of neurotoxic amyloid and insulin appear at the core of the links between Alzheimer's disease and diabetes. |
| 3698 | 17066144 | Functions and expression of insulysin, an enzyme involved in the degradation of neurotoxic amyloid peptides and insulin, are usually impaired or reduced in Alzheimer's disease and diabetes. |
| 3699 | 17066144 | The increased occurrence of insulin resistance in Alzheimer's disease suggests that improving insulin effectiveness and insulysin activity may have therapeutic value in Alzheimer's disease patients and therefore is worth intensive investigation. |
| 3700 | 17107885 | An in vitro model of early islet amyloid polypeptide (IAPP) fibrillogenesis using human IAPP-transgenic mouse islets. |
| 3701 | 17107885 | However, islet amyloid polypeptide (IAPP)-derived islet amyloidosis (IA) has been linked to increased rates of beta-cell apoptosis and, therefore, our goal was to develop an in vitro model of IAPP fibrillogenesis using isolated pancreatic islets from mice transgenic for human IAPP (hIAPP Tg mice). |
| 3702 | 17107885 | An in vitro model of early islet amyloid polypeptide (IAPP) fibrillogenesis using human IAPP-transgenic mouse islets. |
| 3703 | 17107885 | However, islet amyloid polypeptide (IAPP)-derived islet amyloidosis (IA) has been linked to increased rates of beta-cell apoptosis and, therefore, our goal was to develop an in vitro model of IAPP fibrillogenesis using isolated pancreatic islets from mice transgenic for human IAPP (hIAPP Tg mice). |
| 3704 | 17110595 | A nuclear receptor corepressor-dependent pathway mediates suppression of cytokine-induced C-reactive protein gene expression by liver X receptor. |
| 3705 | 17110595 | We demonstrate herein that 2 synthetic LXR ligands, T0901317 and GW3965, inhibit interleukin-1beta/interleukin-6-induced CRP mRNA and protein expression in human hepatocytes. |
| 3706 | 17110595 | Knockdown of LXRalpha/beta by short interfering RNAs completely abolished the inhibitory effect of the LXR agonist T0901317 on cytokine-induced CRP gene transcription. |
| 3707 | 17110595 | Finally, treatment of C57Bl6/J mice with LXR ligands attenuated lipopolysaccharide-induced mouse CRP and serum amyloid P component gene expression in the liver, whereas no effect was observed in LXRalphabeta knockout mice. |
| 3708 | 17110895 | The increased risk of AD may also be mediated by the exacerbation of B-amyloid neurotoxicity by advanced glycosylation end products identified in the matrix of neurofibrillary tangles and amyloid plaques in AD brains, or associations with insulin functions. |
| 3709 | 17123962 | Direct detection of transient alpha-helical states in islet amyloid polypeptide. |
| 3710 | 17123962 | The protein islet amyloid polypeptide (IAPP) is a glucose metabolism associated hormone cosecreted with insulin by the beta-cells of the pancreas. |
| 3711 | 17123962 | Direct detection of transient alpha-helical states in islet amyloid polypeptide. |
| 3712 | 17123962 | The protein islet amyloid polypeptide (IAPP) is a glucose metabolism associated hormone cosecreted with insulin by the beta-cells of the pancreas. |
| 3713 | 17139536 | Evaluation of a commercially available human serum amyloid A (SAA) turbidimetric immunoassay for determination of feline SAA concentration. |
| 3714 | 17139536 | Serum amyloid A (SAA) is an acute-phase protein in cats likely to be useful for diagnosing and monitoring inflammatory diseases, especially if rapid, reliable and automated assays can be made available. |
| 3715 | 17139536 | Evaluation of a commercially available human serum amyloid A (SAA) turbidimetric immunoassay for determination of feline SAA concentration. |
| 3716 | 17139536 | Serum amyloid A (SAA) is an acute-phase protein in cats likely to be useful for diagnosing and monitoring inflammatory diseases, especially if rapid, reliable and automated assays can be made available. |
| 3717 | 17141044 | During differentiation, transcript levels of pancreas-specific transcription factors (i.e., Pdx1, Pax4) and of genes specific for early and mature beta cells, including insulin, islet amyloid pancreatic peptide, somatostatin, and glucagon, are upregulated. |
| 3718 | 17142142 | Serum levels of resistin, serum amyloid A, and soluble vascular cell adhesion molecule-1 were measured by enzyme-linked immunosorbent assay. |
| 3719 | 17142142 | Serum resistin concentrations did not correlate with body mass index; however, there was a significant positive correlation between resistin and soluble vascular cell adhesion molecule-1 in diabetic patients. |
| 3720 | 17157312 | Kinetics of different processes in human insulin amyloid formation. |
| 3721 | 17157312 | Human insulin has long been known to form amyloid fibrils under given conditions. |
| 3722 | 17157312 | Kinetics of different processes in human insulin amyloid formation. |
| 3723 | 17157312 | Human insulin has long been known to form amyloid fibrils under given conditions. |
| 3724 | 17192466 | Human islet amyloid polypeptide oligomers disrupt cell coupling, induce apoptosis, and impair insulin secretion in isolated human islets. |
| 3725 | 17192466 | Both are characterized by the presence of islet amyloid derived from islet amyloid polypeptide (IAPP). |
| 3726 | 17192466 | Human islet amyloid polypeptide oligomers disrupt cell coupling, induce apoptosis, and impair insulin secretion in isolated human islets. |
| 3727 | 17192466 | Both are characterized by the presence of islet amyloid derived from islet amyloid polypeptide (IAPP). |
| 3728 | 17203498 | IAPP mimic blocks Abeta cytotoxic self-assembly: cross-suppression of amyloid toxicity of Abeta and IAPP suggests a molecular link between Alzheimer's disease and type II diabetes. |
| 3729 | 17222388 | To examine the roles of glucose and time on amyloid formation, we developed a rapid in vitro model using isolated islets from human islet amyloid polypeptide (hIAPP) transgenic mice. |
| 3730 | 17222388 | At various time-points throughout the culture period, islets were harvested for determination of amyloid and beta-cell areas, and for measures of cell viability, insulin content, and secretion. |
| 3731 | 17222388 | To examine the roles of glucose and time on amyloid formation, we developed a rapid in vitro model using isolated islets from human islet amyloid polypeptide (hIAPP) transgenic mice. |
| 3732 | 17222388 | At various time-points throughout the culture period, islets were harvested for determination of amyloid and beta-cell areas, and for measures of cell viability, insulin content, and secretion. |
| 3733 | 17237312 | Red meat, relative to control, resulted in: higher protein [5.3 (3.7, 6.9) % of energy], lower carbohydrate [-5.3 (-7.9, -2.7)% of energy], and higher iron [3.2 (1.1, 5.4) mg/d] intakes; lower urinary F2-isoprostane excretion [-137 (-264, -9) pmol/mmol creatinine], lower leukocyte [-0.51 (-0.99, -0.02)x10(9)/L] counts, and a trend for lower serum C-reactive protein concentrations [-1.6 (-3.3, 0.0) mg/L, P=0.06]; and no differences in concentrations of plasma F2-isoprostanes [-12 (-122, 100) pmol/L], serum gamma-glytamyltransferase [-0.8 (-3.2, 1.5) U/L], serum amyloid A protein [-1.4 (-3.4, 0.5) mg/L], and plasma fibrinogen concentrations [-0.08 (-0.40. 0.24) g/L]. |
| 3734 | 17259373 | Identification of the amyloid-degrading enzyme neprilysin in mouse islets and potential role in islet amyloidogenesis. |
| 3735 | 17259373 | It is poorly understood how the building block of amyloid, islet amyloid polypeptide (IAPP), misfolds and accumulates within the islet to contribute to cellular dysfunction. |
| 3736 | 17259373 | We sought to determine whether neprilysin, an amyloid-degrading enzyme, is present in islets and plays a role in the accumulation of amyloid fibrils. |
| 3737 | 17259373 | Islet amyloid was detected in 43% of the 6-month-old hIAPP transgenic male mice only, suggesting the sustained elevation of islet neprilysin in these mice was a compensatory mechanism aimed at preventing amyloid accumulation. |
| 3738 | 17259373 | In keeping with amyloid formation, the proportion of insulin-positive area to islet area was significantly reduced in 6-month-old hIAPP transgenic male mice, which also displayed mild fasting hyperglycemia compared with age-matched transgenic female and nontransgenic mice. |
| 3739 | 17259373 | Together, these findings demonstrate that neprilysin is a factor associated with islet amyloid accumulation and subsequent deterioration of beta-cell function in hIAPP transgenic male mice. |
| 3740 | 17259373 | Identification of the amyloid-degrading enzyme neprilysin in mouse islets and potential role in islet amyloidogenesis. |
| 3741 | 17259373 | It is poorly understood how the building block of amyloid, islet amyloid polypeptide (IAPP), misfolds and accumulates within the islet to contribute to cellular dysfunction. |
| 3742 | 17259373 | We sought to determine whether neprilysin, an amyloid-degrading enzyme, is present in islets and plays a role in the accumulation of amyloid fibrils. |
| 3743 | 17259373 | Islet amyloid was detected in 43% of the 6-month-old hIAPP transgenic male mice only, suggesting the sustained elevation of islet neprilysin in these mice was a compensatory mechanism aimed at preventing amyloid accumulation. |
| 3744 | 17259373 | In keeping with amyloid formation, the proportion of insulin-positive area to islet area was significantly reduced in 6-month-old hIAPP transgenic male mice, which also displayed mild fasting hyperglycemia compared with age-matched transgenic female and nontransgenic mice. |
| 3745 | 17259373 | Together, these findings demonstrate that neprilysin is a factor associated with islet amyloid accumulation and subsequent deterioration of beta-cell function in hIAPP transgenic male mice. |
| 3746 | 17259373 | Identification of the amyloid-degrading enzyme neprilysin in mouse islets and potential role in islet amyloidogenesis. |
| 3747 | 17259373 | It is poorly understood how the building block of amyloid, islet amyloid polypeptide (IAPP), misfolds and accumulates within the islet to contribute to cellular dysfunction. |
| 3748 | 17259373 | We sought to determine whether neprilysin, an amyloid-degrading enzyme, is present in islets and plays a role in the accumulation of amyloid fibrils. |
| 3749 | 17259373 | Islet amyloid was detected in 43% of the 6-month-old hIAPP transgenic male mice only, suggesting the sustained elevation of islet neprilysin in these mice was a compensatory mechanism aimed at preventing amyloid accumulation. |
| 3750 | 17259373 | In keeping with amyloid formation, the proportion of insulin-positive area to islet area was significantly reduced in 6-month-old hIAPP transgenic male mice, which also displayed mild fasting hyperglycemia compared with age-matched transgenic female and nontransgenic mice. |
| 3751 | 17259373 | Together, these findings demonstrate that neprilysin is a factor associated with islet amyloid accumulation and subsequent deterioration of beta-cell function in hIAPP transgenic male mice. |
| 3752 | 17259373 | Identification of the amyloid-degrading enzyme neprilysin in mouse islets and potential role in islet amyloidogenesis. |
| 3753 | 17259373 | It is poorly understood how the building block of amyloid, islet amyloid polypeptide (IAPP), misfolds and accumulates within the islet to contribute to cellular dysfunction. |
| 3754 | 17259373 | We sought to determine whether neprilysin, an amyloid-degrading enzyme, is present in islets and plays a role in the accumulation of amyloid fibrils. |
| 3755 | 17259373 | Islet amyloid was detected in 43% of the 6-month-old hIAPP transgenic male mice only, suggesting the sustained elevation of islet neprilysin in these mice was a compensatory mechanism aimed at preventing amyloid accumulation. |
| 3756 | 17259373 | In keeping with amyloid formation, the proportion of insulin-positive area to islet area was significantly reduced in 6-month-old hIAPP transgenic male mice, which also displayed mild fasting hyperglycemia compared with age-matched transgenic female and nontransgenic mice. |
| 3757 | 17259373 | Together, these findings demonstrate that neprilysin is a factor associated with islet amyloid accumulation and subsequent deterioration of beta-cell function in hIAPP transgenic male mice. |
| 3758 | 17259373 | Identification of the amyloid-degrading enzyme neprilysin in mouse islets and potential role in islet amyloidogenesis. |
| 3759 | 17259373 | It is poorly understood how the building block of amyloid, islet amyloid polypeptide (IAPP), misfolds and accumulates within the islet to contribute to cellular dysfunction. |
| 3760 | 17259373 | We sought to determine whether neprilysin, an amyloid-degrading enzyme, is present in islets and plays a role in the accumulation of amyloid fibrils. |
| 3761 | 17259373 | Islet amyloid was detected in 43% of the 6-month-old hIAPP transgenic male mice only, suggesting the sustained elevation of islet neprilysin in these mice was a compensatory mechanism aimed at preventing amyloid accumulation. |
| 3762 | 17259373 | In keeping with amyloid formation, the proportion of insulin-positive area to islet area was significantly reduced in 6-month-old hIAPP transgenic male mice, which also displayed mild fasting hyperglycemia compared with age-matched transgenic female and nontransgenic mice. |
| 3763 | 17259373 | Together, these findings demonstrate that neprilysin is a factor associated with islet amyloid accumulation and subsequent deterioration of beta-cell function in hIAPP transgenic male mice. |
| 3764 | 17259373 | Identification of the amyloid-degrading enzyme neprilysin in mouse islets and potential role in islet amyloidogenesis. |
| 3765 | 17259373 | It is poorly understood how the building block of amyloid, islet amyloid polypeptide (IAPP), misfolds and accumulates within the islet to contribute to cellular dysfunction. |
| 3766 | 17259373 | We sought to determine whether neprilysin, an amyloid-degrading enzyme, is present in islets and plays a role in the accumulation of amyloid fibrils. |
| 3767 | 17259373 | Islet amyloid was detected in 43% of the 6-month-old hIAPP transgenic male mice only, suggesting the sustained elevation of islet neprilysin in these mice was a compensatory mechanism aimed at preventing amyloid accumulation. |
| 3768 | 17259373 | In keeping with amyloid formation, the proportion of insulin-positive area to islet area was significantly reduced in 6-month-old hIAPP transgenic male mice, which also displayed mild fasting hyperglycemia compared with age-matched transgenic female and nontransgenic mice. |
| 3769 | 17259373 | Together, these findings demonstrate that neprilysin is a factor associated with islet amyloid accumulation and subsequent deterioration of beta-cell function in hIAPP transgenic male mice. |
| 3770 | 17267050 | Serum amyloid A (SAA), a HDL apolipoprotein is a risk marker for cardiovascular disease. |
| 3771 | 17267050 | TNF-alpha, IL-1beta, IL-8 and IL-1ra levels were measured by ELISA in the culture supernatants and in serum of subjects. |
| 3772 | 17267050 | We make the novel observation that neutrophils and monocytes of diabetics are more responsive to SAA for the induction of the proinflammatory cytokine IL-1beta and the proangiogenic and chemotactic protein IL-8. |
| 3773 | 17267050 | Incremental TNF-alpha production was also found to occur when monocytes were stimulated with SAA. |
| 3774 | 17267401 | Insulin antagonizes interleukin-6 signaling and is anti-inflammatory in 3T3-L1 adipocytes. |
| 3775 | 17267401 | Adipose tissue secretes different adipokines, including interleukin-6 (IL-6), that have been implicated in the insulin resistance and inflammatory state characterizing obesity. |
| 3776 | 17267401 | We examined the putative cross-talk between insulin and IL-6 in adipose cells and found that insulin exerts an inhibitory effect on the IL-6 signaling pathway by altering the post-translational modifications of the signal transducer and activator of transcription 3 (STAT3). |
| 3777 | 17267401 | Insulin reduces the tyrosine phosphorylation and increases the serine phosphorylation of STAT3, thereby reducing its nuclear localization and transcriptional activity. |
| 3778 | 17267401 | Signaling through the MEK/MAPK pathway plays an important role as treatment with the MEK inhibitor PD98059 reduces the effects of insulin on IL-6 signaling. |
| 3779 | 17267401 | We also show that the protein tyrosine phosphatase SHP2 is activated upon insulin signaling and is required for the dephosphorylation of STAT3 and that insulin exerts a synergistic effect with IL-6 on suppressor of cytokine signaling 3 expression. |
| 3780 | 17267401 | As a consequence, the IL-6-induced expression of the inflammatory markers serum amyloid A 3 and haptoglobin are significantly decreased in cells incubated with both IL-6 and insulin. |
| 3781 | 17267401 | Thus, insulin exerts an important anti-inflammatory effect in adipose cells by impairing the IL-6 signal at several levels. |
| 3782 | 17311418 | Aromatic interactions are not required for amyloid fibril formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphology. |
| 3783 | 17311418 | Here we examine whether aromatic residues are necessary for amyloid formation by islet amyloid polypeptide (IAPP). |
| 3784 | 17311418 | CD, thioflavin binding assays, AFM, and TEM measurements all show that the triple leucine mutant readily forms amyloid fibrils. |
| 3785 | 17311418 | Aromatic interactions are not required for amyloid fibril formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphology. |
| 3786 | 17311418 | Here we examine whether aromatic residues are necessary for amyloid formation by islet amyloid polypeptide (IAPP). |
| 3787 | 17311418 | CD, thioflavin binding assays, AFM, and TEM measurements all show that the triple leucine mutant readily forms amyloid fibrils. |
| 3788 | 17311418 | Aromatic interactions are not required for amyloid fibril formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphology. |
| 3789 | 17311418 | Here we examine whether aromatic residues are necessary for amyloid formation by islet amyloid polypeptide (IAPP). |
| 3790 | 17311418 | CD, thioflavin binding assays, AFM, and TEM measurements all show that the triple leucine mutant readily forms amyloid fibrils. |
| 3791 | 17340097 | Effects of confinement on insulin amyloid fibrils formation. |
| 3792 | 17340097 | Insulin, a 51-residue protein universally used in diabetes treatment, is known to produce amyloid fibrils at high temperature and acidic conditions. |
| 3793 | 17340097 | Effects of confinement on insulin amyloid fibrils formation. |
| 3794 | 17340097 | Insulin, a 51-residue protein universally used in diabetes treatment, is known to produce amyloid fibrils at high temperature and acidic conditions. |
| 3795 | 17349968 | Membrane interaction of islet amyloid polypeptide. |
| 3796 | 17353295 | The major factors for progressive loss of beta-cell function and mass are glucotoxicity, lipotoxicity, proinflammatory cytokines, leptin, and islet cell amyloid. |
| 3797 | 17353295 | The TZDs improve insulin secretory capacity, decrease beta-cell apoptosis, and reduce islet cell amyloid with maintenance of neogenesis. |
| 3798 | 17353295 | From the two major incretins, glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), only the first one or its mimetics or enhancers can be used for treatment because the diabetic beta-cell is resistant to GIP action. |
| 3799 | 17353295 | The acute effect of GLP-1 and GLP-1 receptor agonists on beta-cells is stimulation of glucose-dependent insulin release, followed by enhancement of insulin biosynthesis and stimulation of insulin gene transcription. |
| 3800 | 17353295 | The inhibition of the activity of the DPP-IV enzyme enhances endogenous GLP-1 action in vivo, mediated not only by GLP-1 but also by other mediators. |
| 3801 | 17353295 | The major factors for progressive loss of beta-cell function and mass are glucotoxicity, lipotoxicity, proinflammatory cytokines, leptin, and islet cell amyloid. |
| 3802 | 17353295 | The TZDs improve insulin secretory capacity, decrease beta-cell apoptosis, and reduce islet cell amyloid with maintenance of neogenesis. |
| 3803 | 17353295 | From the two major incretins, glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), only the first one or its mimetics or enhancers can be used for treatment because the diabetic beta-cell is resistant to GIP action. |
| 3804 | 17353295 | The acute effect of GLP-1 and GLP-1 receptor agonists on beta-cells is stimulation of glucose-dependent insulin release, followed by enhancement of insulin biosynthesis and stimulation of insulin gene transcription. |
| 3805 | 17353295 | The inhibition of the activity of the DPP-IV enzyme enhances endogenous GLP-1 action in vivo, mediated not only by GLP-1 but also by other mediators. |
| 3806 | 17353506 | Toxic human islet amyloid polypeptide (h-IAPP) oligomers are intracellular, and vaccination to induce anti-toxic oligomer antibodies does not prevent h-IAPP-induced beta-cell apoptosis in h-IAPP transgenic mice. |
| 3807 | 17459337 | Complement activation by islet amyloid polypeptide (IAPP) and alpha-synuclein 112. |
| 3808 | 17459337 | We compared their complement activating ability in vitro with those of islet amyloid polypeptide (IAPP), which aggregates in the pancreas of T2DM, and alpha-synuclein (alpha-Syn), which aggregates in PD. |
| 3809 | 17459337 | Complement activation by islet amyloid polypeptide (IAPP) and alpha-synuclein 112. |
| 3810 | 17459337 | We compared their complement activating ability in vitro with those of islet amyloid polypeptide (IAPP), which aggregates in the pancreas of T2DM, and alpha-synuclein (alpha-Syn), which aggregates in PD. |
| 3811 | 17475933 | High expression rates of human islet amyloid polypeptide induce endoplasmic reticulum stress mediated beta-cell apoptosis, a characteristic of humans with type 2 but not type 1 diabetes. |
| 3812 | 17482289 | DPP-4 inhibition improves glucose tolerance and increases insulin and GLP-1 responses to gastric glucose in association with normalized islet topography in mice with beta-cell-specific overexpression of human islet amyloid polypeptide. |
| 3813 | 17482289 | In this study, we explored the effects of DPP-4 inhibition in mice with beta-cell overexpression of human islet amyloid polypeptide (IAPP). |
| 3814 | 17482289 | After eight weeks, a gastric tolerance test showed that vildagliptin improved glucose tolerance and markedly (approximately ten-fold) augmented the insulin response in association with augmented (approximately five-fold) levels of intact glucagon-like peptide-1 (GLP-1). |
| 3815 | 17482289 | DPP-4 inhibition improves glucose tolerance and increases insulin and GLP-1 responses to gastric glucose in association with normalized islet topography in mice with beta-cell-specific overexpression of human islet amyloid polypeptide. |
| 3816 | 17482289 | In this study, we explored the effects of DPP-4 inhibition in mice with beta-cell overexpression of human islet amyloid polypeptide (IAPP). |
| 3817 | 17482289 | After eight weeks, a gastric tolerance test showed that vildagliptin improved glucose tolerance and markedly (approximately ten-fold) augmented the insulin response in association with augmented (approximately five-fold) levels of intact glucagon-like peptide-1 (GLP-1). |
| 3818 | 17487340 | There is evidence to suggest that impaired activities of neurotrophic factors such as insulin, IGF-1 and NGF, which occur in both diabetes and AD, may provide a mechanistic link between the two disorders. |
| 3819 | 17487340 | Impaired insulin signaling in particular appears to be involved in hyperphosphorylation of the tau protein, which constitutes neurofibrillary tangles in AD. |
| 3820 | 17487340 | The linkage between abnormal amyloid metabolism and phosphor-tau is likely to be provided by the activation of caspases both by increased amyloid-beta and by impaired insulin signaling. |
| 3821 | 17495860 | Amylin (islet amyloid peptide) plays a critical role in islet amyloidosis and in the development of beta-cell dysfunction in patients with diabetes; however, the involvement of amylin in renal amyloidosis has not been studied. |
| 3822 | 17502604 | Automated 2D IR spectroscopy using a mid-IR pulse shaper and application of this technology to the human islet amyloid polypeptide. |
| 3823 | 17502604 | With these methods in hand, we apply 2D IR spectroscopy to study the structural diversity in amyloid fibers of aggregated human islet amyloid polypeptide (hIAPP), which is involved with type 2 diabetes. |
| 3824 | 17502604 | Automated 2D IR spectroscopy using a mid-IR pulse shaper and application of this technology to the human islet amyloid polypeptide. |
| 3825 | 17502604 | With these methods in hand, we apply 2D IR spectroscopy to study the structural diversity in amyloid fibers of aggregated human islet amyloid polypeptide (hIAPP), which is involved with type 2 diabetes. |
| 3826 | 17516840 | This review focuses primarily on islet structural and functional changes related to an activated islet renin- angiotensin system (RAS), islet oxidative-redox imbalance, the concurrence of islet fibrosis (pericapillary, intra- and peri-islet), and islet amyloid deposition (pericapillary, intra- and peri-islet). |
| 3827 | 17526769 | In 2004, the human islet amyloid polypeptide (HIP) rat model was created by transfecting the Sprague-Dawley rat with the human islet amyloid polypeptide (hIAPP)-amylin gene. |
| 3828 | 17526769 | The 4-month HIP model (FBS 123 mg/dl) demonstrated an abundance of beta-cells and insulin secretory granules with significant pericapillary and inter-beta-cell islet amyloid deposition. |
| 3829 | 17526769 | In 2004, the human islet amyloid polypeptide (HIP) rat model was created by transfecting the Sprague-Dawley rat with the human islet amyloid polypeptide (hIAPP)-amylin gene. |
| 3830 | 17526769 | The 4-month HIP model (FBS 123 mg/dl) demonstrated an abundance of beta-cells and insulin secretory granules with significant pericapillary and inter-beta-cell islet amyloid deposition. |
| 3831 | 17554795 | Familial amyloid polyneuropathy (FAP) is the most common form of inherited amyloidotic polyneuropathy, with clinical and electrophysiologic findings similar to neuropathies with differing etiologies (e.g., diabetes mellitus). |
| 3832 | 17554795 | Transthyretin amyloidosis is treated by liver transplantation, which eliminates the mutated transthyretin from the blood, but for some patients continued amyloid deposition can occur from wild-type (normal) transthyretin. |
| 3833 | 17554795 | Familial amyloid polyneuropathy (FAP) is the most common form of inherited amyloidotic polyneuropathy, with clinical and electrophysiologic findings similar to neuropathies with differing etiologies (e.g., diabetes mellitus). |
| 3834 | 17554795 | Transthyretin amyloidosis is treated by liver transplantation, which eliminates the mutated transthyretin from the blood, but for some patients continued amyloid deposition can occur from wild-type (normal) transthyretin. |
| 3835 | 17563062 | However, other adipocyte-derived factors, e.g., hyaluronan and serum amyloid A (SAA), can facilitate monocyte adhesion and chemotaxis, respectively. |
| 3836 | 17563062 | Nuclear factor-kappaB was upregulated and peroxisome proliferator-activated receptor (PPAR)gamma was downregulated in hypertrophic 3T3-L1 cells, with increased expression of SAA3 and increased hyaluronan production. |
| 3837 | 17563062 | Hypertrophic adipocytes demonstrated overexpression of SAA3 and hyaluronan synthase 2 in vitro and in vivo in diet-induced and genetic obesity. |
| 3838 | 17563062 | This complex, purified by binding to a biotinylated hyaluronan binding protein affinity column, also showed monocyte chemotactic activity, which was dependent on the presence of SAA3 and hyaluronan but independent of MCP-1. |
| 3839 | 17563062 | We hypothesize that adipocyte hypertrophy leads to increased production of SAA and hyaluronan, which act in concert to recruit and retain monocytes, thereby leading to local inflammation in adipose tissue. |
| 3840 | 17563070 | Impairment of the ubiquitin-proteasome pathway is a downstream endoplasmic reticulum stress response induced by extracellular human islet amyloid polypeptide and contributes to pancreatic beta-cell apoptosis. |
| 3841 | 17565412 | Several mechanisms have been proposed to be responsible for insulin resistance, including increased non-esterified fatty acids, inflammatory cytokines, adipokines, and mitochondrial dysfunction, as well as glucotoxicity, lipotoxicity, and amyloid formation for beta-cell dysfunction. |
| 3842 | 17594389 | The mechanisms responsible for loss of beta-cell function are likely to be multifactorial, but may involve toxicity because of elevated glucose and/or lipid levels, increased secretory demand because of insulin resistance, amyloid deposition and altered levels of cytokines. |
| 3843 | 17660321 | Mechanism of islet amyloid polypeptide fibrillation at lipid interfaces studied by infrared reflection absorption spectroscopy. |
| 3844 | 17660321 | Islet amyloid polypeptide (IAPP) is a pancreatic hormone and one of a number of proteins that are involved in the formation of amyloid deposits in the islets of Langerhans of type II diabetes mellitus patients. |
| 3845 | 17660321 | Mechanism of islet amyloid polypeptide fibrillation at lipid interfaces studied by infrared reflection absorption spectroscopy. |
| 3846 | 17660321 | Islet amyloid polypeptide (IAPP) is a pancreatic hormone and one of a number of proteins that are involved in the formation of amyloid deposits in the islets of Langerhans of type II diabetes mellitus patients. |
| 3847 | 17675900 | Mechanisms implicated in beta-cell dysfunction include genetic abnormalities, prenatal and early postnatal insults, and environmental events along with obesity, dyslipidemia-lipotoxicity, glucotoxicity, oxidative stress, chronic low-grade inflammation, amyloid deposition, and activation of the local renin-angiotensin system. |
| 3848 | 17679816 | That adipose tissue releases a wide range of adipokines, growth factors, enzymes, and enzyme substrates linked to vascular injury provides a plausible explanation for the role of fat in vascular disease: tumor necrosis factor-alpha, leptin, resistin, interleukin-1, -6, -8, and -18, serum amyloid A, monocyte chemoattractant protein I, macrophage inhibitory factor, aortic carboxypeptidase, hepa-rin-binding epidermal growth factor-like growth factor, vascular endothelial growth factor, transforming growth factor beta, angiotensinogen, cathepsin S, estradiol, cortisol, mineralocorticoid releasing factor, and calcitonin peptides are probable fat-derived prothrombotic, proinflammatory, and proatherosclerotic agents acting in a paracrine and/or endocrine manner. |
| 3849 | 17679816 | Other adipocyte products such as adiponectin, transforming growth factor beta, and interleukin-10 exert some antiatherogenic effects. |
| 3850 | 17804609 | Deposition of islet amyloid polypeptide (IAPP) as amyloid in the pancreatic islet occurs in approximately 90% of individuals with Type 2 diabetes and is associated with decreased islet beta-cell mass and function. |
| 3851 | 17882804 | Fat issue secretes leptin, tumor necrosis factor alpha, resistin, adiponectin, interleukin-6, free fatty acids, visfatin, omentin, perilipin, and other substances that influence the condition of insulinoresistance, one of the main factors responsible for DM2. |
| 3852 | 17882804 | The article also cover the participation of other mechanisms - insulin secretion defect, oxidation stress, low secretion of glucagon-like peptide 1, apoptosis, an increased quantity of amyloid and the fl-cell pull in the pancreatic island--in DM2 pathogenesis. |
| 3853 | 17882804 | The authors present data on the secretion of leptin, resistin, adiponectin, and tumor necrosis factor a, as well as the condition of the functional activity of beta-cells and the degree of insulinoresistance in 30 DM2 patients receiving dietotherapy. |
| 3854 | 17891154 | The retromer complex is required for the sorting of acid hydrolases to lysosomes, transcytosis of the polymeric immunoglobulin receptor, Wnt gradient formation, iron transporter recycling and processing of the amyloid precursor protein. |
| 3855 | 17891154 | Human retromer consists of two smaller complexes: the cargo recognition VPS26-VPS29-VPS35 heterotrimer and a membrane-targeting heterodimer or homodimer of SNX1 and/or SNX2 (ref. 13). |
| 3856 | 17891154 | Here we report the crystal structure of a VPS29-VPS35 subcomplex showing how the metallophosphoesterase-fold subunit VPS29 (refs 14, 15) acts as a scaffold for the carboxy-terminal half of VPS35. |
| 3857 | 17891154 | VPS35 forms a horseshoe-shaped, right-handed, alpha-helical solenoid, the concave face of which completely covers the metal-binding site of VPS29, whereas the convex face exposes a series of hydrophobic interhelical grooves. |
| 3858 | 17891154 | A hybrid structural model derived from crystal structures, electron microscopy, interaction studies and bioinformatics shows that the alpha-solenoid fold extends the full length of VPS35, and that VPS26 is bound at the opposite end from VPS29. |
| 3859 | 17924651 | Amyloid formation by pro-islet amyloid polypeptide processing intermediates: examination of the role of protein heparan sulfate interactions and implications for islet amyloid formation in type 2 diabetes. |
| 3860 | 17924651 | In type 2 diabetes, islet amyloid polypeptide (IAPP, also known as amylin) forms cytotoxic amyloid deposits in the pancreas, and these are believed to contribute to the pathology of the disease. |
| 3861 | 17924651 | Amyloid formation by pro-islet amyloid polypeptide processing intermediates: examination of the role of protein heparan sulfate interactions and implications for islet amyloid formation in type 2 diabetes. |
| 3862 | 17924651 | In type 2 diabetes, islet amyloid polypeptide (IAPP, also known as amylin) forms cytotoxic amyloid deposits in the pancreas, and these are believed to contribute to the pathology of the disease. |
| 3863 | 17979302 | The 37-residue amylin peptide, also known as islet amyloid polypeptide, forms fibrils that are the main peptide or protein component of amyloid that develops in the pancreas of type 2 diabetes patients. |
| 3864 | 17979302 | Amylin also readily forms amyloid fibrils in vitro that are highly polymorphic under typical experimental conditions. |
| 3865 | 17979302 | The molecular structure of amylin protofilaments in striated ribbons closely resembles the protofilament in amyloid fibrils with a similar morphology formed by the 40-residue beta-amyloid peptide that is associated with Alzheimer's disease. |
| 3866 | 17979302 | The 37-residue amylin peptide, also known as islet amyloid polypeptide, forms fibrils that are the main peptide or protein component of amyloid that develops in the pancreas of type 2 diabetes patients. |
| 3867 | 17979302 | Amylin also readily forms amyloid fibrils in vitro that are highly polymorphic under typical experimental conditions. |
| 3868 | 17979302 | The molecular structure of amylin protofilaments in striated ribbons closely resembles the protofilament in amyloid fibrils with a similar morphology formed by the 40-residue beta-amyloid peptide that is associated with Alzheimer's disease. |
| 3869 | 17979302 | The 37-residue amylin peptide, also known as islet amyloid polypeptide, forms fibrils that are the main peptide or protein component of amyloid that develops in the pancreas of type 2 diabetes patients. |
| 3870 | 17979302 | Amylin also readily forms amyloid fibrils in vitro that are highly polymorphic under typical experimental conditions. |
| 3871 | 17979302 | The molecular structure of amylin protofilaments in striated ribbons closely resembles the protofilament in amyloid fibrils with a similar morphology formed by the 40-residue beta-amyloid peptide that is associated with Alzheimer's disease. |
| 3872 | 18063919 | LX receptors are also involved in the regulation of renin secretion, inhibit the formation of amyloid ss in the central nervous system, regulate gonadal function and steroidogenesis both in gonads and in adrenals, influence the proliferation and differentiation of keratinocytes, and inhibit the proliferation of tumor cells. |
| 3873 | 18155730 | Islet amyloid polypeptide forms rigid lipid-protein amyloid fibrils on supported phospholipid bilayers. |
| 3874 | 18155730 | Islet amyloid polypeptide (IAPP) forms fibrillar amyloid deposits in the pancreatic islets of Langerhans of patients with type 2 diabetes mellitus, and its misfolding and aggregation are thought to contribute to beta-cell death. |
| 3875 | 18155730 | Islet amyloid polypeptide forms rigid lipid-protein amyloid fibrils on supported phospholipid bilayers. |
| 3876 | 18155730 | Islet amyloid polypeptide (IAPP) forms fibrillar amyloid deposits in the pancreatic islets of Langerhans of patients with type 2 diabetes mellitus, and its misfolding and aggregation are thought to contribute to beta-cell death. |
| 3877 | 18160637 | Reduced mRNA and protein for an apolipoprotein E (ApoE) receptor family member, SorLA (LR11) has been found in LOAD but not early-onset AD, suggesting that LR11 loss is not secondary to pathology. |
| 3878 | 18160637 | LR11 is a neuronal sorting protein that reduces amyloid precursor protein (APP) trafficking to secretases that generate beta-amyloid (Abeta). |
| 3879 | 18160637 | Because lipoprotein receptors are typically lipid-regulated, we postulated that LR11 is regulated by docosahexaenoic acid (DHA), an essential omega-3 fatty acid related to reduced AD risk and reduced Abeta accumulation. |
| 3880 | 18160637 | In vivo elevation of LR11 was also observed with dietary fish oil in young rats with insulin resistance, a model for type II diabetes, another AD risk factor. |
| 3881 | 18160637 | Because reduced LR11 is known to increase Abeta production and may be a significant genetic cause of LOAD, our results indicate that DHA increases in SorLA/LR11 levels may play an important role in preventing LOAD. |
| 3882 | 18184370 | Glycogen synthase kinase-3beta, or a link between amyloid and tau pathology? |
| 3883 | 18193704 | Work on the pentraxin proteins, C-reactive protein (CRP) and serum amyloid P component (SAP), and on amyloidosis, has benefited from abundant serendipity, leading to routine clinical use of CRP measurements, the invention of SAP scintigraphy for amyloidosis, the establishment of the NHS National Amyloidosis Centre providing superior patient care, and latterly the invention of a novel pharmacological mechanism for therapeutic depletion of pathogenic proteins. |
| 3884 | 18197729 | Other genes involved in the disease pathways related to AD pathology in addition to cholesterol metabolism, neuroinflammation, amyloid and tau cascade, neuronal signalling, and plasticity are under investigation. |
| 3885 | 18243137 | The misfolding of islet amyloid polypeptide (IAPP, amylin) results in the formation of islet amyloid, which is one of the most common pathological features of type 2 diabetes (T2D). |
| 3886 | 18243137 | Amylin, a 37-amino-acid peptide co-secreted with insulin and apolipoprotein E (ApoE) from the beta-cells of pancreatic islets, is thought to be responsible for the reduced mass of insulin-producing beta-cells. |
| 3887 | 18267105 | Surface-enhanced nucleation of insulin amyloid fibrillation. |
| 3888 | 18267105 | Here, we show that heterogeneous surfaces accelerate the human insulin nucleation process that is the rate-determining step during amyloid fibril formation. |
| 3889 | 18267105 | Surface-enhanced nucleation of insulin amyloid fibrillation. |
| 3890 | 18267105 | Here, we show that heterogeneous surfaces accelerate the human insulin nucleation process that is the rate-determining step during amyloid fibril formation. |
| 3891 | 18305836 | In this article, we support the case that the neurotoxic agent in Alzheimer's disease is a soluble aggregated form of the amyloid beta peptide (Abeta), probably complexed with divalent copper. |
| 3892 | 18314421 | Type 2 diabetes (T2DM) is characterized by insulin resistance, defective insulin secretion, loss of beta-cell mass with increased beta-cell apoptosis and islet amyloid. |
| 3893 | 18314421 | The islet amyloid is derived from islet amyloid polypeptide (IAPP, amylin), a protein coexpressed and cosecreted with insulin by pancreatic beta-cells. |
| 3894 | 18314421 | Type 2 diabetes (T2DM) is characterized by insulin resistance, defective insulin secretion, loss of beta-cell mass with increased beta-cell apoptosis and islet amyloid. |
| 3895 | 18314421 | The islet amyloid is derived from islet amyloid polypeptide (IAPP, amylin), a protein coexpressed and cosecreted with insulin by pancreatic beta-cells. |
| 3896 | 18320241 | Cleavage agents for soluble oligomers of human islet amyloid polypeptide. |
| 3897 | 18320241 | Soluble oligomers of human islet amyloid polypeptide (h-IAPP) are implicated in the initiation of beta-cell apoptosis leading to type 2 diabetes mellitus (T2DM). |
| 3898 | 18320241 | Cleavage agents for soluble oligomers of human islet amyloid polypeptide. |
| 3899 | 18320241 | Soluble oligomers of human islet amyloid polypeptide (h-IAPP) are implicated in the initiation of beta-cell apoptosis leading to type 2 diabetes mellitus (T2DM). |
| 3900 | 18370645 | More recent data on experimental atherosclerosis in the mouse shows that (1) insulin administration reduces the number and the size of atherosclerotic lesions in apo E null mice and (2) in IRS-2 null mice, the interruption in insulin signal transduction results in enhanced atherogenicity. |
| 3901 | 18370645 | Our own most recent data show that a low dose infusion of insulin in patients with acute myocardial infarction induces a reduction in inflammation (C-reactive protein and serum amyloid A) and oxidative stress, and promotes fibrinolysis. |
| 3902 | 18370776 | In insulin resistant states and diabetes, heat shock factor 1(HSF-1) is low in insulin sensitive tissues, resulting in low Hsp 60, 70, and 90 levels. |
| 3903 | 18370776 | We propose that low Hsps levels are the result of decreased insulin action leading to less phosphorylation of PI3K, PKB, and glycogen synthase kinase-3 (GSK-3). |
| 3904 | 18370776 | Low Hsps make organs vulnerable to injury, impair the stress response, accelerate systemic inflammation, raise islet amyloid polypeptide, and increase insulin resistance. |
| 3905 | 18370776 | Support for the proposed "vicious" cycle is based on the observation that GSK-3 inhibition and Hsp stimulation result in increased insulin sensitivity, reduced accumulation of degenerative proteins with in the cell, improved wound healing, decreased organ damage and improved recovery from vascular ischemia. |
| 3906 | 18372080 | Since diabetes is a risk factor for Alzheimer's disease (AD), we asked if there is a functional interaction between high glucose and elevated beta amyloid peptide (Abeta) in cultured brain microvascular endothelial cells and presymptomatic AD transgenic mice. |
| 3907 | 18406800 | Homeodomain protein IDX-1: a master regulator of pancreas development and insulin gene expression. |
| 3908 | 18406800 | In the adult endocrine pancreas, IDX-1 is primarily expressed in beta cells, where it is a key factor in the upregulation of insulin gene transcription and appears to have a role in the regulation of the somatostatin, glucokinase, glucose transporter-2, and islet amyloid polypeptide genes. |
| 3909 | 18406800 | The observed functions of IDX-1 and its downregulation in parallel with insulin in glucose-toxicity models implicate IDX-1 as a potential factor contributing to the pathogenesis of diabetes mellitus. |
| 3910 | 18407659 | Interaction with amyloid beta peptide compromises the lipid binding function of apolipoprotein E. |
| 3911 | 18407659 | It is also associated with protein misfolding or amyloid proteopathy of the beta amyloid peptide (Abeta) in Alzheimer's disease (AD) and cerebral amyloid angiopathy. |
| 3912 | 18407659 | The objective of this study is to examine if the neurotoxic oligomeric Abeta interacts with apoE CT and if this association affects the lipoprotein binding function of recombinant human apoE CT. |
| 3913 | 18407659 | Site-specific fluorescence labeling of single cysteine-containing apoE CT variants with donor probes were employed to identify the binding of Abeta bearing an acceptor probe by intermolecular fluorescence resonance energy-transfer analysis. |
| 3914 | 18407659 | In addition, incubation of apoE CT with Abeta severely impaired the lipid binding ability and the overall amount of lipid-associated apoE CT. |
| 3915 | 18407659 | However, when apoE CT is present in a lipid-bound state, Abeta appears to be localized within the lipid milieu of the lipoprotein particle and not associated with any specific segments of the protein. |
| 3916 | 18407659 | When our data are taken together, they suggest that Abeta association compromises the fundamental lipoprotein binding function of apoE, which may have implications not only in terms of amyloid buildup but also in terms of the accumulation of cholesterol at extracellular sites. |
| 3917 | 18407659 | Interaction with amyloid beta peptide compromises the lipid binding function of apolipoprotein E. |
| 3918 | 18407659 | It is also associated with protein misfolding or amyloid proteopathy of the beta amyloid peptide (Abeta) in Alzheimer's disease (AD) and cerebral amyloid angiopathy. |
| 3919 | 18407659 | The objective of this study is to examine if the neurotoxic oligomeric Abeta interacts with apoE CT and if this association affects the lipoprotein binding function of recombinant human apoE CT. |
| 3920 | 18407659 | Site-specific fluorescence labeling of single cysteine-containing apoE CT variants with donor probes were employed to identify the binding of Abeta bearing an acceptor probe by intermolecular fluorescence resonance energy-transfer analysis. |
| 3921 | 18407659 | In addition, incubation of apoE CT with Abeta severely impaired the lipid binding ability and the overall amount of lipid-associated apoE CT. |
| 3922 | 18407659 | However, when apoE CT is present in a lipid-bound state, Abeta appears to be localized within the lipid milieu of the lipoprotein particle and not associated with any specific segments of the protein. |
| 3923 | 18407659 | When our data are taken together, they suggest that Abeta association compromises the fundamental lipoprotein binding function of apoE, which may have implications not only in terms of amyloid buildup but also in terms of the accumulation of cholesterol at extracellular sites. |
| 3924 | 18407659 | Interaction with amyloid beta peptide compromises the lipid binding function of apolipoprotein E. |
| 3925 | 18407659 | It is also associated with protein misfolding or amyloid proteopathy of the beta amyloid peptide (Abeta) in Alzheimer's disease (AD) and cerebral amyloid angiopathy. |
| 3926 | 18407659 | The objective of this study is to examine if the neurotoxic oligomeric Abeta interacts with apoE CT and if this association affects the lipoprotein binding function of recombinant human apoE CT. |
| 3927 | 18407659 | Site-specific fluorescence labeling of single cysteine-containing apoE CT variants with donor probes were employed to identify the binding of Abeta bearing an acceptor probe by intermolecular fluorescence resonance energy-transfer analysis. |
| 3928 | 18407659 | In addition, incubation of apoE CT with Abeta severely impaired the lipid binding ability and the overall amount of lipid-associated apoE CT. |
| 3929 | 18407659 | However, when apoE CT is present in a lipid-bound state, Abeta appears to be localized within the lipid milieu of the lipoprotein particle and not associated with any specific segments of the protein. |
| 3930 | 18407659 | When our data are taken together, they suggest that Abeta association compromises the fundamental lipoprotein binding function of apoE, which may have implications not only in terms of amyloid buildup but also in terms of the accumulation of cholesterol at extracellular sites. |
| 3931 | 18408164 | Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane. |
| 3932 | 18408164 | Fibrillar protein deposits (amyloid) in the pancreatic islets of Langerhans are thought to be involved in death of the insulin-producing islet beta cells in type 2 diabetes mellitus. |
| 3933 | 18408164 | It has been suggested that the mechanism of this beta cell death involves membrane disruption by human islet amyloid polypeptide (hIAPP), the major constituent of islet amyloid. |
| 3934 | 18408164 | Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane. |
| 3935 | 18408164 | Fibrillar protein deposits (amyloid) in the pancreatic islets of Langerhans are thought to be involved in death of the insulin-producing islet beta cells in type 2 diabetes mellitus. |
| 3936 | 18408164 | It has been suggested that the mechanism of this beta cell death involves membrane disruption by human islet amyloid polypeptide (hIAPP), the major constituent of islet amyloid. |
| 3937 | 18408164 | Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane. |
| 3938 | 18408164 | Fibrillar protein deposits (amyloid) in the pancreatic islets of Langerhans are thought to be involved in death of the insulin-producing islet beta cells in type 2 diabetes mellitus. |
| 3939 | 18408164 | It has been suggested that the mechanism of this beta cell death involves membrane disruption by human islet amyloid polypeptide (hIAPP), the major constituent of islet amyloid. |
| 3940 | 18424002 | The aims of the study were to investigate whether the level of amyloid beta-peptide (Abeta) (1-40) was increased in brain of diabetic rats and whether the increase was associated with dysfunction of P-glycoprotein at the blood-brain barrier. |
| 3941 | 18442979 | Structure of alpha-helical membrane-bound human islet amyloid polypeptide and its implications for membrane-mediated misfolding. |
| 3942 | 18442979 | Human islet amyloid polypeptide (hIAPP) misfolding is thought to play an important role in the pathogenesis of type II diabetes mellitus. |
| 3943 | 18442979 | Structure of alpha-helical membrane-bound human islet amyloid polypeptide and its implications for membrane-mediated misfolding. |
| 3944 | 18442979 | Human islet amyloid polypeptide (hIAPP) misfolding is thought to play an important role in the pathogenesis of type II diabetes mellitus. |
| 3945 | 18451519 | Amylin (IAPP; islet amyloid polypeptide), an inhibitor for glybenclamide, did not inhibit the activity of the isolated compounds, suggesting that they act through a mechanism(s) different from glybenclamide. |
| 3946 | 18457421 | We have previously demonstrated the potent inhibitory potential of phenolsulfonphthalein, a nontoxic compound that was approved for diagnostic use in human subjects, on aggregation of islet amyloid polypeptide (IAPP) that is associated with type 2 diabetes. |
| 3947 | 18457421 | Differential activity was also observed in the inhibition of insulin amyloid formation by these two compounds, and density-gradient experiments clearly demonstrated the different inhibitory effect of the two compounds on the formation of prefibrillar assemblies. |
| 3948 | 18457421 | We have previously demonstrated the potent inhibitory potential of phenolsulfonphthalein, a nontoxic compound that was approved for diagnostic use in human subjects, on aggregation of islet amyloid polypeptide (IAPP) that is associated with type 2 diabetes. |
| 3949 | 18457421 | Differential activity was also observed in the inhibition of insulin amyloid formation by these two compounds, and density-gradient experiments clearly demonstrated the different inhibitory effect of the two compounds on the formation of prefibrillar assemblies. |
| 3950 | 18457428 | Rifampicin does not prevent amyloid fibril formation by human islet amyloid polypeptide but does inhibit fibril thioflavin-T interactions: implications for mechanistic studies of beta-cell death. |
| 3951 | 18457428 | Recent studies have highlighted the potential use of rifampicin as an inhibitor of amyloid formation by a variety of polypeptides; however, there are conflicting reports on its ability to inhibit amyloid formation by islet amyloid polypeptide (IAPP). |
| 3952 | 18457428 | Rifampicin does not prevent amyloid fibril formation by human islet amyloid polypeptide but does inhibit fibril thioflavin-T interactions: implications for mechanistic studies of beta-cell death. |
| 3953 | 18457428 | Recent studies have highlighted the potential use of rifampicin as an inhibitor of amyloid formation by a variety of polypeptides; however, there are conflicting reports on its ability to inhibit amyloid formation by islet amyloid polypeptide (IAPP). |
| 3954 | 18466898 | Therefore, the present study was designed to test the effects of the insulin-releasing gut hormone, glucagon-like peptide 1 (GLP-1). |
| 3955 | 18466898 | The injection of (Val8)GLP-1 (15 nmol i.c.v.) 30 min prior to injection of amyloid (25-35) (100 nmol i.c.v.) fully reversed the impairment of LTP induced by beta-amyloid. |
| 3956 | 18483477 | The aim of this study was to determine whether amyloid precursor protein (APP) is expressed in human adipose tissue, dysregulated in obesity, and related to insulin resistance and inflammation. |
| 3957 | 18483477 | APP expression correlated to in vivo indices of insulin resistance independently of BMI and with the expression of proinflammatory genes, such as monocyte chemoattractant protein-1 (MCP-1) (R=0.62, P=0.004), macrophage inflammatory protein-1alpha (MIP-1alpha) (R=0.60, P=0.005), and interleukin-6 (IL-6) (R=0.71, P=0.0005). |
| 3958 | 18483477 | In summary, APP is highly expressed in adipose tissue, upregulated in obesity, and expression levels correlate with insulin resistance and adipocyte cytokine expression levels. |
| 3959 | 18483477 | These data suggest a possible role for APP and/or Abeta in the development of obesity-related insulin resistance and adipose tissue inflammation. |
| 3960 | 18483616 | Recent insights in islet amyloid polypeptide-induced membrane disruption and its role in beta-cell death in type 2 diabetes mellitus. |
| 3961 | 18483616 | The presence of fibrillar protein deposits (amyloid) of human islet amyloid polypeptide (hIAPP) in the pancreatic islets of Langerhans is thought to be related to death of the insulin-producing islet beta-cells in type 2 diabetes mellitus (DM2). |
| 3962 | 18483616 | Recent insights in islet amyloid polypeptide-induced membrane disruption and its role in beta-cell death in type 2 diabetes mellitus. |
| 3963 | 18483616 | The presence of fibrillar protein deposits (amyloid) of human islet amyloid polypeptide (hIAPP) in the pancreatic islets of Langerhans is thought to be related to death of the insulin-producing islet beta-cells in type 2 diabetes mellitus (DM2). |
| 3964 | 18497871 | Human islet amyloid polypeptide transgenic mice: in vivo and ex vivo models for the role of hIAPP in type 2 diabetes mellitus. |
| 3965 | 18497871 | Human islet amyloid polypeptide (hIAPP), a pancreatic islet protein of 37 amino acids, is the main component of islet amyloid, seen at autopsy in patients with type 2 diabetes mellitus (DM2). |
| 3966 | 18497871 | To investigate the roles of hIAPP and islet amyloid in DM2, we generated transgenic mice expressing hIAPP in their islet beta cells. |
| 3967 | 18497871 | In this study, we found that after a long-term, high-fat diet challenge islet amyloid was observed in only 4 of 19 hIAPP transgenic mice. hIAPP transgenic females exhibited severe glucose intolerance, which was associated with a downregulation of GLUT-2 mRNA expression. |
| 3968 | 18497871 | Human islet amyloid polypeptide transgenic mice: in vivo and ex vivo models for the role of hIAPP in type 2 diabetes mellitus. |
| 3969 | 18497871 | Human islet amyloid polypeptide (hIAPP), a pancreatic islet protein of 37 amino acids, is the main component of islet amyloid, seen at autopsy in patients with type 2 diabetes mellitus (DM2). |
| 3970 | 18497871 | To investigate the roles of hIAPP and islet amyloid in DM2, we generated transgenic mice expressing hIAPP in their islet beta cells. |
| 3971 | 18497871 | In this study, we found that after a long-term, high-fat diet challenge islet amyloid was observed in only 4 of 19 hIAPP transgenic mice. hIAPP transgenic females exhibited severe glucose intolerance, which was associated with a downregulation of GLUT-2 mRNA expression. |
| 3972 | 18497871 | Human islet amyloid polypeptide transgenic mice: in vivo and ex vivo models for the role of hIAPP in type 2 diabetes mellitus. |
| 3973 | 18497871 | Human islet amyloid polypeptide (hIAPP), a pancreatic islet protein of 37 amino acids, is the main component of islet amyloid, seen at autopsy in patients with type 2 diabetes mellitus (DM2). |
| 3974 | 18497871 | To investigate the roles of hIAPP and islet amyloid in DM2, we generated transgenic mice expressing hIAPP in their islet beta cells. |
| 3975 | 18497871 | In this study, we found that after a long-term, high-fat diet challenge islet amyloid was observed in only 4 of 19 hIAPP transgenic mice. hIAPP transgenic females exhibited severe glucose intolerance, which was associated with a downregulation of GLUT-2 mRNA expression. |
| 3976 | 18497871 | Human islet amyloid polypeptide transgenic mice: in vivo and ex vivo models for the role of hIAPP in type 2 diabetes mellitus. |
| 3977 | 18497871 | Human islet amyloid polypeptide (hIAPP), a pancreatic islet protein of 37 amino acids, is the main component of islet amyloid, seen at autopsy in patients with type 2 diabetes mellitus (DM2). |
| 3978 | 18497871 | To investigate the roles of hIAPP and islet amyloid in DM2, we generated transgenic mice expressing hIAPP in their islet beta cells. |
| 3979 | 18497871 | In this study, we found that after a long-term, high-fat diet challenge islet amyloid was observed in only 4 of 19 hIAPP transgenic mice. hIAPP transgenic females exhibited severe glucose intolerance, which was associated with a downregulation of GLUT-2 mRNA expression. |
| 3980 | 18498175 | Effect of pressure on islet amyloid polypeptide aggregation: revealing the polymorphic nature of the fibrillation process. |
| 3981 | 18498175 | Type II diabetes mellitus is a disease which is characterized by peripheral insulin resistance coupled with a progressive loss of insulin secretion that is associated with a decrease in pancreatic islet beta-cell mass and the deposition of amyloid in the extracellular matrix of beta-cells, which lead to islet cell death. |
| 3982 | 18498175 | The principal component of the islet amyloid is a pancreatic hormone called islet amyloid polypeptide (IAPP). |
| 3983 | 18498175 | Effect of pressure on islet amyloid polypeptide aggregation: revealing the polymorphic nature of the fibrillation process. |
| 3984 | 18498175 | Type II diabetes mellitus is a disease which is characterized by peripheral insulin resistance coupled with a progressive loss of insulin secretion that is associated with a decrease in pancreatic islet beta-cell mass and the deposition of amyloid in the extracellular matrix of beta-cells, which lead to islet cell death. |
| 3985 | 18498175 | The principal component of the islet amyloid is a pancreatic hormone called islet amyloid polypeptide (IAPP). |
| 3986 | 18498175 | Effect of pressure on islet amyloid polypeptide aggregation: revealing the polymorphic nature of the fibrillation process. |
| 3987 | 18498175 | Type II diabetes mellitus is a disease which is characterized by peripheral insulin resistance coupled with a progressive loss of insulin secretion that is associated with a decrease in pancreatic islet beta-cell mass and the deposition of amyloid in the extracellular matrix of beta-cells, which lead to islet cell death. |
| 3988 | 18498175 | The principal component of the islet amyloid is a pancreatic hormone called islet amyloid polypeptide (IAPP). |
| 3989 | 18556473 | Atomic structure of the cross-beta spine of islet amyloid polypeptide (amylin). |
| 3990 | 18556473 | Human islet amyloid polypeptide (IAPP or amylin) is a 37-residue hormone found as fibrillar deposits in pancreatic extracts of nearly all type II diabetics. |
| 3991 | 18556473 | Atomic structure of the cross-beta spine of islet amyloid polypeptide (amylin). |
| 3992 | 18556473 | Human islet amyloid polypeptide (IAPP or amylin) is a 37-residue hormone found as fibrillar deposits in pancreatic extracts of nearly all type II diabetics. |
| 3993 | 18566678 | The role of the 14-20 domain of the islet amyloid polypeptide in amyloid formation. |
| 3994 | 18566678 | The molecular mechanism of amyloid formation by the islet amyloid polypeptide (IAPP) has been intensively studied since its identification in the late 1980s. |
| 3995 | 18566678 | The role of the 14-20 domain of the islet amyloid polypeptide in amyloid formation. |
| 3996 | 18566678 | The molecular mechanism of amyloid formation by the islet amyloid polypeptide (IAPP) has been intensively studied since its identification in the late 1980s. |
| 3997 | 18566681 | Real-time monitoring of apoptosis by caspase-3-like protease induced FRET reduction triggered by amyloid aggregation. |
| 3998 | 18584041 | Acute-phase serum amyloid A as a marker of insulin resistance in mice. |
| 3999 | 18584041 | Acute-phase serum amyloid A (A-SAA) was shown recently to correlate with obesity and insulin resistance in humans. |
| 4000 | 18584041 | Plasma A-SAA elevation was due to induction of Saa1 and Saa2 expression in liver but not in adipose tissue. |
| 4001 | 18584041 | Proinflammatory genes (Ccl2, Saa3) were induced while genes critical for insulin sensitivity (Irs1, Adipoq, Glut4) were down-regulated. |
| 4002 | 18584041 | Acute-phase serum amyloid A as a marker of insulin resistance in mice. |
| 4003 | 18584041 | Acute-phase serum amyloid A (A-SAA) was shown recently to correlate with obesity and insulin resistance in humans. |
| 4004 | 18584041 | Plasma A-SAA elevation was due to induction of Saa1 and Saa2 expression in liver but not in adipose tissue. |
| 4005 | 18584041 | Proinflammatory genes (Ccl2, Saa3) were induced while genes critical for insulin sensitivity (Irs1, Adipoq, Glut4) were down-regulated. |
| 4006 | 18603587 | When bound by its many ligands (which include advanced glycation endproducts, certain members of the S100/calgranulin family, extracellular high-mobility group box 1, the integrin Mac-1, amyloid beta-peptide and fibrils), RAGE activates programs responsible for acute and chronic inflammation. |
| 4007 | 18615201 | Disturbed alpha-cell function in mice with beta-cell specific overexpression of human islet amyloid polypeptide. |
| 4008 | 18615201 | Exogenous administration of islet amyloid polypeptide (IAPP) has been shown to inhibit both insulin and glucagon secretion. |
| 4009 | 18615201 | Disturbed alpha-cell function in mice with beta-cell specific overexpression of human islet amyloid polypeptide. |
| 4010 | 18615201 | Exogenous administration of islet amyloid polypeptide (IAPP) has been shown to inhibit both insulin and glucagon secretion. |
| 4011 | 18621727 | Molecular basis for the thiol sensitivity of insulin-degrading enzyme. |
| 4012 | 18621727 | Insulin-degrading enzyme (IDE) is a ubiquitous zinc-metalloprotease that hydrolyzes several pathophysiologically relevant peptides, including insulin and the amyloid beta-protein (Abeta). |
| 4013 | 18621727 | IDE is inhibited irreversibly by compounds that covalently modify cysteine residues, a mechanism that could be operative in the etiology of type 2 diabetes mellitus (DM2) or Alzheimer's disease (AD). |
| 4014 | 18621727 | Unexpectedly, alkylation of C590 was found to activate hydrolysis of Abeta significantly, while having no effect on insulin, demonstrating that chemical modulation of IDE can be both bidirectional and highly substrate selective. |
| 4015 | 18621727 | Our findings resolve a long-standing riddle about the basic enzymology of IDE with important implications for the etiology of DM2 and AD. |
| 4016 | 18624122 | In response to hyperglycemia, beta-cells release insulin and C-peptide, as well as islet amyloid pancreatic polypeptide - amylin. |
| 4017 | 18624122 | Amylin replacement with pramlintide as an adjunct to insulin therapy is a novel physiological approach toward improved long-term glycemic and weight control in patients with type 1 and type 2 diabetes. |
| 4018 | 18633116 | Spontaneous diabetes in hemizygous human amylin transgenic mice that developed neither islet amyloid nor peripheral insulin resistance. |
| 4019 | 18655073 | Insulin is a favored model for amyloid formation, not only because amyloidosis can be a problem in diabetes, but also because aggregation and fibrillation causes problems during production, storage, and delivery. |
| 4020 | 18665237 | Albumin has been implicated in Alzheimer's disease (AD) since it can bind to and transport amyloid beta (Abeta), the causative agent of AD; albumin is also a potent inhibitor of Abeta polymerization. |
| 4021 | 18665237 | These data indicate that microglial cells may play a beneficial role in AD by secreting albumin that not only inhibits Abeta polymerization but also increases its clearance. |
| 4022 | 18710262 | Human amylin, or islet amyloid polypeptide, is a peptide cosecreted with insulin by the beta cells of the pancreatic islets of Langerhans. |
| 4023 | 18723371 | The proinflammatory cytokine Interleukin 1 beta (IL-1beta) is elevated in obese individuals and rodents and it is implicated in impaired insulin secretion, decreased cell proliferation and apoptosis of pancreatic beta cells. |
| 4024 | 18723371 | After 13 weeks of treatment the IL-1beta antibody treated group showed reduced glycated hemoglobin (( *)P=0.049), reduced serum levels of proinsulin (( *)P=0.015), reduced levels of insulin and smaller islet size (( *)P=1.65E-13) relative to the control antibody treated group. |
| 4025 | 18723371 | Neutralization of IL-1beta also significantly reduced serum amyloid A (SAA) which is an indicator of inflammation-induced acute phase response (( *)P=0.024). |
| 4026 | 18765820 | Interaction of membrane-bound islet amyloid polypeptide with soluble and crystalline insulin. |
| 4027 | 18765820 | Islet amyloid polypeptide (IAPP, also known as amylin) is the major protein component of pancreatic amyloid fibers in type II diabetes and is normally cosecreted with insulin from the beta-cells of the pancreas. |
| 4028 | 18765820 | In this work, we investigate insulin-IAPP-lipid interactions in vitro under conditions chosen to approximate native secretory vesicle physiology and the amyloid disease state. |
| 4029 | 18765820 | Interaction of membrane-bound islet amyloid polypeptide with soluble and crystalline insulin. |
| 4030 | 18765820 | Islet amyloid polypeptide (IAPP, also known as amylin) is the major protein component of pancreatic amyloid fibers in type II diabetes and is normally cosecreted with insulin from the beta-cells of the pancreas. |
| 4031 | 18765820 | In this work, we investigate insulin-IAPP-lipid interactions in vitro under conditions chosen to approximate native secretory vesicle physiology and the amyloid disease state. |
| 4032 | 18765820 | Interaction of membrane-bound islet amyloid polypeptide with soluble and crystalline insulin. |
| 4033 | 18765820 | Islet amyloid polypeptide (IAPP, also known as amylin) is the major protein component of pancreatic amyloid fibers in type II diabetes and is normally cosecreted with insulin from the beta-cells of the pancreas. |
| 4034 | 18765820 | In this work, we investigate insulin-IAPP-lipid interactions in vitro under conditions chosen to approximate native secretory vesicle physiology and the amyloid disease state. |
| 4035 | 18777156 | Our aim was to study, at the same glycemic control, how treatment with either the insulin secretagogue repaglinide or exogenous insulin aspart affects endogenous insulin secretion, plasma insulin and IAPP (islet amyloid polypeptide) levels, GH-IGF (growth hormone-insulin-like growth factor) axis and plasma lipoprotein concentrations in patients with type 2 diabetes. |
| 4036 | 18777156 | Blood glucose, C-peptide, free human insulin, free total (human and analogue) insulin, proinsulin, IAPP, IGF-I, IGFBP-1 (IGF binding protein-1), GHBP (growth hormone binding protein) and plasma lipoprotein concentrations were measured. |
| 4037 | 18777156 | Proinsulin, GHBP were higher and IAPP levels tended to be higher during repaglinide compared to insulin aspart. |
| 4038 | 18777156 | Postprandial plasma total cholesterol, triglycerides and apolipoprotein B concentrations were higher on repaglinide than on insulin aspart treatment. |
| 4039 | 18788162 | The cytoplasm of B cells and extracellular amyloid display immunohistological binding of anti-insulin antibody. |
| 4040 | 18788162 | Correspondingly, ferritin-labeled anti-insulin antibody was found by electron microscopy on and between the amyloid fibrils. |
| 4041 | 18788162 | Insulin or proinsulin (or a protein closely related to insulin) thus appears to be a component of the protein which constitutes the amyloid. |
| 4042 | 18788162 | The cytoplasm of B cells and extracellular amyloid display immunohistological binding of anti-insulin antibody. |
| 4043 | 18788162 | Correspondingly, ferritin-labeled anti-insulin antibody was found by electron microscopy on and between the amyloid fibrils. |
| 4044 | 18788162 | Insulin or proinsulin (or a protein closely related to insulin) thus appears to be a component of the protein which constitutes the amyloid. |
| 4045 | 18788162 | The cytoplasm of B cells and extracellular amyloid display immunohistological binding of anti-insulin antibody. |
| 4046 | 18788162 | Correspondingly, ferritin-labeled anti-insulin antibody was found by electron microscopy on and between the amyloid fibrils. |
| 4047 | 18788162 | Insulin or proinsulin (or a protein closely related to insulin) thus appears to be a component of the protein which constitutes the amyloid. |
| 4048 | 18813861 | Therefore, we directly investigated exercise training to determine whether it was able to ameliorate the molecular pathogenic phenotypes in the brain using a neuron-specific enolase (NSE)/Swedish mutation of amyloid precursor protein (APPsw) transgenic (Tg) mice as a novel AD model. |
| 4049 | 18813861 | The results indicated (i) that amyloid beta-42 (Abeta-42) peptides were significantly decreased in the NSE/APPsw Tg mice following exercise training; (ii) that exercise training inhibited the apoptotic biochemical cascades, including cytochrome c, caspase-9, caspase-3 and Bax; (iii) that the glucose transporter-1 (GLUT-1) and brain-derived neurotrophic factor (BDNF) proteins induced by exercise training protected the neurons from injury by inducing the concomitant expression of genes that encode proteins such as superoxide dismutase-1 (SOD-1), catalase and Bcl-2, which suppress oxidative stress and excitotoxic injury; (iv) that heat-shock protein-70 (HSP-70) and glucose-regulated protein-78 (GRP-78) were significantly increased in the exercise (EXE) group when compared to the sedentary (SED) group, and that these proteins may benefit the brain by making it more resistant to stress-induced neuron cell damage; (v) and that exercise training contributed to the restoration of normal levels of serum total cholesterol, insulin and glucose. |
| 4050 | 18813861 | Therefore, we directly investigated exercise training to determine whether it was able to ameliorate the molecular pathogenic phenotypes in the brain using a neuron-specific enolase (NSE)/Swedish mutation of amyloid precursor protein (APPsw) transgenic (Tg) mice as a novel AD model. |
| 4051 | 18813861 | The results indicated (i) that amyloid beta-42 (Abeta-42) peptides were significantly decreased in the NSE/APPsw Tg mice following exercise training; (ii) that exercise training inhibited the apoptotic biochemical cascades, including cytochrome c, caspase-9, caspase-3 and Bax; (iii) that the glucose transporter-1 (GLUT-1) and brain-derived neurotrophic factor (BDNF) proteins induced by exercise training protected the neurons from injury by inducing the concomitant expression of genes that encode proteins such as superoxide dismutase-1 (SOD-1), catalase and Bcl-2, which suppress oxidative stress and excitotoxic injury; (iv) that heat-shock protein-70 (HSP-70) and glucose-regulated protein-78 (GRP-78) were significantly increased in the exercise (EXE) group when compared to the sedentary (SED) group, and that these proteins may benefit the brain by making it more resistant to stress-induced neuron cell damage; (v) and that exercise training contributed to the restoration of normal levels of serum total cholesterol, insulin and glucose. |
| 4052 | 18825272 | Transthyretin and amyloid in the islets of Langerhans in type-2 diabetes. |
| 4053 | 18825272 | Transthyretin (TTR) is a major amyloid fibril protein in certain systemic forms of amyloidosis. |
| 4054 | 18825272 | A weak transthyretin immunoreaction in IAPP-derived amyloid occurred in some specimens. |
| 4055 | 18825272 | In seeding experiments in vitro, we found that TTR fibrils did not seed IAPP while IAPP fibrils seeded TTR. |
| 4056 | 18825272 | Transthyretin and amyloid in the islets of Langerhans in type-2 diabetes. |
| 4057 | 18825272 | Transthyretin (TTR) is a major amyloid fibril protein in certain systemic forms of amyloidosis. |
| 4058 | 18825272 | A weak transthyretin immunoreaction in IAPP-derived amyloid occurred in some specimens. |
| 4059 | 18825272 | In seeding experiments in vitro, we found that TTR fibrils did not seed IAPP while IAPP fibrils seeded TTR. |
| 4060 | 18825272 | Transthyretin and amyloid in the islets of Langerhans in type-2 diabetes. |
| 4061 | 18825272 | Transthyretin (TTR) is a major amyloid fibril protein in certain systemic forms of amyloidosis. |
| 4062 | 18825272 | A weak transthyretin immunoreaction in IAPP-derived amyloid occurred in some specimens. |
| 4063 | 18825272 | In seeding experiments in vitro, we found that TTR fibrils did not seed IAPP while IAPP fibrils seeded TTR. |
| 4064 | 18855585 | Peripheral hyperinsulinemia correlates with an abnormal removal of the amyloid beta peptide (Abeta) and an increase of tau hyperphosphorylation as a result of augmented cdk5 and GSK3beta activities. |
| 4065 | 18922715 | We show examples of low-temperature (13)C NMR data for two biomolecular samples, namely the peptide Abeta(14-23) in the form of amyloid fibrils and the protein HP35 in frozen glycerol/water solution. |
| 4066 | 18936727 | In addition to advanced glycation end products (AGEs), RAGE binds amphoterin, S100/calgranulin, amyloid, transthyretin, and a leukocyte integrin, Mac-1. |
| 4067 | 18989932 | Structures of rat and human islet amyloid polypeptide IAPP(1-19) in micelles by NMR spectroscopy. |
| 4068 | 18989933 | A single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicity. |
| 4069 | 18989933 | Islet amyloid polypeptide (IAPP or amylin) is a 37-residue peptide secreted with insulin by beta-cells in the islets of Langerhans. |
| 4070 | 18989933 | A single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicity. |
| 4071 | 18989933 | Islet amyloid polypeptide (IAPP or amylin) is a 37-residue peptide secreted with insulin by beta-cells in the islets of Langerhans. |
| 4072 | 18991244 | The effects of the different egg diets on apolipoprotein A1 and B (Apo A1 and B), lipoprotein (a), creatinine, cystatin C, C-reactive protein, serum amyloid protein A, interleukin 6, triglycerides, glucose, total-, high-density lipoprotein and low-density lipo-protein cholesterol concentrations were analyzed. |
| 4073 | 18991244 | Consumption of omega-3 enriched eggs resulted in higher levels of ApoA1, lower ApoB/ApoA1 ratio and lower plasma glucose. |
| 4074 | 18998217 | Rosiglitazone, peroxisome proliferator-activated receptor-gamma agonist, is an insulin sensitizing agent in peripheral tissues. |
| 4075 | 18998217 | There were significant differences in cocaine- and amphetamine-regulated transcript (CART) and pancreatic polypeptide (PP) cell numbers between rosiglitazone control group and rosiglitazone + STZ-diabetic group. |
| 4076 | 18998217 | We found a statistically significant difference in islet amyloid polypeptide (IAPP) mRNA signals between the STZ-diabetic group and the rosiglitazone + STZ-diabetic group. |
| 4077 | 19026743 | For instance, in AD the accumulation of the amyloid-beta peptide (Abeta), which characterizes the disease and is thought to participate in the neurodegenerative process, may also induce neuronal insulin resistance. |
| 4078 | 19026743 | Conversely, disrupting normal glucose metabolism in transgenic animal models of AD that over-express the human amyloid precursor protein (hAPP) promotes amyloid-peptide aggregation and accelerates the disease progression. |
| 4079 | 19026743 | Studying these processes at a cellular level suggests that insulin resistance and Abeta aggregation may not only be the consequence of excitotoxicity, aberrant Ca(2+) signals, and proinflammatory cytokines such as TNF-alpha, but may also promote these pathological effectors. |
| 4080 | 19026743 | At the molecular level, insulin resistance and Abeta disrupt common signal transduction cascades including the insulin receptor family/PI3 kinase/Akt/GSK3 pathway. |
| 4081 | 19038266 | Abeta(1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils. |
| 4082 | 19038266 | Alzheimer's amyloid fibrils consist of amyloid-beta (Abeta) peptide and occur in a range of structurally different fibril morphologies. |
| 4083 | 19038266 | The structural characteristics of 12 single Abeta(1-40) amyloid fibrils, all formed under the same solution conditions, were determined by electron cryo-microscopy and three-dimensional reconstruction. |
| 4084 | 19038266 | Abeta(1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils. |
| 4085 | 19038266 | Alzheimer's amyloid fibrils consist of amyloid-beta (Abeta) peptide and occur in a range of structurally different fibril morphologies. |
| 4086 | 19038266 | The structural characteristics of 12 single Abeta(1-40) amyloid fibrils, all formed under the same solution conditions, were determined by electron cryo-microscopy and three-dimensional reconstruction. |
| 4087 | 19038266 | Abeta(1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils. |
| 4088 | 19038266 | Alzheimer's amyloid fibrils consist of amyloid-beta (Abeta) peptide and occur in a range of structurally different fibril morphologies. |
| 4089 | 19038266 | The structural characteristics of 12 single Abeta(1-40) amyloid fibrils, all formed under the same solution conditions, were determined by electron cryo-microscopy and three-dimensional reconstruction. |
| 4090 | 19100955 | The amyloid hypothesis of type 2 diabetes mellitus postulates that elevated levels of normally expressed monomeric proteins of human islet amyloid polypeptide (hIAPP) trigger oligomerization that independently causes fibril formation and disease progression. |
| 4091 | 19100955 | Several markers for insulin, IAPP, amyloid fibrils (thioflavin T), and apoptosis (cleaved caspase-3) were used in combination with an oligomer-specific antibody. |
| 4092 | 19100955 | The amyloid hypothesis of type 2 diabetes mellitus postulates that elevated levels of normally expressed monomeric proteins of human islet amyloid polypeptide (hIAPP) trigger oligomerization that independently causes fibril formation and disease progression. |
| 4093 | 19100955 | Several markers for insulin, IAPP, amyloid fibrils (thioflavin T), and apoptosis (cleaved caspase-3) were used in combination with an oligomer-specific antibody. |
| 4094 | 19117266 | BACE2 is a protease homologous to BACE1 protein, an enzyme involved in the amyloid formation of Alzheimer disease (AD). |
| 4095 | 19117266 | BACE2 immunoreactivity was found in secretory granules of beta cells, co-stored with insulin and IAPP, while it was lacking in the other endocrine and exocrine cell types. |
| 4096 | 19135149 | Whereas insulin is clearly neurothrophic at moderate concentrations, too much insulin in the brain may be associated with reduced amyloid-beta (Abeta) clearance due to competition for their common and main depurative mechanism - the Insulin-Degrading Enzyme (IDE). |
| 4097 | 19135149 | Since IDE is much more selective for insulin than for Abeta, brain hyperinsulinism may deprive Abeta of its main clearance mechanism. |
| 4098 | 19135149 | Hyperglycemia and hyperinsulinemia seems to accelerate brain aging also by inducing tau hyperphosphorylation and amyloid oligomerization, as well as by leading to widespread brain microangiopathy. |
| 4099 | 19165839 | Inhibiting islet amyloid polypeptide fibril formation by the red wine compound resveratrol. |
| 4100 | 19188609 | Protection of synapses against Alzheimer's-linked toxins: insulin signaling prevents the pathogenic binding of Abeta oligomers. |
| 4101 | 19188609 | Synapse deterioration underlying severe memory loss in early Alzheimer's disease (AD) is thought to be caused by soluble amyloid beta (Abeta) oligomers. |
| 4102 | 19188609 | Before spine loss, ADDLs caused major downregulation of plasma membrane insulin receptors (IRs), via a mechanism sensitive to calcium calmodulin-dependent kinase II (CaMKII) and casein kinase II (CK2) inhibition. |
| 4103 | 19195555 | Amylin, a 37-amino acid peptide hormone produced and secreted by pancreatic beta-cells, is the principal constituent of amyloid deposits in Type II Diabetes Mellitus (TTDM). |
| 4104 | 19208933 | Important examples of the latter include the Abeta peptide of Alzheimer's disease, atrial natriuretic factor, calcitonin, pro-calcitonin, islet amyloid polypeptide (IAPP, amylin), alpha-synuclein and the medin polypeptide. |
| 4105 | 19229175 | Here, we demonstrate application of PICUP to cross-linking of three amyloidogenic proteins the 40- and 42-residue amyloid beta-protein variants (Abeta40 and Abeta42), and calcitonin, and a control protein, growth-hormone releasing factor (GRF). |
| 4106 | 19237574 | Antidiabetic drug metformin (GlucophageR) increases biogenesis of Alzheimer's amyloid peptides via up-regulating BACE1 transcription. |
| 4107 | 19237574 | Insulin modulates metabolism of beta-amyloid precursor protein (APP) in neurons, decreasing the intracellular accumulation of beta-amyloid (Abeta) peptides, which are pivotal in AD pathogenesis. |
| 4108 | 19237574 | The present study investigates whether the widely prescribed insulin-sensitizing drug, metformin (Glucophage(R)), affects APP metabolism and Abeta generation in various cell models. |
| 4109 | 19237574 | We demonstrate that metformin, at doses that lead to activation of the AMP-activated protein kinase (AMPK), significantly increases the generation of both intracellular and extracellular Abeta species. |
| 4110 | 19237574 | Furthermore, the effect of metformin on Abeta generation is mediated by transcriptional up-regulation of beta-secretase (BACE1), which results in an elevated protein level and increased enzymatic activity. |
| 4111 | 19237574 | Unlike insulin, metformin exerts no effect on Abeta degradation. |
| 4112 | 19237574 | In addition, we found that glucose deprivation and various tyrphostins, known inhibitors of insulin-like growth factors/insulin receptor tyrosine kinases, do not modulate the effect of metformin on Abeta. |
| 4113 | 19237574 | Finally, inhibition of AMP-activated protein kinase (AMPK) by the pharmacological inhibitor Compound C largely suppresses metformin's effect on Abeta generation and BACE1 transcription, suggesting an AMPK-dependent mechanism. |
| 4114 | 19237574 | Although insulin and metformin display opposing effects on Abeta generation, in combined use, metformin enhances insulin's effect in reducing Abeta levels. |
| 4115 | 19244088 | Serum amyloid A, C-reactive protein, and retinal microvascular changes in hypertensive diabetic and nondiabetic individuals: an Anglo-Scandinavian Cardiac Outcomes Trial (ASCOT) substudy. |
| 4116 | 19277203 | More than 10 years ago, we demonstrated that amyloid deposits rapidly formed in human islets and in mouse islets transgenic for human IAPP when grafted into nude mice. |
| 4117 | 19278224 | Induction of negative curvature as a mechanism of cell toxicity by amyloidogenic peptides: the case of islet amyloid polypeptide. |
| 4118 | 19322705 | Epidemiological evidence accruing in the human suggests upregulation of RAGE's ligands (AGEs, S100/calgranulins, high mobility group box-1 (HMGB1), and amyloid beta-peptide and beta-sheet fibrils) and the receptor itself at sites of inflammation and in chronic diseases such as diabetes and neurodegeneration. |
| 4119 | 19343195 | Importance of aggregated islet amyloid polypeptide for the progressive beta-cell failure in type 2 diabetes and in transplanted human islets. |
| 4120 | 19346479 | Using a recently invented method of collecting 2-dimensional infrared spectra and site-specific isotope labeling, we have measured the development of secondary structures for 6 residues during the aggregation process of the 37-residue polypeptide associated with type 2 diabetes, the human islet amyloid polypeptide (hIAPP). |
| 4121 | 19364070 | Engrafted beta-cells showed positive carboxypeptidase E (CPE) and prohormone convertase 1 (PC1) staining, while prohormone convertase 2 (PC2) was undetectable. |
| 4122 | 19364070 | Cell cycle inhibitors p16(INK4), p21(WAF1), and p27(Kip1) were abundantly expressed in the islet grafts and showed a predominant nuclear localization. |
| 4123 | 19364070 | In conclusion, diabetic nude mice transplanted with human islets showed disproportionate hyperproinsulinemia and graft evidence of beta-cell restricted PC2 depletion, amyloid deposition and beta-cell death, and lack of beta-cell replication with nuclear translocation of p27(Kip1) and p21(WAF1) that together may contribute to delayed graft failure. |
| 4124 | 19374013 | The principal component of the amyloid deposits in Alzheimer's disease is the beta-amyloid polypeptide, while in type II diabetes the deposits consist primarily of Islet amyloid polypeptide. |
| 4125 | 19376202 | Hippocampal caspase-3+ and beta amyloid (Abeta+) cell numbers, as well as beta-site amyloid precursor protein-cleaving enzyme (BACE1) levels and activity, increased in both groups. |
| 4126 | 19376202 | Moreover, HFD-STZ treatment exacerbated stroke-induced cognitive deficits, additively increased MCAO-induced activation of caspase-3, and increased levels of BACE1, C99 and Abeta. |
| 4127 | 19376202 | We concluded that type 2 diabetes exacerbated poststroke dementia possibly due to brain injury and synergistic generation of Abeta via activation of BACE1. |
| 4128 | 19376973 | Studies by solid-state nuclear magnetic resonance (NMR) of amyloid fibrils prepared in vitro from synthetic 40-residue beta-amyloid (Abeta(1-40)) peptides have shown that the molecular structure of Abeta(1-40) fibrils is not uniquely determined by amino acid sequence. |
| 4129 | 19376973 | Because amyloid structures propagate themselves in seeded growth, as shown in previous studies, the molecular structures of brain-seeded synthetic Abeta(1-40) fibrils most likely reflect structures that are present in AD brain. |
| 4130 | 19376973 | Studies by solid-state nuclear magnetic resonance (NMR) of amyloid fibrils prepared in vitro from synthetic 40-residue beta-amyloid (Abeta(1-40)) peptides have shown that the molecular structure of Abeta(1-40) fibrils is not uniquely determined by amino acid sequence. |
| 4131 | 19376973 | Because amyloid structures propagate themselves in seeded growth, as shown in previous studies, the molecular structures of brain-seeded synthetic Abeta(1-40) fibrils most likely reflect structures that are present in AD brain. |
| 4132 | 19379129 | Moreover, the presence of inductive factors in the Matrigel plus exendin-4 led to an increase in Pdx1 and endocrine genes, such as insulin, islet amyloid polypeptide, glucagon, the glucose transporter GLUT2, chromogranin A and the convertases PC1/3 and PC2 were also detected. |
| 4133 | 19379129 | We identified a population of PaSCs that express the ABCG2+ transporter and have the capacity to transdifferentiate into insulin-producing cells. |
| 4134 | 19402658 | Conformation preorganization: effects of S20G mutation on the structure of human islet amyloid polypeptide segment. |
| 4135 | 19402658 | The missense mutation S20G in the human islet amyloid polypeptide (hIAPP) is supposed to be associated with the early onset of type II diabetes (T2DM) in Asian population. |
| 4136 | 19402658 | Conformation preorganization: effects of S20G mutation on the structure of human islet amyloid polypeptide segment. |
| 4137 | 19402658 | The missense mutation S20G in the human islet amyloid polypeptide (hIAPP) is supposed to be associated with the early onset of type II diabetes (T2DM) in Asian population. |
| 4138 | 19403868 | Beneficial endocrine but adverse exocrine effects of sitagliptin in the human islet amyloid polypeptide transgenic rat model of type 2 diabetes: interactions with metformin. |
| 4139 | 19405534 | Association of highly compact type II diabetes related islet amyloid polypeptide intermediate species at physiological temperature revealed by diffusion NMR spectroscopy. |
| 4140 | 19405534 | Self-association of human islet amyloid polypeptide (hIAPP) is correlated with the development of type II diabetes by the disruption of cellular homeostasis in islet cells through the formation of membrane-active oligomers. |
| 4141 | 19405534 | Association of highly compact type II diabetes related islet amyloid polypeptide intermediate species at physiological temperature revealed by diffusion NMR spectroscopy. |
| 4142 | 19405534 | Self-association of human islet amyloid polypeptide (hIAPP) is correlated with the development of type II diabetes by the disruption of cellular homeostasis in islet cells through the formation of membrane-active oligomers. |
| 4143 | 19413589 | Imbalanced generation of the Abeta42 peptide from the amyloid beta protein precursor (APP) is implicated in the pathogenesis of Alzheimer's disease. 2. |
| 4144 | 19427320 | Human islet amyloid polypeptide (hIAPP), which is considered the primary culprit for beta-cell loss in type 2 diabetes mellitus patients, is synthesized in beta-cells of the pancreas from its precursor pro-islet amyloid polypeptide (proIAPP), which may be important in early intracellular amyloid formation as well. |
| 4145 | 19456151 | Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy. |
| 4146 | 19456151 | Islet amyloid polypeptide (IAPP or amylin) is a 37-residue peptide hormone associated with glucose metabolism that is cosecreted with insulin by beta-cells in the pancreas. |
| 4147 | 19456151 | Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy. |
| 4148 | 19456151 | Islet amyloid polypeptide (IAPP or amylin) is a 37-residue peptide hormone associated with glucose metabolism that is cosecreted with insulin by beta-cells in the pancreas. |
| 4149 | 19461118 | Furthermore, both statins reduced expression of microtubule-associated protein tau in astrocytes (P < 0.01), while both statins increased its expression in neuroblastoma cells (P < 0.01). |
| 4150 | 19461118 | In SK-N-SH cells, simvastatin significantly increased cyclin-dependent kinase 5 and glycogen synthase kinase 3beta expression, while pravastatin increased amyloid precursor protein expression. |
| 4151 | 19470833 | Type 2 diabetes is characterized by hyperglycemia, a deficit in beta-cells, increased beta-cell apoptosis, and islet amyloid derived from islet amyloid polypeptide (IAPP). |
| 4152 | 19474523 | Serum amyloid A attenuates cellular insulin sensitivity by increasing JNK activity in 3T3-L1 adipocytes. |
| 4153 | 19474523 | A permanent increase in acute-phase serum amyloid A (A-SAA) level is observed in obesity and insulin resistance. |
| 4154 | 19474523 | In this study, we used two cellular models of insulin resistance, one induced by treatment with tumor necrosis factor-alpha (TNF-alpha) and the other with the glucocorticoid dexamethasone. |
| 4155 | 19474523 | Gene expression analysis showed that SAA3 mRNA levels were increased in both models of insulin resistance, and ELISA showed that A-SAA levels were increased in both models too. |
| 4156 | 19474523 | To assess the potential impact of A-SAA on insulin resistance, we treated 3T3-L1 adipocytes with recombinant human SAA (Rh-SAA) and found that Rh-SAA attenuated cellular insulin sensitivity, up-regulated the level of phosphor-JNK, and down-regulated the level of phosphotyrosine-IRS-1 and the expression of glucose transporter 4 (GLUT4) in 3T3-L1 adipocytes. |
| 4157 | 19474523 | Pre-treatment of cells with C-Jun amino-terminal kinases (JNK) inhibitor brought about partial restoration of Rh-SAA-induced insulin resistance. |
| 4158 | 19474523 | In sum, our findings suggest that serum amyloid A might be a marker of insulin resistance, and it might play a major role in the development of obesity-related insulin resistance. |
| 4159 | 19474523 | Moreover, in our study it has been proved that JNK is indeed a crucial component of the pathway responsible for SAA-induced insulin resistance in 3T3-L1 adipocytes, which suggests that a selective interference with JNK activity might be a useful strategy in the treatment of Type 2 diabetes and other insulin-resistant states. |
| 4160 | 19474523 | Serum amyloid A attenuates cellular insulin sensitivity by increasing JNK activity in 3T3-L1 adipocytes. |
| 4161 | 19474523 | A permanent increase in acute-phase serum amyloid A (A-SAA) level is observed in obesity and insulin resistance. |
| 4162 | 19474523 | In this study, we used two cellular models of insulin resistance, one induced by treatment with tumor necrosis factor-alpha (TNF-alpha) and the other with the glucocorticoid dexamethasone. |
| 4163 | 19474523 | Gene expression analysis showed that SAA3 mRNA levels were increased in both models of insulin resistance, and ELISA showed that A-SAA levels were increased in both models too. |
| 4164 | 19474523 | To assess the potential impact of A-SAA on insulin resistance, we treated 3T3-L1 adipocytes with recombinant human SAA (Rh-SAA) and found that Rh-SAA attenuated cellular insulin sensitivity, up-regulated the level of phosphor-JNK, and down-regulated the level of phosphotyrosine-IRS-1 and the expression of glucose transporter 4 (GLUT4) in 3T3-L1 adipocytes. |
| 4165 | 19474523 | Pre-treatment of cells with C-Jun amino-terminal kinases (JNK) inhibitor brought about partial restoration of Rh-SAA-induced insulin resistance. |
| 4166 | 19474523 | In sum, our findings suggest that serum amyloid A might be a marker of insulin resistance, and it might play a major role in the development of obesity-related insulin resistance. |
| 4167 | 19474523 | Moreover, in our study it has been proved that JNK is indeed a crucial component of the pathway responsible for SAA-induced insulin resistance in 3T3-L1 adipocytes, which suggests that a selective interference with JNK activity might be a useful strategy in the treatment of Type 2 diabetes and other insulin-resistant states. |
| 4168 | 19474523 | Serum amyloid A attenuates cellular insulin sensitivity by increasing JNK activity in 3T3-L1 adipocytes. |
| 4169 | 19474523 | A permanent increase in acute-phase serum amyloid A (A-SAA) level is observed in obesity and insulin resistance. |
| 4170 | 19474523 | In this study, we used two cellular models of insulin resistance, one induced by treatment with tumor necrosis factor-alpha (TNF-alpha) and the other with the glucocorticoid dexamethasone. |
| 4171 | 19474523 | Gene expression analysis showed that SAA3 mRNA levels were increased in both models of insulin resistance, and ELISA showed that A-SAA levels were increased in both models too. |
| 4172 | 19474523 | To assess the potential impact of A-SAA on insulin resistance, we treated 3T3-L1 adipocytes with recombinant human SAA (Rh-SAA) and found that Rh-SAA attenuated cellular insulin sensitivity, up-regulated the level of phosphor-JNK, and down-regulated the level of phosphotyrosine-IRS-1 and the expression of glucose transporter 4 (GLUT4) in 3T3-L1 adipocytes. |
| 4173 | 19474523 | Pre-treatment of cells with C-Jun amino-terminal kinases (JNK) inhibitor brought about partial restoration of Rh-SAA-induced insulin resistance. |
| 4174 | 19474523 | In sum, our findings suggest that serum amyloid A might be a marker of insulin resistance, and it might play a major role in the development of obesity-related insulin resistance. |
| 4175 | 19474523 | Moreover, in our study it has been proved that JNK is indeed a crucial component of the pathway responsible for SAA-induced insulin resistance in 3T3-L1 adipocytes, which suggests that a selective interference with JNK activity might be a useful strategy in the treatment of Type 2 diabetes and other insulin-resistant states. |
| 4176 | 19478200 | MIF deficiency reduces chronic inflammation in white adipose tissue and impairs the development of insulin resistance, glucose intolerance, and associated atherosclerotic disease. |
| 4177 | 19478200 | This study examines whether MIF is required for the development of obesity, IR, glucose intolerance, and atherosclerosis in the LDL receptor-deficient (Ldlr(-/-)) mouse model of disease. |
| 4178 | 19478200 | Ldlr(-/-) mice develop IR and glucose intolerance within 15 weeks, whereas Mif(-/-)Ldlr(-/-) littermates are protected. |
| 4179 | 19478200 | MIF deficiency does not affect obesity and lipid risk factors but specifically reduces inflammation in WAT and liver, as reflected by lower plasma serum amyloid A and fibrinogen levels at baseline and under inflammatory conditions. |
| 4180 | 19478200 | Conversely, MIF stimulates the in vivo expression of human C-reactive protein, an inflammation marker and risk factor of IR and cardiovascular disease. |
| 4181 | 19478200 | In WAT, MIF deficiency reduces nuclear c-Jun levels and improves insulin sensitivity; MIF deficiency also reduces macrophage accumulation in WAT and blunts the expression of two proteins that regulate macrophage infiltration (intercellular adhesion molecule-1, CD44). |
| 4182 | 19498343 | Plasma concentrations of the acute-phase reactant serum amyloid A (SAA) are elevated in both obesity and cardiovascular disease. |
| 4183 | 19498343 | Moreover, SAA was localized with apoB-containing lipoproteins and biglycan in the vascular wall. |
| 4184 | 19498343 | Taken together, these data suggest male apoE-deficient mice are a model of metabolic syndrome and that chronic low level inflammation associated with increased SAA concentrations may mediate atherosclerotic lesion formation. |
| 4185 | 19523795 | DHA is specifically protective against AD via additional mechanisms: It limits the production and accumulation of the amyloid beta peptide toxin that is widely believed to drive the disease; and it also suppresses several signal transduction pathways induced by Abeta, including two major kinases that phosphorylate the microtubule-associated protein tau and promote neurofibrillary tangle pathology. |
| 4186 | 19541956 | However, amyloids may also have a normal biological function, as demonstrated by fungal prions, which are involved in prion replication, and the amyloid protein Pmel17, which is involved in mammalian skin pigmentation. |
| 4187 | 19556854 | This activity, which minimally requires Hsp70 and its co-chaperone Hsp40, is essential for yeast prion replication. |
| 4188 | 19556854 | We discuss the variety of effects Hsp70 and its regulators have on different prions and how the effects might be due to the many ways chaperones interact with each other and with amyloid. |
| 4189 | 19583433 | The islet amyloid polypeptide (IAPP) or amylin is a pancreatic hormone and crucially involved in the pathogenesis of type-II diabetes mellitus (T2DM). |
| 4190 | 19597329 | Structural polymorphism of Alzheimer Abeta and other amyloid fibrils. |
| 4191 | 19616077 | Role of the JNK-interacting protein 1/islet brain 1 in cell degeneration in Alzheimer disease and diabetes. |
| 4192 | 19616077 | Deposits of amyloid aggregate and hyperphosphorylation of tau, which are hallmarks of AD, have been also found in degenerating pancreatic islets beta-cells of patients with T2D. |
| 4193 | 19616077 | Increased c-Jun NH(2)-terminal kinase (JNK) activity is found in neurofibrillary tangles (NFT) of AD and promotes programmed cell death of beta-cells exposed to a diabetic environment. |
| 4194 | 19616077 | The JNK-interacting protein 1 (JIP-1), also called islet brain 1 (IB1) because it is mostly expressed in the brain and islets, is a key regulator of the JNK pathway in neuronal and beta-cells. |
| 4195 | 19616077 | JNK, hyperphosphorylated tau and IB1/JIP-1 all co-localize with amyloids deposits in NFT and islets of AD and patients with T2D. |
| 4196 | 19616077 | This review discusses the role of the IB1/JIP-1 and the JNK pathway in the molecular pathogenesis of AD and T2D. |
| 4197 | 19647738 | Ganglioside-induced amyloid formation by human islet amyloid polypeptide in lipid rafts. |
| 4198 | 19647738 | Human islet amyloid polypeptide (hIAPP) is the primary component of the amyloid deposits found in the pancreatic islets of patients with type 2 diabetes mellitus. |
| 4199 | 19647738 | Ganglioside-induced amyloid formation by human islet amyloid polypeptide in lipid rafts. |
| 4200 | 19647738 | Human islet amyloid polypeptide (hIAPP) is the primary component of the amyloid deposits found in the pancreatic islets of patients with type 2 diabetes mellitus. |
| 4201 | 19647750 | Helix stabilization precedes aqueous and bilayer-catalyzed fiber formation in islet amyloid polypeptide. |
| 4202 | 19647750 | Islet amyloid polypeptide (IAPP) is an unstructured polypeptide hormone that is cosecreted with insulin. |
| 4203 | 19647750 | Helix stabilization precedes aqueous and bilayer-catalyzed fiber formation in islet amyloid polypeptide. |
| 4204 | 19647750 | Islet amyloid polypeptide (IAPP) is an unstructured polypeptide hormone that is cosecreted with insulin. |
| 4205 | 19666488 | The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis. |
| 4206 | 19666488 | We suggest that RPT is the amyloid core domain of the Pmel17 filaments so critical for melanin formation. |
| 4207 | 19666488 | The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis. |
| 4208 | 19666488 | We suggest that RPT is the amyloid core domain of the Pmel17 filaments so critical for melanin formation. |
| 4209 | 19669260 | An HNF1alpha germline mutation is observed in less than 5% of HCA cases and can be associated with MODY 3 diabetes. (2) An activating beta-catenin mutation was found in 10% of HCA. |
| 4210 | 19669260 | These beta-catenin activated HCAs are observed in men and women, and specific risk factors, such as male hormone administration or glycogenosis, are associated with their development. |
| 4211 | 19669260 | Immunohistochemistry studies show that these HCAs overexpress beta-catenin (nuclear and cytoplasmic) and glutamine synthetase. |
| 4212 | 19669260 | They express serum amyloid A and C-reactive protein. |
| 4213 | 19669260 | An additional 10% of inflammatory HCAs express beta-catenin, and are also at risk of malignant transformation. (4) Currently, less than 10% of HCAs are unclassified. |
| 4214 | 19672057 | Plasma amyloid-beta peptide levels correlate with adipocyte amyloid precursor protein gene expression in obese individuals. |
| 4215 | 19683329 | Three patients with insulin dependent type 1 diabetes mellitus and one with insulin dependent type 2 diabetes mellitus developed localized amyloid tumors at their general insulin injection sites. |
| 4216 | 19683329 | Insulin was found to be the major component of the amyloid tumors in all four patients. |
| 4217 | 19683329 | These 4 cases were diagnosed recently within a relatively short period of time, which leads to the conjecture that local insulin-derived amyloid tumors remain principally a differential diagnosis of skin tumors in insulin-dependent diabetic patients. |
| 4218 | 19683329 | Three patients with insulin dependent type 1 diabetes mellitus and one with insulin dependent type 2 diabetes mellitus developed localized amyloid tumors at their general insulin injection sites. |
| 4219 | 19683329 | Insulin was found to be the major component of the amyloid tumors in all four patients. |
| 4220 | 19683329 | These 4 cases were diagnosed recently within a relatively short period of time, which leads to the conjecture that local insulin-derived amyloid tumors remain principally a differential diagnosis of skin tumors in insulin-dependent diabetic patients. |
| 4221 | 19683329 | Three patients with insulin dependent type 1 diabetes mellitus and one with insulin dependent type 2 diabetes mellitus developed localized amyloid tumors at their general insulin injection sites. |
| 4222 | 19683329 | Insulin was found to be the major component of the amyloid tumors in all four patients. |
| 4223 | 19683329 | These 4 cases were diagnosed recently within a relatively short period of time, which leads to the conjecture that local insulin-derived amyloid tumors remain principally a differential diagnosis of skin tumors in insulin-dependent diabetic patients. |
| 4224 | 19720065 | Cholesterol regulates assembly of human islet amyloid polypeptide on model membranes. |
| 4225 | 19720065 | Amylin, a 37-aa pancreatic hormone, is the major constituent of islet amyloid, a hallmark of type II diabetes mellitus. |
| 4226 | 19720065 | Cholesterol regulates assembly of human islet amyloid polypeptide on model membranes. |
| 4227 | 19720065 | Amylin, a 37-aa pancreatic hormone, is the major constituent of islet amyloid, a hallmark of type II diabetes mellitus. |
| 4228 | 19758820 | Association of serum amyloid A levels with adipocyte size and serum levels of adipokines: differences between men and women. |
| 4229 | 19758820 | The aim of this study was to characterize the association between adipocyte enlargement and circulating levels of serum amyloid A (SAA). |
| 4230 | 19758820 | Adipocyte diameter as well as circulating levels of SAA, C-reactive protein (CRP), adiponectin, leptin, interleukin-6, tumor necrosis factor alpha, glucose and insulin were measured. |
| 4231 | 19758820 | SAA levels were weakly but positively correlated with BMI (p=0.043) and % body fat (p=0.027) in all subjects as well as subcutaneous adipocyte diameter (p=0.034) in women. |
| 4232 | 19758820 | Furthermore, in all subjects we found correlations between SAA levels and levels of CRP (p<0.001), interleukin-6 (p<0.001), leptin (p=0.003), insulin (p=0.006), HbA1c (p=0.02) and HOMA-IR (p=0.002). |
| 4233 | 19758820 | Association of serum amyloid A levels with adipocyte size and serum levels of adipokines: differences between men and women. |
| 4234 | 19758820 | The aim of this study was to characterize the association between adipocyte enlargement and circulating levels of serum amyloid A (SAA). |
| 4235 | 19758820 | Adipocyte diameter as well as circulating levels of SAA, C-reactive protein (CRP), adiponectin, leptin, interleukin-6, tumor necrosis factor alpha, glucose and insulin were measured. |
| 4236 | 19758820 | SAA levels were weakly but positively correlated with BMI (p=0.043) and % body fat (p=0.027) in all subjects as well as subcutaneous adipocyte diameter (p=0.034) in women. |
| 4237 | 19758820 | Furthermore, in all subjects we found correlations between SAA levels and levels of CRP (p<0.001), interleukin-6 (p<0.001), leptin (p=0.003), insulin (p=0.006), HbA1c (p=0.02) and HOMA-IR (p=0.002). |
| 4238 | 19794060 | Tetracycline treatment retards the onset and slows the progression of diabetes in human amylin/islet amyloid polypeptide transgenic mice. |
| 4239 | 19810772 | Similarly, the misfolding of the beta-cell hormone human islet amyloid polypeptide (h-IAPP) into toxic oligomers plays a central role in the induction of beta-cell apoptosis in the context of type 2 diabetes. |
| 4240 | 19810772 | In this study, we show that annexin A5 plays a role in interacting with and reducing the toxicity of the amyloidogenic proteins, h-IAPP and alpha-synuclein. |
| 4241 | 19810772 | Experiments with transgenic expression of alpha-synuclein in Caenorhabditis elegans show that annexin A5 reduces alpha-synuclein inclusions in vivo. |
| 4242 | 19810772 | Using thioflavin T fluorescence, electron microscopy, and electron paramagnetic resonance, we provide evidence that substoichiometric amounts of annexin A5 inhibit h-IAPP and alpha-synuclein misfolding and fibril formation. |
| 4243 | 19810772 | We conclude that annexin A5 might act as a molecular safeguard against the formation of toxic amyloid aggregates. |
| 4244 | 19810772 | Similarly, the misfolding of the beta-cell hormone human islet amyloid polypeptide (h-IAPP) into toxic oligomers plays a central role in the induction of beta-cell apoptosis in the context of type 2 diabetes. |
| 4245 | 19810772 | In this study, we show that annexin A5 plays a role in interacting with and reducing the toxicity of the amyloidogenic proteins, h-IAPP and alpha-synuclein. |
| 4246 | 19810772 | Experiments with transgenic expression of alpha-synuclein in Caenorhabditis elegans show that annexin A5 reduces alpha-synuclein inclusions in vivo. |
| 4247 | 19810772 | Using thioflavin T fluorescence, electron microscopy, and electron paramagnetic resonance, we provide evidence that substoichiometric amounts of annexin A5 inhibit h-IAPP and alpha-synuclein misfolding and fibril formation. |
| 4248 | 19810772 | We conclude that annexin A5 might act as a molecular safeguard against the formation of toxic amyloid aggregates. |
| 4249 | 19817482 | Impaired processing of human pro-islet amyloid polypeptide is not a causative factor for fibril formation or membrane damage in vitro. |
| 4250 | 19817482 | Human islet amyloid polypeptide (hIAPP) forms amyloid fibrils in pancreatic islets of patients with type 2 diabetes mellitus (DM2). hIAPP is synthesized by islet beta-cells initially as a preprohormone, processing of which occurs in several steps. |
| 4251 | 19817482 | Impaired processing of human pro-islet amyloid polypeptide is not a causative factor for fibril formation or membrane damage in vitro. |
| 4252 | 19817482 | Human islet amyloid polypeptide (hIAPP) forms amyloid fibrils in pancreatic islets of patients with type 2 diabetes mellitus (DM2). hIAPP is synthesized by islet beta-cells initially as a preprohormone, processing of which occurs in several steps. |
| 4253 | 19843871 | Amylin is the major component of pancreatic amyloid, which is implicated in the development of type 2 diabetes. |
| 4254 | 19917634 | Basic research suggests that insulin accelerates Alzheimer-related pathology through its effects on the amyloid beta (Abeta). |
| 4255 | 19917634 | Moreover, amyloid imaging in non-demented older people with or without insulin resistance would verify the role of insulin in the processing and deposition of Abeta. |
| 4256 | 19917634 | Basic research suggests that insulin accelerates Alzheimer-related pathology through its effects on the amyloid beta (Abeta). |
| 4257 | 19917634 | Moreover, amyloid imaging in non-demented older people with or without insulin resistance would verify the role of insulin in the processing and deposition of Abeta. |
| 4258 | 19945428 | Insulin amyloid fibrillation studied by terahertz spectroscopy and other biophysical methods. |
| 4259 | 19945428 | To study the changes in secondary, tertiary, quaternary structures, and the alteration in the collective vibrational mode density of states during the amyloid fibrillation, bovine insulin in 20% acetic acid was incubated at 60 degrees C, and its multi-level structures were followed by various biophysical techniques, including circular dichroism (CD), thioflavin T fluorescence (ThT), dynamic light scattering (DLS), electron microscopy, and terahertz (THz) absorption spectroscopy. |
| 4260 | 19945428 | Insulin amyloid fibrillation studied by terahertz spectroscopy and other biophysical methods. |
| 4261 | 19945428 | To study the changes in secondary, tertiary, quaternary structures, and the alteration in the collective vibrational mode density of states during the amyloid fibrillation, bovine insulin in 20% acetic acid was incubated at 60 degrees C, and its multi-level structures were followed by various biophysical techniques, including circular dichroism (CD), thioflavin T fluorescence (ThT), dynamic light scattering (DLS), electron microscopy, and terahertz (THz) absorption spectroscopy. |
| 4262 | 19948124 | Islet amyloid polypeptide (amylin) is the main component in amyloid deposits formed in type II diabetes. |
| 4263 | 19966530 | In addition, Tanis was postulated as a hepatic receptor for an inflammatory marker, serum amyloid A-1 (SAA1), which represents a risk factor for cardiovascular disease. |
| 4264 | 20019678 | Subjects with T2D had higher VAT expression of molecules regulating inflammation (tumor necrosis factor-alpha (TNFalpha), macrophage inflammatory protein (MIP), interleukin-8 (IL-8)). |
| 4265 | 20019678 | Fasting glucose related to VAT expression of TNFalpha, MIP, serum amyloid A (SAA), IL-1alpha, IL-1beta, IL-8, and IL-8 receptor. |
| 4266 | 20019678 | Abdominal fat mass was related to VAT expression of MIP, SAA, cAMP response element-binding protein (CREBP), IL-1beta, and IL-8. |
| 4267 | 20019678 | There were depot-specific differences in expression of serum T2D predictors: VAT expressed higher levels of complement C3; SAT expressed higher levels of retinol-binding protein-4 (RBP4), adiponectin, and leptin. |
| 4268 | 20028124 | The ability of rodent islet amyloid polypeptide to inhibit amyloid formation by human islet amyloid polypeptide has important implications for the mechanism of amyloid formation and the design of inhibitors. |
| 4269 | 20028124 | Islet amyloid polypeptide (IAPP) is a 37-residue polypeptide hormone that is responsible for islet amyloid formation in type II diabetes. |
| 4270 | 20028124 | The ability of rodent islet amyloid polypeptide to inhibit amyloid formation by human islet amyloid polypeptide has important implications for the mechanism of amyloid formation and the design of inhibitors. |
| 4271 | 20028124 | Islet amyloid polypeptide (IAPP) is a 37-residue polypeptide hormone that is responsible for islet amyloid formation in type II diabetes. |
| 4272 | 20030463 | It was also demonstrated that neurotoxins, coined amyloid beta-derived diffusible ligands (ADDLs), disrupt signal transduction at synapses, making the cell insulin resistant. |
| 4273 | 20036826 | The first, Alzheimer's disease (AD), is the most prevalent neurodegenerative disease and is thought to be initiated by the aggregation of a natively unstructured peptide called amyloid beta (Abeta). |
| 4274 | 20042670 | Evidence for proteotoxicity in beta cells in type 2 diabetes: toxic islet amyloid polypeptide oligomers form intracellularly in the secretory pathway. |
| 4275 | 20042670 | The islet in type 2 diabetes mellitus (T2DM) is characterized by a deficit in beta cells and islet amyloid derived from islet amyloid polypeptide (IAPP), a protein co-expressed with insulin by beta cells. |
| 4276 | 20042670 | Evidence for proteotoxicity in beta cells in type 2 diabetes: toxic islet amyloid polypeptide oligomers form intracellularly in the secretory pathway. |
| 4277 | 20042670 | The islet in type 2 diabetes mellitus (T2DM) is characterized by a deficit in beta cells and islet amyloid derived from islet amyloid polypeptide (IAPP), a protein co-expressed with insulin by beta cells. |
| 4278 | 20052582 | The role of the disulfide bond in the interaction of islet amyloid polypeptide with membranes. |
| 4279 | 20052582 | Human islet amyloid polypeptide (hIAPP) forms amyloid fibrils in pancreatic islets of patients with type 2 diabetes mellitus. |
| 4280 | 20052582 | The role of the disulfide bond in the interaction of islet amyloid polypeptide with membranes. |
| 4281 | 20052582 | Human islet amyloid polypeptide (hIAPP) forms amyloid fibrils in pancreatic islets of patients with type 2 diabetes mellitus. |
| 4282 | 20055378 | Among these are Parkinson's disease (alpha-synuclein), Type II diabetes (islet amyloid polypeptide), and Alzheimer's disease (amyloid beta-peptide, Abeta). |
| 4283 | 20069542 | The 37-amino acid polypeptide islet amyloid polypeptide (IAPP), or amylin, is found as amyloid aggregates in the islets of Langerhans in patients with type II diabetes. |
| 4284 | 20093026 | Deposits consisting mainly of a small protein, called islet amyloid polypeptide (amylin), which aggregates into oligo-/polymeric beta sheet structures is responsible for cytotoxicity to the pancreatic beta-cells, thus inhibition of this process has been explored as a potential prevention or treatment. |
| 4285 | 20110613 | In contrast, sporadic AD has been proposed to start with an insulin-resistant brain state (IRBS).We investigated the effect of IRBS induced by intracerebroventricularly (icv) administered streptozotocin (STZ) on behavior, glycogen synthase kinase-3 (GSK) alpha/beta content, and the formation of AD-like morphological hallmarks Abeta and tau protein in AbetaPP Tg2576 mice. |
| 4286 | 20110613 | Soluble and aggregated Abeta40/42 fragments, total and phosphorylated tau protein, and GSK-3alpha/beta were determined by ELISA. |
| 4287 | 20110613 | In Tg mice, STZ treatment increased mortality, reduced spatial cognition, and increased cerebral aggregated Abeta fragments, total tau protein, and congophilic amyloid deposits. |
| 4288 | 20132476 | Insulin inhibits Abeta fibrillogenesis through a decrease of the GM1 ganglioside-rich microdomain in neuronal membranes. |
| 4289 | 20132476 | To investigate whether insulin is associated with the assembly of amyloid beta-protein from the cell surface, we treated nerve growth factor (NGF)-treated rat pheochromocytoma 12 (PC12) cells with insulin, which is related to the development of diabetes. |
| 4290 | 20132476 | Insulin treatment induced a decrease in GM1 ganglioside (GM1) levels in detergent-resistant membrane microdomains of NGF-treated PC12 cells. |
| 4291 | 20132476 | The insulin-induced effects on GM1 levels were regulated by a phosphatidylinositol 3-kinase inhibitor, but not by an extracellular signal-regulated kinase inhibitor. |
| 4292 | 20132476 | In addition, insulin failed to induce formation of fibrils from soluble amyloid beta-protein or to accelerate GM1-induced fibril formation. |
| 4293 | 20132476 | Furthermore, assembly of amyloid beta-protein in cultures of NGF-treated PC12 cells was significantly decreased by insulin. |
| 4294 | 20132476 | These results suggest that insulin inhibits amyloid beta-protein assembly by decreasing GM1 expression in detergent-resistant membrane microdomains of neuronal membranes. |
| 4295 | 20132476 | Insulin inhibits Abeta fibrillogenesis through a decrease of the GM1 ganglioside-rich microdomain in neuronal membranes. |
| 4296 | 20132476 | To investigate whether insulin is associated with the assembly of amyloid beta-protein from the cell surface, we treated nerve growth factor (NGF)-treated rat pheochromocytoma 12 (PC12) cells with insulin, which is related to the development of diabetes. |
| 4297 | 20132476 | Insulin treatment induced a decrease in GM1 ganglioside (GM1) levels in detergent-resistant membrane microdomains of NGF-treated PC12 cells. |
| 4298 | 20132476 | The insulin-induced effects on GM1 levels were regulated by a phosphatidylinositol 3-kinase inhibitor, but not by an extracellular signal-regulated kinase inhibitor. |
| 4299 | 20132476 | In addition, insulin failed to induce formation of fibrils from soluble amyloid beta-protein or to accelerate GM1-induced fibril formation. |
| 4300 | 20132476 | Furthermore, assembly of amyloid beta-protein in cultures of NGF-treated PC12 cells was significantly decreased by insulin. |
| 4301 | 20132476 | These results suggest that insulin inhibits amyloid beta-protein assembly by decreasing GM1 expression in detergent-resistant membrane microdomains of neuronal membranes. |
| 4302 | 20132476 | Insulin inhibits Abeta fibrillogenesis through a decrease of the GM1 ganglioside-rich microdomain in neuronal membranes. |
| 4303 | 20132476 | To investigate whether insulin is associated with the assembly of amyloid beta-protein from the cell surface, we treated nerve growth factor (NGF)-treated rat pheochromocytoma 12 (PC12) cells with insulin, which is related to the development of diabetes. |
| 4304 | 20132476 | Insulin treatment induced a decrease in GM1 ganglioside (GM1) levels in detergent-resistant membrane microdomains of NGF-treated PC12 cells. |
| 4305 | 20132476 | The insulin-induced effects on GM1 levels were regulated by a phosphatidylinositol 3-kinase inhibitor, but not by an extracellular signal-regulated kinase inhibitor. |
| 4306 | 20132476 | In addition, insulin failed to induce formation of fibrils from soluble amyloid beta-protein or to accelerate GM1-induced fibril formation. |
| 4307 | 20132476 | Furthermore, assembly of amyloid beta-protein in cultures of NGF-treated PC12 cells was significantly decreased by insulin. |
| 4308 | 20132476 | These results suggest that insulin inhibits amyloid beta-protein assembly by decreasing GM1 expression in detergent-resistant membrane microdomains of neuronal membranes. |
| 4309 | 20132476 | Insulin inhibits Abeta fibrillogenesis through a decrease of the GM1 ganglioside-rich microdomain in neuronal membranes. |
| 4310 | 20132476 | To investigate whether insulin is associated with the assembly of amyloid beta-protein from the cell surface, we treated nerve growth factor (NGF)-treated rat pheochromocytoma 12 (PC12) cells with insulin, which is related to the development of diabetes. |
| 4311 | 20132476 | Insulin treatment induced a decrease in GM1 ganglioside (GM1) levels in detergent-resistant membrane microdomains of NGF-treated PC12 cells. |
| 4312 | 20132476 | The insulin-induced effects on GM1 levels were regulated by a phosphatidylinositol 3-kinase inhibitor, but not by an extracellular signal-regulated kinase inhibitor. |
| 4313 | 20132476 | In addition, insulin failed to induce formation of fibrils from soluble amyloid beta-protein or to accelerate GM1-induced fibril formation. |
| 4314 | 20132476 | Furthermore, assembly of amyloid beta-protein in cultures of NGF-treated PC12 cells was significantly decreased by insulin. |
| 4315 | 20132476 | These results suggest that insulin inhibits amyloid beta-protein assembly by decreasing GM1 expression in detergent-resistant membrane microdomains of neuronal membranes. |
| 4316 | 20153100 | Aggregation of human islet amyloid polypeptide (hIAPP) into cytotoxic beta-sheet oligomers and amyloid plaques is considered a key event in pancreatic beta-cell degeneration in type 2 diabetes (T2D). hIAPP is synthesized in the pancreatic beta-cells and it is stored, co-processed in the secretory granules, and co-secreted to the extracellular matrix together with insulin. |
| 4317 | 20153100 | For comparison, the effects of insulin, which is a natively occurring hIAPP aggregation inhibitor, rat IAPP (rIAPP), which is a natively non-amyloidogenic hIAPP analog, and the hIAPP amyloid core peptide hIAPP(22-27) or NFGAIL were also studied. |
| 4318 | 20153100 | Aggregation of human islet amyloid polypeptide (hIAPP) into cytotoxic beta-sheet oligomers and amyloid plaques is considered a key event in pancreatic beta-cell degeneration in type 2 diabetes (T2D). hIAPP is synthesized in the pancreatic beta-cells and it is stored, co-processed in the secretory granules, and co-secreted to the extracellular matrix together with insulin. |
| 4319 | 20153100 | For comparison, the effects of insulin, which is a natively occurring hIAPP aggregation inhibitor, rat IAPP (rIAPP), which is a natively non-amyloidogenic hIAPP analog, and the hIAPP amyloid core peptide hIAPP(22-27) or NFGAIL were also studied. |
| 4320 | 20160085 | Aggregates of the beta cell peptide islet amyloid polypeptide (IAPP) promote beta cell apoptosis and rapid amyloid formation occurs in transplanted islets. |
| 4321 | 20176106 | The 51-residue polypeptide hormone insulin, which is associated with type II diabetes, has been shown to self-assemble to form amyloid fibrils in vitro. |
| 4322 | 20182863 | Amyloid formation is considered a significant factor in deterioration of islet function and reduction in beta cell mass, and involves aggregation of monomers of the normally soluble beta cell peptide, human islet amyloid polypeptide (hIAPP) into oligomers, fibrils and, ultimately, mature amyloid deposits. |
| 4323 | 20190472 | Immunostains with insulin antibody were positive for this deposition but not so with amylin or AA or AL amyloid. |
| 4324 | 20213024 | This receptor, which is frequently associated with proinflammatory responses, has been shown to be activated by various ligands such as high mobility group box-1 (HMGB1/amphoterin), amyloid fibrils, transthyrein, Mac-1 (Integrin Mac-1), as well as advanced glycation end products (AGEs). |
| 4325 | 20229808 | Peripheral hyperinsulinemia may link to cerebral insulin resistance, leading to the inhibition of removal of amyloid beta protein and the increase of tau hyperphosphorylation. |
| 4326 | 20231468 | Notably, APP(+)-ob/ob mice showed cerebrovascular inflammation and severe amyloid angiopathy. |
| 4327 | 20308712 | Additional pathological-anatomical investigations demonstrated insulin in one (the most recent) amyloid tumour. |
| 4328 | 20369225 | Differences between amyloid toxicity in alpha and beta cells in human and mouse islets and the role of caspase-3. |
| 4329 | 20400513 | Neprilysin impedes islet amyloid formation by inhibition of fibril formation rather than peptide degradation. |
| 4330 | 20400513 | Deposition of islet amyloid polypeptide (IAPP) as islet amyloid in type 2 diabetes contributes to loss of beta-cell function and mass, yet the mechanism for its occurrence is unclear. |
| 4331 | 20400513 | Neprilysin is a metallopeptidase known to degrade amyloid in Alzheimer disease. |
| 4332 | 20400513 | We previously demonstrated neprilysin to be present in pancreatic islets and now sought to determine whether it plays a role in degrading islet amyloid. |
| 4333 | 20400513 | Following neprilysin inhibition, islet amyloid deposition and beta-cell apoptosis increased by 54 and 75%, respectively, whereas when neprilysin was up-regulated islet amyloid deposition and beta-cell apoptosis both decreased by 79%. |
| 4334 | 20400513 | To determine if neprilysin modulated amyloid deposition by cleaving hIAPP, analysis of hIAPP incubated with neprilysin was performed by mass spectrometry, which failed to demonstrate neprilysin-induced cleavage. |
| 4335 | 20400513 | In summary, neprilysin decreases islet amyloid deposition by inhibiting hIAPP fibril formation, rather than degrading hIAPP. |
| 4336 | 20400513 | These findings suggest that targeting the role of neprilysin in IAPP fibril assembly, in addition to IAPP cleavage by other peptidases, may provide a novel approach to reduce and/or prevent islet amyloid deposition in type 2 diabetes. |
| 4337 | 20400513 | Neprilysin impedes islet amyloid formation by inhibition of fibril formation rather than peptide degradation. |
| 4338 | 20400513 | Deposition of islet amyloid polypeptide (IAPP) as islet amyloid in type 2 diabetes contributes to loss of beta-cell function and mass, yet the mechanism for its occurrence is unclear. |
| 4339 | 20400513 | Neprilysin is a metallopeptidase known to degrade amyloid in Alzheimer disease. |
| 4340 | 20400513 | We previously demonstrated neprilysin to be present in pancreatic islets and now sought to determine whether it plays a role in degrading islet amyloid. |
| 4341 | 20400513 | Following neprilysin inhibition, islet amyloid deposition and beta-cell apoptosis increased by 54 and 75%, respectively, whereas when neprilysin was up-regulated islet amyloid deposition and beta-cell apoptosis both decreased by 79%. |
| 4342 | 20400513 | To determine if neprilysin modulated amyloid deposition by cleaving hIAPP, analysis of hIAPP incubated with neprilysin was performed by mass spectrometry, which failed to demonstrate neprilysin-induced cleavage. |
| 4343 | 20400513 | In summary, neprilysin decreases islet amyloid deposition by inhibiting hIAPP fibril formation, rather than degrading hIAPP. |
| 4344 | 20400513 | These findings suggest that targeting the role of neprilysin in IAPP fibril assembly, in addition to IAPP cleavage by other peptidases, may provide a novel approach to reduce and/or prevent islet amyloid deposition in type 2 diabetes. |
| 4345 | 20400513 | Neprilysin impedes islet amyloid formation by inhibition of fibril formation rather than peptide degradation. |
| 4346 | 20400513 | Deposition of islet amyloid polypeptide (IAPP) as islet amyloid in type 2 diabetes contributes to loss of beta-cell function and mass, yet the mechanism for its occurrence is unclear. |
| 4347 | 20400513 | Neprilysin is a metallopeptidase known to degrade amyloid in Alzheimer disease. |
| 4348 | 20400513 | We previously demonstrated neprilysin to be present in pancreatic islets and now sought to determine whether it plays a role in degrading islet amyloid. |
| 4349 | 20400513 | Following neprilysin inhibition, islet amyloid deposition and beta-cell apoptosis increased by 54 and 75%, respectively, whereas when neprilysin was up-regulated islet amyloid deposition and beta-cell apoptosis both decreased by 79%. |
| 4350 | 20400513 | To determine if neprilysin modulated amyloid deposition by cleaving hIAPP, analysis of hIAPP incubated with neprilysin was performed by mass spectrometry, which failed to demonstrate neprilysin-induced cleavage. |
| 4351 | 20400513 | In summary, neprilysin decreases islet amyloid deposition by inhibiting hIAPP fibril formation, rather than degrading hIAPP. |
| 4352 | 20400513 | These findings suggest that targeting the role of neprilysin in IAPP fibril assembly, in addition to IAPP cleavage by other peptidases, may provide a novel approach to reduce and/or prevent islet amyloid deposition in type 2 diabetes. |
| 4353 | 20400513 | Neprilysin impedes islet amyloid formation by inhibition of fibril formation rather than peptide degradation. |
| 4354 | 20400513 | Deposition of islet amyloid polypeptide (IAPP) as islet amyloid in type 2 diabetes contributes to loss of beta-cell function and mass, yet the mechanism for its occurrence is unclear. |
| 4355 | 20400513 | Neprilysin is a metallopeptidase known to degrade amyloid in Alzheimer disease. |
| 4356 | 20400513 | We previously demonstrated neprilysin to be present in pancreatic islets and now sought to determine whether it plays a role in degrading islet amyloid. |
| 4357 | 20400513 | Following neprilysin inhibition, islet amyloid deposition and beta-cell apoptosis increased by 54 and 75%, respectively, whereas when neprilysin was up-regulated islet amyloid deposition and beta-cell apoptosis both decreased by 79%. |
| 4358 | 20400513 | To determine if neprilysin modulated amyloid deposition by cleaving hIAPP, analysis of hIAPP incubated with neprilysin was performed by mass spectrometry, which failed to demonstrate neprilysin-induced cleavage. |
| 4359 | 20400513 | In summary, neprilysin decreases islet amyloid deposition by inhibiting hIAPP fibril formation, rather than degrading hIAPP. |
| 4360 | 20400513 | These findings suggest that targeting the role of neprilysin in IAPP fibril assembly, in addition to IAPP cleavage by other peptidases, may provide a novel approach to reduce and/or prevent islet amyloid deposition in type 2 diabetes. |
| 4361 | 20400513 | Neprilysin impedes islet amyloid formation by inhibition of fibril formation rather than peptide degradation. |
| 4362 | 20400513 | Deposition of islet amyloid polypeptide (IAPP) as islet amyloid in type 2 diabetes contributes to loss of beta-cell function and mass, yet the mechanism for its occurrence is unclear. |
| 4363 | 20400513 | Neprilysin is a metallopeptidase known to degrade amyloid in Alzheimer disease. |
| 4364 | 20400513 | We previously demonstrated neprilysin to be present in pancreatic islets and now sought to determine whether it plays a role in degrading islet amyloid. |
| 4365 | 20400513 | Following neprilysin inhibition, islet amyloid deposition and beta-cell apoptosis increased by 54 and 75%, respectively, whereas when neprilysin was up-regulated islet amyloid deposition and beta-cell apoptosis both decreased by 79%. |
| 4366 | 20400513 | To determine if neprilysin modulated amyloid deposition by cleaving hIAPP, analysis of hIAPP incubated with neprilysin was performed by mass spectrometry, which failed to demonstrate neprilysin-induced cleavage. |
| 4367 | 20400513 | In summary, neprilysin decreases islet amyloid deposition by inhibiting hIAPP fibril formation, rather than degrading hIAPP. |
| 4368 | 20400513 | These findings suggest that targeting the role of neprilysin in IAPP fibril assembly, in addition to IAPP cleavage by other peptidases, may provide a novel approach to reduce and/or prevent islet amyloid deposition in type 2 diabetes. |
| 4369 | 20400513 | Neprilysin impedes islet amyloid formation by inhibition of fibril formation rather than peptide degradation. |
| 4370 | 20400513 | Deposition of islet amyloid polypeptide (IAPP) as islet amyloid in type 2 diabetes contributes to loss of beta-cell function and mass, yet the mechanism for its occurrence is unclear. |
| 4371 | 20400513 | Neprilysin is a metallopeptidase known to degrade amyloid in Alzheimer disease. |
| 4372 | 20400513 | We previously demonstrated neprilysin to be present in pancreatic islets and now sought to determine whether it plays a role in degrading islet amyloid. |
| 4373 | 20400513 | Following neprilysin inhibition, islet amyloid deposition and beta-cell apoptosis increased by 54 and 75%, respectively, whereas when neprilysin was up-regulated islet amyloid deposition and beta-cell apoptosis both decreased by 79%. |
| 4374 | 20400513 | To determine if neprilysin modulated amyloid deposition by cleaving hIAPP, analysis of hIAPP incubated with neprilysin was performed by mass spectrometry, which failed to demonstrate neprilysin-induced cleavage. |
| 4375 | 20400513 | In summary, neprilysin decreases islet amyloid deposition by inhibiting hIAPP fibril formation, rather than degrading hIAPP. |
| 4376 | 20400513 | These findings suggest that targeting the role of neprilysin in IAPP fibril assembly, in addition to IAPP cleavage by other peptidases, may provide a novel approach to reduce and/or prevent islet amyloid deposition in type 2 diabetes. |
| 4377 | 20400513 | Neprilysin impedes islet amyloid formation by inhibition of fibril formation rather than peptide degradation. |
| 4378 | 20400513 | Deposition of islet amyloid polypeptide (IAPP) as islet amyloid in type 2 diabetes contributes to loss of beta-cell function and mass, yet the mechanism for its occurrence is unclear. |
| 4379 | 20400513 | Neprilysin is a metallopeptidase known to degrade amyloid in Alzheimer disease. |
| 4380 | 20400513 | We previously demonstrated neprilysin to be present in pancreatic islets and now sought to determine whether it plays a role in degrading islet amyloid. |
| 4381 | 20400513 | Following neprilysin inhibition, islet amyloid deposition and beta-cell apoptosis increased by 54 and 75%, respectively, whereas when neprilysin was up-regulated islet amyloid deposition and beta-cell apoptosis both decreased by 79%. |
| 4382 | 20400513 | To determine if neprilysin modulated amyloid deposition by cleaving hIAPP, analysis of hIAPP incubated with neprilysin was performed by mass spectrometry, which failed to demonstrate neprilysin-induced cleavage. |
| 4383 | 20400513 | In summary, neprilysin decreases islet amyloid deposition by inhibiting hIAPP fibril formation, rather than degrading hIAPP. |
| 4384 | 20400513 | These findings suggest that targeting the role of neprilysin in IAPP fibril assembly, in addition to IAPP cleavage by other peptidases, may provide a novel approach to reduce and/or prevent islet amyloid deposition in type 2 diabetes. |
| 4385 | 20400513 | Neprilysin impedes islet amyloid formation by inhibition of fibril formation rather than peptide degradation. |
| 4386 | 20400513 | Deposition of islet amyloid polypeptide (IAPP) as islet amyloid in type 2 diabetes contributes to loss of beta-cell function and mass, yet the mechanism for its occurrence is unclear. |
| 4387 | 20400513 | Neprilysin is a metallopeptidase known to degrade amyloid in Alzheimer disease. |
| 4388 | 20400513 | We previously demonstrated neprilysin to be present in pancreatic islets and now sought to determine whether it plays a role in degrading islet amyloid. |
| 4389 | 20400513 | Following neprilysin inhibition, islet amyloid deposition and beta-cell apoptosis increased by 54 and 75%, respectively, whereas when neprilysin was up-regulated islet amyloid deposition and beta-cell apoptosis both decreased by 79%. |
| 4390 | 20400513 | To determine if neprilysin modulated amyloid deposition by cleaving hIAPP, analysis of hIAPP incubated with neprilysin was performed by mass spectrometry, which failed to demonstrate neprilysin-induced cleavage. |
| 4391 | 20400513 | In summary, neprilysin decreases islet amyloid deposition by inhibiting hIAPP fibril formation, rather than degrading hIAPP. |
| 4392 | 20400513 | These findings suggest that targeting the role of neprilysin in IAPP fibril assembly, in addition to IAPP cleavage by other peptidases, may provide a novel approach to reduce and/or prevent islet amyloid deposition in type 2 diabetes. |
| 4393 | 20404854 | Islet amyloid polypeptide is a hormone synthesized in pancreatic beta cells and cosecreted with insulin. |
| 4394 | 20404854 | Circulating islet amyloid polypeptide binds to receptors located in the hindbrain and increases satiety, delays gastric emptying and suppresses glucagon secretion. |
| 4395 | 20404854 | Thus, islet amyloid polypeptide complements the effects of insulin. |
| 4396 | 20404854 | T1DM is a state of both islet amyloid polypeptide and insulin deficiency. |
| 4397 | 20404854 | Pramlintide, a synthetic analog of islet amyloid polypeptide, can replace this hormone in patients with T1DM. |
| 4398 | 20404854 | Agents that decrease intestinal carbohydrate digestion (alpha-glucosidase inhibitors) or decrease insulin resistance (metformin) might be alternative adjunctive therapies in T1DM, though its benefits are marginally supported by clinical data. |
| 4399 | 20404854 | Islet amyloid polypeptide is a hormone synthesized in pancreatic beta cells and cosecreted with insulin. |
| 4400 | 20404854 | Circulating islet amyloid polypeptide binds to receptors located in the hindbrain and increases satiety, delays gastric emptying and suppresses glucagon secretion. |
| 4401 | 20404854 | Thus, islet amyloid polypeptide complements the effects of insulin. |
| 4402 | 20404854 | T1DM is a state of both islet amyloid polypeptide and insulin deficiency. |
| 4403 | 20404854 | Pramlintide, a synthetic analog of islet amyloid polypeptide, can replace this hormone in patients with T1DM. |
| 4404 | 20404854 | Agents that decrease intestinal carbohydrate digestion (alpha-glucosidase inhibitors) or decrease insulin resistance (metformin) might be alternative adjunctive therapies in T1DM, though its benefits are marginally supported by clinical data. |
| 4405 | 20404854 | Islet amyloid polypeptide is a hormone synthesized in pancreatic beta cells and cosecreted with insulin. |
| 4406 | 20404854 | Circulating islet amyloid polypeptide binds to receptors located in the hindbrain and increases satiety, delays gastric emptying and suppresses glucagon secretion. |
| 4407 | 20404854 | Thus, islet amyloid polypeptide complements the effects of insulin. |
| 4408 | 20404854 | T1DM is a state of both islet amyloid polypeptide and insulin deficiency. |
| 4409 | 20404854 | Pramlintide, a synthetic analog of islet amyloid polypeptide, can replace this hormone in patients with T1DM. |
| 4410 | 20404854 | Agents that decrease intestinal carbohydrate digestion (alpha-glucosidase inhibitors) or decrease insulin resistance (metformin) might be alternative adjunctive therapies in T1DM, though its benefits are marginally supported by clinical data. |
| 4411 | 20404854 | Islet amyloid polypeptide is a hormone synthesized in pancreatic beta cells and cosecreted with insulin. |
| 4412 | 20404854 | Circulating islet amyloid polypeptide binds to receptors located in the hindbrain and increases satiety, delays gastric emptying and suppresses glucagon secretion. |
| 4413 | 20404854 | Thus, islet amyloid polypeptide complements the effects of insulin. |
| 4414 | 20404854 | T1DM is a state of both islet amyloid polypeptide and insulin deficiency. |
| 4415 | 20404854 | Pramlintide, a synthetic analog of islet amyloid polypeptide, can replace this hormone in patients with T1DM. |
| 4416 | 20404854 | Agents that decrease intestinal carbohydrate digestion (alpha-glucosidase inhibitors) or decrease insulin resistance (metformin) might be alternative adjunctive therapies in T1DM, though its benefits are marginally supported by clinical data. |
| 4417 | 20404854 | Islet amyloid polypeptide is a hormone synthesized in pancreatic beta cells and cosecreted with insulin. |
| 4418 | 20404854 | Circulating islet amyloid polypeptide binds to receptors located in the hindbrain and increases satiety, delays gastric emptying and suppresses glucagon secretion. |
| 4419 | 20404854 | Thus, islet amyloid polypeptide complements the effects of insulin. |
| 4420 | 20404854 | T1DM is a state of both islet amyloid polypeptide and insulin deficiency. |
| 4421 | 20404854 | Pramlintide, a synthetic analog of islet amyloid polypeptide, can replace this hormone in patients with T1DM. |
| 4422 | 20404854 | Agents that decrease intestinal carbohydrate digestion (alpha-glucosidase inhibitors) or decrease insulin resistance (metformin) might be alternative adjunctive therapies in T1DM, though its benefits are marginally supported by clinical data. |
| 4423 | 20421886 | The multiligand receptor of the immunoglobulin superfamily, receptor for advanced glycation endproducts (RAGE), is a signal transduction receptor that binds advanced glycation endproducts, certain members of the S100/calgranulin family of proteins, high mobility group box 1 (HMGB1), advanced oxidation protein products, and amyloid (beta-sheet fibrils). |
| 4424 | 20429571 | The human Islet amyloid polypeptide (hIAPP or amylin) is a 37-residue peptide hormone that is normally cosecreted with insulin by the pancreatic beta-cells. |
| 4425 | 20452363 | The sulfated triphenyl methane derivative acid fuchsin is a potent inhibitor of amyloid formation by human islet amyloid polypeptide and protects against the toxic effects of amyloid formation. |
| 4426 | 20452363 | Islet amyloid polypeptide (IAPP), also known as amylin, is responsible for amyloid formation in type 2 diabetes. |
| 4427 | 20452363 | The compound is less effective against the beta-amyloid peptide, indicating specificity in its ability to inhibit amyloid formation by IAPP. |
| 4428 | 20452363 | The sulfated triphenyl methane derivative acid fuchsin is a potent inhibitor of amyloid formation by human islet amyloid polypeptide and protects against the toxic effects of amyloid formation. |
| 4429 | 20452363 | Islet amyloid polypeptide (IAPP), also known as amylin, is responsible for amyloid formation in type 2 diabetes. |
| 4430 | 20452363 | The compound is less effective against the beta-amyloid peptide, indicating specificity in its ability to inhibit amyloid formation by IAPP. |
| 4431 | 20452363 | The sulfated triphenyl methane derivative acid fuchsin is a potent inhibitor of amyloid formation by human islet amyloid polypeptide and protects against the toxic effects of amyloid formation. |
| 4432 | 20452363 | Islet amyloid polypeptide (IAPP), also known as amylin, is responsible for amyloid formation in type 2 diabetes. |
| 4433 | 20452363 | The compound is less effective against the beta-amyloid peptide, indicating specificity in its ability to inhibit amyloid formation by IAPP. |
| 4434 | 20467341 | Up-regulated pancreatic tissue microRNA-375 associates with human type 2 diabetes through beta-cell deficit and islet amyloid deposition. |
| 4435 | 20471471 | In this study, we proposed that amyloid precursor protein (APP) expression was regulated by AGEs. |
| 4436 | 20472067 | We describe our 2D IR spectrometer, as well as protocols for (13)C(18)O isotope labeling, and then illustrate the technique with an application to the aggregation of the human islet amyloid polypeptide implicated in type 2 diabetes. |
| 4437 | 20487079 | Glycemia and levels of cerebrospinal fluid amyloid and tau in patients attending a memory clinic. |
| 4438 | 20494101 | Studies of the nonpolar, transmembrane surfactant protein C (SP-C) have revealed amino acid sequence features that determine its amyloid fibril formation, features that are also found in the amyloid beta-peptide in Alzheimer's disease and the prion protein. |
| 4439 | 20495767 | Human islet amyloid polypeptide fibril binding to catalase: a transmission electron microscopy and microplate study. |
| 4440 | 20495767 | The diabetes-associated human islet amyloid polypeptide (IAPP) is a 37-amino-acid peptide that forms fibrils in vitro and in vivo. |
| 4441 | 20495767 | Human IAPP fibrils are toxic in a similar manner to Alzheimer's amyloid-beta (A-beta) and prion protein (PrP) fibrils. |
| 4442 | 20495767 | Previous studies have shown that catalase binds to A-beta fibrils and appears to recognize a region containing the Gly-Ala-Ile-Ile sequence that is similar to the Gly-Ala-Ile-Leu sequence found in human IAPP residues 24-27. |
| 4443 | 20495767 | These results suggest that catalase recognizes a Gly-Ala-Ile-Leu-like sequence in amyloid fibril-forming peptides. |
| 4444 | 20495767 | The ability of catalase to bind IAPP, A-beta, and PrP fibrils demonstrates the presence of similar accessible structural motifs that may be targets for antiamyloid therapeutic development. |
| 4445 | 20495767 | Human islet amyloid polypeptide fibril binding to catalase: a transmission electron microscopy and microplate study. |
| 4446 | 20495767 | The diabetes-associated human islet amyloid polypeptide (IAPP) is a 37-amino-acid peptide that forms fibrils in vitro and in vivo. |
| 4447 | 20495767 | Human IAPP fibrils are toxic in a similar manner to Alzheimer's amyloid-beta (A-beta) and prion protein (PrP) fibrils. |
| 4448 | 20495767 | Previous studies have shown that catalase binds to A-beta fibrils and appears to recognize a region containing the Gly-Ala-Ile-Ile sequence that is similar to the Gly-Ala-Ile-Leu sequence found in human IAPP residues 24-27. |
| 4449 | 20495767 | These results suggest that catalase recognizes a Gly-Ala-Ile-Leu-like sequence in amyloid fibril-forming peptides. |
| 4450 | 20495767 | The ability of catalase to bind IAPP, A-beta, and PrP fibrils demonstrates the presence of similar accessible structural motifs that may be targets for antiamyloid therapeutic development. |
| 4451 | 20495767 | Human islet amyloid polypeptide fibril binding to catalase: a transmission electron microscopy and microplate study. |
| 4452 | 20495767 | The diabetes-associated human islet amyloid polypeptide (IAPP) is a 37-amino-acid peptide that forms fibrils in vitro and in vivo. |
| 4453 | 20495767 | Human IAPP fibrils are toxic in a similar manner to Alzheimer's amyloid-beta (A-beta) and prion protein (PrP) fibrils. |
| 4454 | 20495767 | Previous studies have shown that catalase binds to A-beta fibrils and appears to recognize a region containing the Gly-Ala-Ile-Ile sequence that is similar to the Gly-Ala-Ile-Leu sequence found in human IAPP residues 24-27. |
| 4455 | 20495767 | These results suggest that catalase recognizes a Gly-Ala-Ile-Leu-like sequence in amyloid fibril-forming peptides. |
| 4456 | 20495767 | The ability of catalase to bind IAPP, A-beta, and PrP fibrils demonstrates the presence of similar accessible structural motifs that may be targets for antiamyloid therapeutic development. |
| 4457 | 20509034 | Amylin is the major constituent of pancreatic islet amyloid whose accumulation characterizes patients with type 2 diabetes mellitus (T2DM). |
| 4458 | 20570648 | The N-terminal fragment of human islet amyloid polypeptide is non-fibrillogenic in the presence of membranes and does not cause leakage of bilayers of physiologically relevant lipid composition. |
| 4459 | 20570648 | Human islet amyloid polypeptide (hIAPP) forms amyloid fibrils in pancreatic islets of patients with type 2 diabetes mellitus (DM2). |
| 4460 | 20570648 | The N-terminal fragment of human islet amyloid polypeptide is non-fibrillogenic in the presence of membranes and does not cause leakage of bilayers of physiologically relevant lipid composition. |
| 4461 | 20570648 | Human islet amyloid polypeptide (hIAPP) forms amyloid fibrils in pancreatic islets of patients with type 2 diabetes mellitus (DM2). |
| 4462 | 20585346 | This Review addresses the physiological roles of peptide YY, pancreatic polypeptide, islet amyloid polypeptide, glucagon-like peptide 1, glucagon, oxyntomodulin, cholecystokinin and ghrelin and discusses their potential as targets for the development of novel treatments for obesity. |
| 4463 | 20604554 | Recent studies have implicated non-fibrillar oligomers of the amyloid beta (Abeta) peptide as the primary toxic species in Alzheimer's disease. |
| 4464 | 20619299 | Beta-cell selective K(ATP)-channel activation protects beta-cells and human islets from human islet amyloid polypeptide induced toxicity. |
| 4465 | 20632994 | Insulin, a 51-residue peptide hormone, is an intrinsically amyloidogenic peptide, forming amyloid fibrils in vitro. |
| 4466 | 20649634 | Exendin-4 protects pancreatic beta cells from human islet amyloid polypeptide-induced cell damage: potential involvement of AKT and mitochondria biogenesis. |
| 4467 | 20674218 | The distinct effect of T2DM induction on the pattern of rat serum includes the down-regulation of Apolipoprotein E, Apolipoprotein A-I, Ig gamma-2A chain C region, and up-regulation of Transthyretin (TTR), Haptoglobin (Hp), Serum amyloid P-componen (SAP), Prothrombin. |
| 4468 | 20684641 | pH-Dependent interactions of human islet amyloid polypeptide segments with insulin studied by replica exchange molecular dynamics simulations. |
| 4469 | 20684641 | Amyloidogenesis of human islet amyloid polypeptide (hIAPP) within or surrounding secretory beta-cells of pancreas has long been related to the pathology of type II diabetes. |
| 4470 | 20684641 | Insulin, coexpressed and cosecreted with hIAPP in vivo, has the capacity of interacting with hIAPP and further inhibiting the amyloid deposition of the peptide. |
| 4471 | 20684641 | pH-Dependent interactions of human islet amyloid polypeptide segments with insulin studied by replica exchange molecular dynamics simulations. |
| 4472 | 20684641 | Amyloidogenesis of human islet amyloid polypeptide (hIAPP) within or surrounding secretory beta-cells of pancreas has long been related to the pathology of type II diabetes. |
| 4473 | 20684641 | Insulin, coexpressed and cosecreted with hIAPP in vivo, has the capacity of interacting with hIAPP and further inhibiting the amyloid deposition of the peptide. |
| 4474 | 20684641 | pH-Dependent interactions of human islet amyloid polypeptide segments with insulin studied by replica exchange molecular dynamics simulations. |
| 4475 | 20684641 | Amyloidogenesis of human islet amyloid polypeptide (hIAPP) within or surrounding secretory beta-cells of pancreas has long been related to the pathology of type II diabetes. |
| 4476 | 20684641 | Insulin, coexpressed and cosecreted with hIAPP in vivo, has the capacity of interacting with hIAPP and further inhibiting the amyloid deposition of the peptide. |
| 4477 | 20685871 | Inhaled insulin forms toxic pulmonary amyloid aggregates. |
| 4478 | 20685871 | Our studies were designed to investigate the harmful potential that inhaled insulin has in pulmonary tissue in vivo, through an amyloid formation mechanism. |
| 4479 | 20685871 | Our data demonstrate that inhaled insulin rapidly forms amyloid in the lungs causing a significant reduction in pulmonary air flow. |
| 4480 | 20685871 | These insulin deposits resemble the amyloid structures implicated in protein misfolding disorders, such as Alzheimer's and Parkinson's diseases, and could as well be deleterious in nature. |
| 4481 | 20685871 | Inhaled insulin forms toxic pulmonary amyloid aggregates. |
| 4482 | 20685871 | Our studies were designed to investigate the harmful potential that inhaled insulin has in pulmonary tissue in vivo, through an amyloid formation mechanism. |
| 4483 | 20685871 | Our data demonstrate that inhaled insulin rapidly forms amyloid in the lungs causing a significant reduction in pulmonary air flow. |
| 4484 | 20685871 | These insulin deposits resemble the amyloid structures implicated in protein misfolding disorders, such as Alzheimer's and Parkinson's diseases, and could as well be deleterious in nature. |
| 4485 | 20685871 | Inhaled insulin forms toxic pulmonary amyloid aggregates. |
| 4486 | 20685871 | Our studies were designed to investigate the harmful potential that inhaled insulin has in pulmonary tissue in vivo, through an amyloid formation mechanism. |
| 4487 | 20685871 | Our data demonstrate that inhaled insulin rapidly forms amyloid in the lungs causing a significant reduction in pulmonary air flow. |
| 4488 | 20685871 | These insulin deposits resemble the amyloid structures implicated in protein misfolding disorders, such as Alzheimer's and Parkinson's diseases, and could as well be deleterious in nature. |
| 4489 | 20685871 | Inhaled insulin forms toxic pulmonary amyloid aggregates. |
| 4490 | 20685871 | Our studies were designed to investigate the harmful potential that inhaled insulin has in pulmonary tissue in vivo, through an amyloid formation mechanism. |
| 4491 | 20685871 | Our data demonstrate that inhaled insulin rapidly forms amyloid in the lungs causing a significant reduction in pulmonary air flow. |
| 4492 | 20685871 | These insulin deposits resemble the amyloid structures implicated in protein misfolding disorders, such as Alzheimer's and Parkinson's diseases, and could as well be deleterious in nature. |
| 4493 | 20699477 | Because inappropriate gamma-secretase processing of amyloid precursor protein (APP) in humans is associated with familial Alzheimer's disease, understanding essential elements within each gamma-secretase component is crucial to functional studies. |
| 4494 | 20730162 | Copper-induced cytotoxicity: reactive oxygen species or islet amyloid polypeptide oligomer formation. |
| 4495 | 20730162 | Copper enhances amyloid cytotoxicity and mediates human islet amyloid polypeptide (hIAPP) oligomerization; nickel, a redox inactive metal with similar protein binding affinity to copper, also mimics this effect, thereby demonstrating copper-mediated hIAPP cytotoxicity is due mainly to granular oligomer generation rather than ROS accumulation in type 2 diabetes. |
| 4496 | 20730162 | Copper-induced cytotoxicity: reactive oxygen species or islet amyloid polypeptide oligomer formation. |
| 4497 | 20730162 | Copper enhances amyloid cytotoxicity and mediates human islet amyloid polypeptide (hIAPP) oligomerization; nickel, a redox inactive metal with similar protein binding affinity to copper, also mimics this effect, thereby demonstrating copper-mediated hIAPP cytotoxicity is due mainly to granular oligomer generation rather than ROS accumulation in type 2 diabetes. |
| 4498 | 20809197 | The role of aromatic side-chains in amyloid growth and membrane interaction of the islet amyloid polypeptide fragment LANFLVH. |
| 4499 | 20809197 | Human islet amyloid polypeptide (hIAPP) is known to misfold and aggregate into amyloid deposits that may be found in pancreatic tissues of patients affected by type 2 diabetes. |
| 4500 | 20809197 | The role of aromatic side-chains in amyloid growth and membrane interaction of the islet amyloid polypeptide fragment LANFLVH. |
| 4501 | 20809197 | Human islet amyloid polypeptide (hIAPP) is known to misfold and aggregate into amyloid deposits that may be found in pancreatic tissues of patients affected by type 2 diabetes. |
| 4502 | 20835230 | Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1β in type 2 diabetes. |
| 4503 | 20835230 | Interleukin 1β (IL-1β) is an important inflammatory mediator of type 2 diabetes. |
| 4504 | 20835230 | Here we show that oligomers of islet amyloid polypeptide (IAPP), a protein that forms amyloid deposits in the pancreas during type 2 diabetes, triggered the NLRP3 inflammasome and generated mature IL-1β. |
| 4505 | 20835230 | Finally, mice transgenic for human IAPP had more IL-1β in pancreatic islets, which localized together with amyloid and macrophages. |
| 4506 | 20835230 | Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1β in type 2 diabetes. |
| 4507 | 20835230 | Interleukin 1β (IL-1β) is an important inflammatory mediator of type 2 diabetes. |
| 4508 | 20835230 | Here we show that oligomers of islet amyloid polypeptide (IAPP), a protein that forms amyloid deposits in the pancreas during type 2 diabetes, triggered the NLRP3 inflammasome and generated mature IL-1β. |
| 4509 | 20835230 | Finally, mice transgenic for human IAPP had more IL-1β in pancreatic islets, which localized together with amyloid and macrophages. |
| 4510 | 20835230 | Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1β in type 2 diabetes. |
| 4511 | 20835230 | Interleukin 1β (IL-1β) is an important inflammatory mediator of type 2 diabetes. |
| 4512 | 20835230 | Here we show that oligomers of islet amyloid polypeptide (IAPP), a protein that forms amyloid deposits in the pancreas during type 2 diabetes, triggered the NLRP3 inflammasome and generated mature IL-1β. |
| 4513 | 20835230 | Finally, mice transgenic for human IAPP had more IL-1β in pancreatic islets, which localized together with amyloid and macrophages. |
| 4514 | 20856987 | Cyclen-hybrid compound captures copper to protect INS-1 cells from islet amyloid polypeptide cytotoxicity by inhibiting and lysing effects. |
| 4515 | 20856987 | Human islet amyloid polypeptide (hIAPP) deposit is the hallmark of type 2 diabetes pathology. |
| 4516 | 20856987 | Cyclen-hybrid compound captures copper to protect INS-1 cells from islet amyloid polypeptide cytotoxicity by inhibiting and lysing effects. |
| 4517 | 20856987 | Human islet amyloid polypeptide (hIAPP) deposit is the hallmark of type 2 diabetes pathology. |
| 4518 | 20873820 | The approach is validated using inhibitors of amyloid formation by islet amyloid polypeptide, the causative agent of amyloid formation in type 2 diabetes and the Alzheimer's disease Aβ peptide. |
| 4519 | 20930481 | Phosphatidylserine and phosphatidylglycerol were also reported to trigger fibril formation by human islet amyloid polypeptide (hIAPP). |
| 4520 | 20943756 | In type 2 diabetes, amyloid deposition within the pancreatic islets is a pathophysiological hallmark, making crucial the study in the pancreas of BACE1 and its homologous BACE2 to understand the pathological mechanisms of this disease. |
| 4521 | 20943756 | Intracellular analysis using immunofluorescence showed colocalization of BACE1 with insulin and BACE2 with clathrin-coated vesicles of the plasma membrane in MIN6 cells. |
| 4522 | 20943756 | When BACE1 and -2 were pharmacologically inhibited, BACE1 localization was not altered, whereas BACE2 content in clathrin-coated vesicles was increased. |
| 4523 | 21035753 | A recent report in Nature Immunology (Masters et al., 2010) identifies amyloid polypeptide as an additional enhancer of IL-1β production. |
| 4524 | 21067307 | The effect of curcumin on human islet amyloid polypeptide misfolding and toxicity. |
| 4525 | 21067307 | Type 2 diabetes involves aberrant misfolding of human islet amyloid polypeptide (h-IAPP) and resultant pancreatic amyloid deposits. |
| 4526 | 21067307 | The effect of curcumin on human islet amyloid polypeptide misfolding and toxicity. |
| 4527 | 21067307 | Type 2 diabetes involves aberrant misfolding of human islet amyloid polypeptide (h-IAPP) and resultant pancreatic amyloid deposits. |
| 4528 | 21124955 | The region at 11p15.5-p13 (rs4150642; p = 3.20×10(-111)) contains serum amyloid A1 (SAA1) and the adjacent general transcription factor 2 H1 (GTF2H1), Hermansky-Pudlak Syndrome 5 (HPS5), lactate dehydrogenase A (LDHA), and lactate dehydrogenase C (LDHC). |
| 4529 | 21148563 | The molecular basis of distinct aggregation pathways of islet amyloid polypeptide. |
| 4530 | 21148563 | Abnormal aggregation of islet amyloid polypeptide (IAPP) into amyloid fibrils is a hallmark of type 2 diabetes. |
| 4531 | 21148563 | The molecular basis of distinct aggregation pathways of islet amyloid polypeptide. |
| 4532 | 21148563 | Abnormal aggregation of islet amyloid polypeptide (IAPP) into amyloid fibrils is a hallmark of type 2 diabetes. |
| 4533 | 21150342 | Transmission electron microscopy can be used to evaluate these tissues from young rodent models of insulin resistance and T2DM, including the transgenic Ren2 rat, db/db obese insulin resistant - T2DM mouse, and human islet amyloid polypeptide (HIP) rat model of T2DM. |
| 4534 | 21158384 | Structural polymorphism of human islet amyloid polypeptide (hIAPP) oligomers highlights the importance of interfacial residue interactions. |
| 4535 | 21158384 | A 37-residue of human islet amyloid polypeptide (hIAPP or amylin) is a main component of amyloid plaques found in the pancreas of ∼90% of type II diabetes patients. |
| 4536 | 21158384 | Structural polymorphism of human islet amyloid polypeptide (hIAPP) oligomers highlights the importance of interfacial residue interactions. |
| 4537 | 21158384 | A 37-residue of human islet amyloid polypeptide (hIAPP or amylin) is a main component of amyloid plaques found in the pancreas of ∼90% of type II diabetes patients. |
| 4538 | 21163363 | Involvement of mitochondrial dysfunction in human islet amyloid polypeptide-induced apoptosis in INS-1E pancreatic beta cells: An effect attenuated by phycocyanin. |
| 4539 | 21163363 | Misfolded human islet amyloid polypeptide (hIAPP) in pancreatic islets is associated with the loss of insulin-secreting beta cells in type 2 diabetes. |
| 4540 | 21163363 | Further molecular analysis showed that hIAPP induced changes in the expression of Bcl-2 family members, release of cytochrome c and apoptosis-inducing factor (AIF) from mitochondria into cytosol, activation of caspases and cleavage of poly (ADP-ribose) polymerase. |
| 4541 | 21163363 | Involvement of mitochondrial dysfunction in human islet amyloid polypeptide-induced apoptosis in INS-1E pancreatic beta cells: An effect attenuated by phycocyanin. |
| 4542 | 21163363 | Misfolded human islet amyloid polypeptide (hIAPP) in pancreatic islets is associated with the loss of insulin-secreting beta cells in type 2 diabetes. |
| 4543 | 21163363 | Further molecular analysis showed that hIAPP induced changes in the expression of Bcl-2 family members, release of cytochrome c and apoptosis-inducing factor (AIF) from mitochondria into cytosol, activation of caspases and cleavage of poly (ADP-ribose) polymerase. |
| 4544 | 21170561 | The catalyst candidates were tested for their activity to cleave the soluble oligomers of amyloidogenic peptides amyloid β-42 and human islet amyloid polypeptide (h-IAPP), which are believed to be the pathogenic species for Alzheimer's disease and type 2 diabetes mellitus, respectively. |
| 4545 | 21175596 | Serum amyloid A (SAA) levels are elevated highly in acute phase response and elevated slightly and persistently in chronic diseases such as rheumatoid arthritis and diabetes. |
| 4546 | 21175596 | In addition, the expression of p47-phox was up-regulated by SAA (P < 0·001) and diphenyliodonium (DPI), a nicotinamide adenine dinucleotide phosphate (NADPH) oxidase inhibitor, reduced the release of O(2) (-) by 50%. |
| 4547 | 21195086 | Inhibition of glycosaminoglycan-mediated amyloid formation by islet amyloid polypeptide and proIAPP processing intermediates. |
| 4548 | 21195086 | Islet amyloid polypeptide (IAPP; also known as amylin) is responsible for islet amyloid formation in type 2 diabetes, and IAPP-induced toxicity is believed to contribute to the loss of β-cell mass associated with the late stages of type 2 diabetes. |
| 4549 | 21195086 | IAPP is produced as a prohormone, pro-islet amyloid polypeptide (proIAPP), and processed in the secretory granules of the pancreatic β-cells. |
| 4550 | 21195086 | Inhibition of glycosaminoglycan-mediated amyloid formation by islet amyloid polypeptide and proIAPP processing intermediates. |
| 4551 | 21195086 | Islet amyloid polypeptide (IAPP; also known as amylin) is responsible for islet amyloid formation in type 2 diabetes, and IAPP-induced toxicity is believed to contribute to the loss of β-cell mass associated with the late stages of type 2 diabetes. |
| 4552 | 21195086 | IAPP is produced as a prohormone, pro-islet amyloid polypeptide (proIAPP), and processed in the secretory granules of the pancreatic β-cells. |
| 4553 | 21195086 | Inhibition of glycosaminoglycan-mediated amyloid formation by islet amyloid polypeptide and proIAPP processing intermediates. |
| 4554 | 21195086 | Islet amyloid polypeptide (IAPP; also known as amylin) is responsible for islet amyloid formation in type 2 diabetes, and IAPP-induced toxicity is believed to contribute to the loss of β-cell mass associated with the late stages of type 2 diabetes. |
| 4555 | 21195086 | IAPP is produced as a prohormone, pro-islet amyloid polypeptide (proIAPP), and processed in the secretory granules of the pancreatic β-cells. |
| 4556 | 21215287 | A mechanistic approach for islet amyloid polypeptide aggregation to develop anti-amyloidogenic agents for type-2 diabetes. |
| 4557 | 21215287 | Type-2 diabetes mellitus (DM-2) is a conformational disease involving intrinsically disordered islet amyloid polypeptide (IAPP), in which a structural transition from physiological polypeptide to pathological deposits takes place. |
| 4558 | 21215287 | A mechanistic approach for islet amyloid polypeptide aggregation to develop anti-amyloidogenic agents for type-2 diabetes. |
| 4559 | 21215287 | Type-2 diabetes mellitus (DM-2) is a conformational disease involving intrinsically disordered islet amyloid polypeptide (IAPP), in which a structural transition from physiological polypeptide to pathological deposits takes place. |
| 4560 | 21218505 | Islet amyloid polypeptide acts on glucose- stimulated beta cells to reduce voltage-gated calcium channel activation, intracellular Ca(2+) concentration, and insulin secretion. |
| 4561 | 21239459 | To see whether molecules associated with acute phase protein, LPS signaling, and persistent recruitment of monocytes, are produced at higher amounts in adipocytes co-cultured with macrophages stimulated with low concentration of LPS (1 ng/ml), we measured serum amyloid A (SAA), LPS binding protein (LBP), soluble CD14 (sCD14), and RANTES levels in culture supernatant of co-cultures. |
| 4562 | 21239459 | Investigated molecules, especially LBP, SAA, and RANTES were produced at higher amounts in co-cultures stimulated with LPS compared with the cells without LPS. |
| 4563 | 21239459 | The ob/ob, and high-fat diet-induced obesity mice produced higher amounts of LBP, SAA, and RANTES one day after LPS infusion (1 ng/ml/g body weight) compared with ob/- and normal-fat fed control mice. |
| 4564 | 21251764 | Milk signalling down-regulates the key transcription factor FoxO1 leading to up-regulation of insulin promoter factor-1 which stimulates β-cell proliferation, insulin secretion as well as coexpression of islet amyloid polypeptide (IAPP). |
| 4565 | 21266844 | These amyloid deposits comprise predominantly of fibrillar aggregates of the 37-amino acid human amylin (hA) monomer, also known as islet amyloid polypeptide (IAPP), which is co-secreted with insulin from pancreatic islet β-cells via the regulated secretory pathway. hA has a propensity to aggregate in vitro into fibrillar structures through the self-association of monomers that is largely mediated by an amyloidogenic region spanning amino acids 20-29 (reviewed in ref. 8). |
| 4566 | 21281583 | Biphasic effects of insulin on islet amyloid polypeptide membrane disruption. |
| 4567 | 21281583 | Type II diabetes, in its late stages, is often associated with the formation of extracellular islet amyloid deposits composed of islet amyloid polypeptide (IAPP or amylin). |
| 4568 | 21281583 | Biphasic effects of insulin on islet amyloid polypeptide membrane disruption. |
| 4569 | 21281583 | Type II diabetes, in its late stages, is often associated with the formation of extracellular islet amyloid deposits composed of islet amyloid polypeptide (IAPP or amylin). |
| 4570 | 21281586 | The amyloid precursor protein (APP) is subject to proteolytic processing by γ-secretase within neuronal membranes, leading to Alzheimer's disease-associated β-amyloid peptide production by cleavage near the midpoint of the single transmembrane (TM) segment of APP. |
| 4571 | 21281635 | It has been shown that the expression of 3R tau is modulated by peptide amyloid β (Aβ) and that 3R tau levels increase with the progression of AD. |
| 4572 | 21298325 | Anti-inflammatory effect of insulin in the human hepatoma cell line HepG2 involves decreased transcription of IL-6 target genes and nuclear exclusion of FOXO1. |
| 4573 | 21298325 | The liver is an important target for interleukin-6 (IL-6) action leading to an increased inflammatory response with impaired insulin signaling and action. |
| 4574 | 21298325 | The aims of this study are to address if insulin is anti-inflammatory and attenuates IL-6-induced inflammation in the human hepatoma cell line HepG2 and if this involves signal transducer and activator of transcription 3 (STAT3) signal transduction. |
| 4575 | 21298325 | It was found that insulin significantly reduced IL-6-induced gene transcription of serum amyloid 1 (SAA1), serum amyloid 2 (SAA2), haptoglobin, orosomucoid, and plasmin activator inhibitor-1 (PAI-1). |
| 4576 | 21298325 | However, the authors did not find any evidence that insulin inhibited IL-6 signal transduction, i.e., no effect of insulin was detected on STAT3 phosphorylation or its translocation to cell nucleus. |
| 4577 | 21298325 | Taken together, these results suggest that the anti-inflammatory effect of insulin on IL-6 action is exerted at the level of the transcriptional activation of the genes. |
| 4578 | 21298325 | Further analysis revealed that insulin regulates nuclear localization of FOXO1, which is an important co-activator for STAT3 mediated transcription. |
| 4579 | 21298325 | Insulin induced nuclear exit and Thr24 phosphorylation of FOXO1, thus, inhibiting STAT3-mediated transcription. |
| 4580 | 21332024 | Subcutaneous adipose tissue biopsies were taken after 8 weeks treatment to analyze gene expression, glucose uptake capacity, insulin-signaling, and adipocyte size. |
| 4581 | 21332024 | Adipose tissue gene expression of serum amyloid A (SAA) was higher after hydrochlorothiazide treatment compared to candesartan (p=0.036), and this was in accordance with our previous finding on circulating SAA levels. |
| 4582 | 21347704 | RAGE is a pattern recognition receptor that binds to multiple ligands, including amphoterin, members of the S100/calgranulin family, the integrin Mac-1, and amyloid β-peptide (Aβ). |
| 4583 | 21352095 | Possible pathophysiologic mechanisms common to both T2DM and AD are glucose toxicity and a direct effect of insulin on amyloid metabolism. |
| 4584 | 21352095 | In fact, AD and T2DM have comparable pathological features in the islet and brain (amyloid derived from amyloid β protein (β-amyloid) in the brain in AD and islet amyloid derived from islet amyloid polypeptide in the pancreas in T2DM). |
| 4585 | 21352095 | Possible pathophysiologic mechanisms common to both T2DM and AD are glucose toxicity and a direct effect of insulin on amyloid metabolism. |
| 4586 | 21352095 | In fact, AD and T2DM have comparable pathological features in the islet and brain (amyloid derived from amyloid β protein (β-amyloid) in the brain in AD and islet amyloid derived from islet amyloid polypeptide in the pancreas in T2DM). |
| 4587 | 21404645 | [Amyloid fibril formation of islet amyloid polypeptide in the presence of lipid membrane and membrane disruption]. |
| 4588 | 21428404 | Heterogeneous triangular structures of human islet amyloid polypeptide (amylin) with internal hydrophobic cavity and external wrapping morphology reveal the polymorphic nature of amyloid fibrils. |
| 4589 | 21428404 | The misfolding and self-assembly of human islet amyloid polypeptide (hIAPP or amylin) into amyloid fibrils is pathologically linked to type II diabetes. |
| 4590 | 21428404 | Heterogeneous triangular structures of human islet amyloid polypeptide (amylin) with internal hydrophobic cavity and external wrapping morphology reveal the polymorphic nature of amyloid fibrils. |
| 4591 | 21428404 | The misfolding and self-assembly of human islet amyloid polypeptide (hIAPP or amylin) into amyloid fibrils is pathologically linked to type II diabetes. |
| 4592 | 21448434 | Redox regulation of insulin degradation by insulin-degrading enzyme. |
| 4593 | 21448434 | Insulin-degrading enzyme (IDE) is a thiol sensitive peptidase that degrades insulin and amyloid β, and has been linked to type 2 diabetes mellitus and Alzheimer's disease. |
| 4594 | 21448434 | Reduced glutathione had no effect on IDE, but reacted with partially degraded insulin to disrupt its disulfide bonds and accelerate its breakdown to trichloroacetic acid soluble fragments. |
| 4595 | 21448434 | Our results demonstrate the sensitivity of insulin degradation by IDE to the redox environment and suggest another mechanism by which the cell's oxidation state may contribute to the development of, and the link between, type 2 diabetes and Alzheimer's disease. |
| 4596 | 21452073 | FUS/TLS forms cytoplasmic aggregates, inhibits cell growth and interacts with TDP-43 in a yeast model of amyotrophic lateral sclerosis. |
| 4597 | 21452073 | Both wild-type and mutant forms of the RNA-binding proteins FUS and TDP-43 accumulate in cytoplasmic inclusions in the neurons of ALS patients. |
| 4598 | 21452073 | We find that FUS and TDP-43 have a high propensity for co-aggregation, unlike the aggregation patterns of several other aggregation-prone proteins. |
| 4599 | 21452073 | Moreover, the biophysical properties of FUS aggregates in yeast are distinctly different from many amyloidogenic proteins, suggesting they are not composed of amyloid. |
| 4600 | 21452804 | Influence of hydrophobicity on the surface-catalyzed assembly of the islet amyloid polypeptide. |
| 4601 | 21452804 | The islet amyloid polypeptide (IAPP) is a hormonal factor secreted by the β-cells in the pancreas. |
| 4602 | 21452804 | Influence of hydrophobicity on the surface-catalyzed assembly of the islet amyloid polypeptide. |
| 4603 | 21452804 | The islet amyloid polypeptide (IAPP) is a hormonal factor secreted by the β-cells in the pancreas. |
| 4604 | 21484213 | Exendin-4 increases islet amyloid deposition but offsets the resultant beta cell toxicity in human islet amyloid polypeptide transgenic mouse islets. |
| 4605 | 21502851 | Relation between insulin, insulin-related factors, and plasma amyloid beta peptide levels at midlife in a population-based study. |
| 4606 | 21516511 | AD pathology is driven by genetic factors related not to aging per se, but instead to the amyloid precursor protein (APP). |
| 4607 | 21517093 | The amyloid formation mechanism in human IAPP: dimers have β-strand monomer-monomer interfaces. |
| 4608 | 21519521 | Exogenous application of streptozotocin, which disrupts systemic insulin secretion, results in insulin deficiency, increased tau phosphorylation, and cognitive impairments that can be reversed by exogenous insulin supplementation. |
| 4609 | 21519521 | The symptoms of this AD pathology included increased tau phosphorylation at multiple sites, increased tau cleavage, and greater neuronal and synaptic damage, even with increased amyloid β protein production. |
| 4610 | 21523678 | Important inflammatory mediators, which take part in pathogenesis of ACS, are acute phase proteins such as: C-reactive protein, adhesion molecules VCAM-1, ICAM-1, selectins, plasma amyloid A, metalloproteinases, interleukins-1 and -6, tumour necrosis factor-a and vascular endothelial growth factor. |
| 4611 | 21534603 | Using these chiral vibrational signatures, we studied the aggregation of human islet amyloid polypeptide (hIAPP), which is implicated in type II diabetes. |
| 4612 | 21537460 | The islet amyloid polypeptide has been associated with β-cell apoptosis. |
| 4613 | 21543720 | In both of these diseases, a protein complex known as the inflammasome is stimulated to activate interleukin-1β (IL-1β) and IL-18, which are pathogenic inflammatory cytokines. |
| 4614 | 21543720 | Triggers for the inflammasome are obesity-related factors, such as cholesterol crystals in atherosclerosis, or hyperglycemia, ceramides, and islet amyloid polypeptide in type 2 diabetes. |
| 4615 | 21566116 | Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions. |
| 4616 | 21566116 | We studied the formation of fibrils of human islet amyloid polypeptide associated with type II diabetes in the presence of various concentrations of 1,1,1,3,3,3-hexafluoroisopropanol (HFIP) under acidic and neutral pH conditions using CD, amyloid-specific thioflavin T fluorescence, fluorescence imaging with thioflavin T, and atomic force microscopy. |
| 4617 | 21566116 | Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions. |
| 4618 | 21566116 | We studied the formation of fibrils of human islet amyloid polypeptide associated with type II diabetes in the presence of various concentrations of 1,1,1,3,3,3-hexafluoroisopropanol (HFIP) under acidic and neutral pH conditions using CD, amyloid-specific thioflavin T fluorescence, fluorescence imaging with thioflavin T, and atomic force microscopy. |
| 4619 | 21571086 | Prion protein (Prion diseases), amyloid-beta (Alzheimer's disease), alpha-synuclein (Parkinson's disease), Huntingtin (Huntington's disease), serum amyloid A (AA amyloidosis) and islet amyloid polypeptide (type 2 diabetes) are some of the proteins that trigger disease when they get misfolded. |
| 4620 | 21630409 | Alzheimer's disease (AD) and type 2 diabetes (T2D) are linked to the self-association of β-amyloid peptide (Aβ) and islet amyloid polypeptide (IAPP), respectively. |
| 4621 | 21633185 | Islet amyloid polypeptide in pancreatic islets from type 1 diabetic subjects. |
| 4622 | 21695120 | Drosophila melanogaster as a model system for studies of islet amyloid polypeptide aggregation. |
| 4623 | 21704966 | Intraocular expression of serum amyloid a and interleukin-6 in proliferative diabetic retinopathy. |
| 4624 | 21734016 | Islet amyloid polypeptide is a target antigen for diabetogenic CD4+ T cells. |
| 4625 | 21738623 | The expression of the receptor for advanced glycation end products (RAGE), serum amyloid A and serum C-reactive protein, markers of protein oxidation, glycation and inflammation, were also increased in diabetic Akita mice and reduced by fisetin. |
| 4626 | 21742788 | Islet amyloid polypeptide, islet amyloid, and diabetes mellitus. |
| 4627 | 21742788 | Islet amyloid polypeptide (IAPP, or amylin) is one of the major secretory products of β-cells of the pancreatic islets of Langerhans. |
| 4628 | 21742788 | Islet amyloid polypeptide, islet amyloid, and diabetes mellitus. |
| 4629 | 21742788 | Islet amyloid polypeptide (IAPP, or amylin) is one of the major secretory products of β-cells of the pancreatic islets of Langerhans. |
| 4630 | 21808014 | We find little difference in ATPase, protein refolding, and amyloid inhibiting activities of purified Ssa1p and Ssa2p, but show that interchanging NBD residue alanine 83 (Ssa1p) and glycine 83 (Ssa2p) switched functions of Ssa1p and Ssa2p in [URE3] propagation and FBPase degradation. |
| 4631 | 21813778 | IL-1 blockade attenuates islet amyloid polypeptide-induced proinflammatory cytokine release and pancreatic islet graft dysfunction. |
| 4632 | 21813778 | We sought to determine whether human islet amyloid polypeptide (hIAPP), the main component of islet amyloid, might contribute to islet inflammation by recruiting and activating macrophages. |
| 4633 | 21813778 | Early aggregates of hIAPP, but not nonamyloidogenic rodent islet amyloid polypeptide, caused release of CCL2 and CXCL1 by islets and induced secretion of TNF-α, IL-1α, IL-1β, CCL2, CCL3, CXCL1, CXCL2, and CXCL10 by C57BL/6 bone marrow-derived macrophages. hIAPP-induced TNF-α secretion was markedly diminished in MyD88-, but not TLR2- or TLR4-deficient macrophages, and in cells treated with the IL-1R antagonist (IL-1Ra) anakinra. |
| 4634 | 21813778 | Our results suggest that hIAPP-induced islet chemokine secretion promotes macrophage recruitment and that IL-1R/MyD88, but not TLR2 or TLR4 signaling is required for maximal macrophage responsiveness to prefibrillar hIAPP. |
| 4635 | 21813778 | IL-1 blockade attenuates islet amyloid polypeptide-induced proinflammatory cytokine release and pancreatic islet graft dysfunction. |
| 4636 | 21813778 | We sought to determine whether human islet amyloid polypeptide (hIAPP), the main component of islet amyloid, might contribute to islet inflammation by recruiting and activating macrophages. |
| 4637 | 21813778 | Early aggregates of hIAPP, but not nonamyloidogenic rodent islet amyloid polypeptide, caused release of CCL2 and CXCL1 by islets and induced secretion of TNF-α, IL-1α, IL-1β, CCL2, CCL3, CXCL1, CXCL2, and CXCL10 by C57BL/6 bone marrow-derived macrophages. hIAPP-induced TNF-α secretion was markedly diminished in MyD88-, but not TLR2- or TLR4-deficient macrophages, and in cells treated with the IL-1R antagonist (IL-1Ra) anakinra. |
| 4638 | 21813778 | Our results suggest that hIAPP-induced islet chemokine secretion promotes macrophage recruitment and that IL-1R/MyD88, but not TLR2 or TLR4 signaling is required for maximal macrophage responsiveness to prefibrillar hIAPP. |
| 4639 | 21813778 | IL-1 blockade attenuates islet amyloid polypeptide-induced proinflammatory cytokine release and pancreatic islet graft dysfunction. |
| 4640 | 21813778 | We sought to determine whether human islet amyloid polypeptide (hIAPP), the main component of islet amyloid, might contribute to islet inflammation by recruiting and activating macrophages. |
| 4641 | 21813778 | Early aggregates of hIAPP, but not nonamyloidogenic rodent islet amyloid polypeptide, caused release of CCL2 and CXCL1 by islets and induced secretion of TNF-α, IL-1α, IL-1β, CCL2, CCL3, CXCL1, CXCL2, and CXCL10 by C57BL/6 bone marrow-derived macrophages. hIAPP-induced TNF-α secretion was markedly diminished in MyD88-, but not TLR2- or TLR4-deficient macrophages, and in cells treated with the IL-1R antagonist (IL-1Ra) anakinra. |
| 4642 | 21813778 | Our results suggest that hIAPP-induced islet chemokine secretion promotes macrophage recruitment and that IL-1R/MyD88, but not TLR2 or TLR4 signaling is required for maximal macrophage responsiveness to prefibrillar hIAPP. |
| 4643 | 21818468 | This tutorial review presents descriptions of two amyloidogenic proteins, amyloid-β (Aβ) peptides and islet amyloid polypeptide (IAPP), whose misfolding propensities are implicated in Alzheimer's disease (AD) and type II diabetes, respectively. |
| 4644 | 21822534 | Pen-2 is a key regulator of the γ-secretase complex, which is involved in the production of the amyloid β (Aβ)-42 peptides, which ultimately lead to Alzheimer's disease (AD). |
| 4645 | 21822534 | NSE/hPen-2 Tg mice were produced by the microinjection of the NSE/hPen-2 gene into the pronucleus of fertilized eggs. |
| 4646 | 21822534 | The expression of the hPen-2 gene under the control of the NSE promoter was successfully detected only in the brain and kidney tissue of NSE/hPen-2 Tg mice. |
| 4647 | 21822534 | Also, 12-month-old NSE/hPen-2 Tg mice displayed behavioral dysfunction in the water maze test, motor activity and feeding behavior dysfunction in food intake/water intake/motor activity monitoring system. |
| 4648 | 21822534 | Furthermore, NSE/hPen-2 Tg mice exhibiting feeding behavior dysfunction were significantly more apt to display symptoms related to diabetes and obesity. |
| 4649 | 21822534 | These results suggest that Pen-2 overexpression in NSE/hPen-2 Tg mice may induce all the AD-like phenotypes, including behavioral deficits, motor activity and feeding behavior dysfunction, Aβ-42 peptide deposition and chronic disease induction. |
| 4650 | 21907142 | Here we identified, through a siRNA screen, beta site amyloid precursor protein cleaving enzyme 2 (Bace2) as the sheddase of the proproliferative plasma membrane protein Tmem27 in murine and human β cells. |
| 4651 | 21907142 | Mice with functionally inactive Bace2 and insulin-resistant mice treated with a newly identified Bace2 inhibitor both display augmented β cell mass and improved control of glucose homeostasis due to increased insulin levels. |
| 4652 | 21917439 | CD4T cells are attracted to islets by β-cell antigens which include insulin and the two new autoantigens, chromogranin A and islet amyloid polypeptide, all proteins of the secretory granule. |
| 4653 | 21917439 | Peptides of insulin and ChgA bind to the NOD class II molecule in an unconventional manner and since autoantigenic peptides may typically bind to MHC with low affinity, it is postulated that post-translational modifications of β-cell peptides could contribute to the interaction between peptides, MHC, and the autoreactive TCR. |
| 4654 | 21921296 | To address this, the authors examined the metabolic and physiological consequences of experimentally controlled circadian rhythm disruption in wild-type (WT) Sprague Dawley and diabetes-prone human islet amyloid polypeptide transgenic (HIP) rats: a validated model of T2DM. |
| 4655 | 21966328 | Amylin, (islet amyloid polypeptide) or diabetes-associated peptide is co-secreted with insulin in the islet of Langerhans of diabetic patients in approximately 1:100, amylin-insulin ratio. |
| 4656 | 21984830 | Involvement of ATP-sensitive potassium (K(ATP)) channels in the loss of beta-cell function induced by human islet amyloid polypeptide. |
| 4657 | 21984830 | Islet amyloid polypeptide (IAPP) is a major component of amyloid deposition in pancreatic islets of patients with type 2 diabetes. |
| 4658 | 21984830 | Involvement of ATP-sensitive potassium (K(ATP)) channels in the loss of beta-cell function induced by human islet amyloid polypeptide. |
| 4659 | 21984830 | Islet amyloid polypeptide (IAPP) is a major component of amyloid deposition in pancreatic islets of patients with type 2 diabetes. |
| 4660 | 21986708 | Serum amyloid A is a growth factor for 3T3-L1 adipocytes, inhibits differentiation and promotes insulin resistance. |
| 4661 | 22000494 | The mechanisms of action include a decrease of hepatic insulin resistance, change in bile acids metabolism, incretins release and decreased amyloid deposits. |
| 4662 | 22003494 | Co-assembly of human islet amyloid polypeptide (hIAPP)/insulin. |
| 4663 | 22038516 | cJUN N-terminal kinase (JNK) activation mediates islet amyloid-induced beta cell apoptosis in cultured human islet amyloid polypeptide transgenic mouse islets. |
| 4664 | 22057897 | Insulin receptor signaling mediates APP processing and β-amyloid accumulation without altering survival in a transgenic mouse model of Alzheimer's disease. |
| 4665 | 22057897 | In brains from patients with Alzheimer's disease (AD), expression of insulin receptor (IR), insulin-like growth factor-1 receptor (IGF-1R), and insulin receptor substrate proteins is downregulated. |
| 4666 | 22057897 | A key step in the pathogenesis of AD is the accumulation of amyloid precursor protein (APP) cleavage products, β-amyloid (Aβ)(1-42) and Aβ(1-40). |
| 4667 | 22057897 | Analyzing APP C-terminal fragments (CTF) revealed decreased α-/β-CTFs in the brains of nIR(-/-)Tg2576 mice suggesting decreased APP processing. |
| 4668 | 22057897 | Cell based experiments showed that inhibition of the PI3-kinase pathway suppresses endosomal APP cleavage and decreases α- as well as β-secretase activity. |
| 4669 | 22057897 | Deletion of only one copy of the neuronal IGF-1R partially rescues the premature mortality of Tg2576 mice without altering total amyloid load. |
| 4670 | 22057897 | Analysis of Tg2576 mice expressing either a dominant negative or constitutively active form of forkhead box-O (FoxO)1 did not reveal any alteration of amyloid burden, APP processing and did not rescue premature mortality in these mice. |
| 4671 | 22057897 | But exclusively decreased IGF-1R expression reduces AD-associated mortality independent of β-amyloid accumulation and FoxO1-mediated transcription. |
| 4672 | 22057897 | Insulin receptor signaling mediates APP processing and β-amyloid accumulation without altering survival in a transgenic mouse model of Alzheimer's disease. |
| 4673 | 22057897 | In brains from patients with Alzheimer's disease (AD), expression of insulin receptor (IR), insulin-like growth factor-1 receptor (IGF-1R), and insulin receptor substrate proteins is downregulated. |
| 4674 | 22057897 | A key step in the pathogenesis of AD is the accumulation of amyloid precursor protein (APP) cleavage products, β-amyloid (Aβ)(1-42) and Aβ(1-40). |
| 4675 | 22057897 | Analyzing APP C-terminal fragments (CTF) revealed decreased α-/β-CTFs in the brains of nIR(-/-)Tg2576 mice suggesting decreased APP processing. |
| 4676 | 22057897 | Cell based experiments showed that inhibition of the PI3-kinase pathway suppresses endosomal APP cleavage and decreases α- as well as β-secretase activity. |
| 4677 | 22057897 | Deletion of only one copy of the neuronal IGF-1R partially rescues the premature mortality of Tg2576 mice without altering total amyloid load. |
| 4678 | 22057897 | Analysis of Tg2576 mice expressing either a dominant negative or constitutively active form of forkhead box-O (FoxO)1 did not reveal any alteration of amyloid burden, APP processing and did not rescue premature mortality in these mice. |
| 4679 | 22057897 | But exclusively decreased IGF-1R expression reduces AD-associated mortality independent of β-amyloid accumulation and FoxO1-mediated transcription. |
| 4680 | 22057897 | Insulin receptor signaling mediates APP processing and β-amyloid accumulation without altering survival in a transgenic mouse model of Alzheimer's disease. |
| 4681 | 22057897 | In brains from patients with Alzheimer's disease (AD), expression of insulin receptor (IR), insulin-like growth factor-1 receptor (IGF-1R), and insulin receptor substrate proteins is downregulated. |
| 4682 | 22057897 | A key step in the pathogenesis of AD is the accumulation of amyloid precursor protein (APP) cleavage products, β-amyloid (Aβ)(1-42) and Aβ(1-40). |
| 4683 | 22057897 | Analyzing APP C-terminal fragments (CTF) revealed decreased α-/β-CTFs in the brains of nIR(-/-)Tg2576 mice suggesting decreased APP processing. |
| 4684 | 22057897 | Cell based experiments showed that inhibition of the PI3-kinase pathway suppresses endosomal APP cleavage and decreases α- as well as β-secretase activity. |
| 4685 | 22057897 | Deletion of only one copy of the neuronal IGF-1R partially rescues the premature mortality of Tg2576 mice without altering total amyloid load. |
| 4686 | 22057897 | Analysis of Tg2576 mice expressing either a dominant negative or constitutively active form of forkhead box-O (FoxO)1 did not reveal any alteration of amyloid burden, APP processing and did not rescue premature mortality in these mice. |
| 4687 | 22057897 | But exclusively decreased IGF-1R expression reduces AD-associated mortality independent of β-amyloid accumulation and FoxO1-mediated transcription. |
| 4688 | 22064122 | Here we test backbone contributions to fibril stability using analogs of the 6-10 residue fibril core of human islet amyloid polypeptide, a 37 amino acid peptide involved in the pathogenesis of type II diabetes. |
| 4689 | 22075273 | Short-term walnut consumption increases circulating total adiponectin and apolipoprotein A concentrations, but does not affect markers of inflammation or vascular injury in obese humans with the metabolic syndrome: data from a double-blinded, randomized, placebo-controlled study. |
| 4690 | 22075273 | Consumption of walnuts was associated with a statistically significant increase in serum apolipoprotein A concentrations (P = .03), but did not affect circulating levels of fetuin A, resistin, C-reactive protein, serum amyloid A, soluble intercellular adhesion molecules 1 and 3, soluble vascular cell adhesion protein 1, interleukins 6 and 8, tumor necrosis factor α, E-selectin, P-selectin, and thrombomodulin. |
| 4691 | 22098747 | TTR is found in amyloid deposits of patients with senile systemic amyloidosis. |
| 4692 | 22098747 | TTR mutants lead to familial amyloidotic polyneuropathy and familial amyloid cardiomyopathy, with an earlier age of onset. |
| 4693 | 22098747 | Studies of amyloid fibrils of familial amyloidotic polyneuropathy mutant TTR suggest a structure similar to the native state with only a simple opening of a β-strand-loop-strand region exposing the two main β-sheets of the protein for fibril elongation. |
| 4694 | 22098747 | However, we find that the wild-type TTR sequence forms amyloid fibrils that are considerably different from the previously suggested amyloid structure. |
| 4695 | 22098747 | We also find that the TTR amyloid is incapable of binding thyroxine as monitored by either isothermal calorimetry or 1,8-anilinonaphthalene sulfonate competition. |
| 4696 | 22098747 | TTR is found in amyloid deposits of patients with senile systemic amyloidosis. |
| 4697 | 22098747 | TTR mutants lead to familial amyloidotic polyneuropathy and familial amyloid cardiomyopathy, with an earlier age of onset. |
| 4698 | 22098747 | Studies of amyloid fibrils of familial amyloidotic polyneuropathy mutant TTR suggest a structure similar to the native state with only a simple opening of a β-strand-loop-strand region exposing the two main β-sheets of the protein for fibril elongation. |
| 4699 | 22098747 | However, we find that the wild-type TTR sequence forms amyloid fibrils that are considerably different from the previously suggested amyloid structure. |
| 4700 | 22098747 | We also find that the TTR amyloid is incapable of binding thyroxine as monitored by either isothermal calorimetry or 1,8-anilinonaphthalene sulfonate competition. |
| 4701 | 22098747 | TTR is found in amyloid deposits of patients with senile systemic amyloidosis. |
| 4702 | 22098747 | TTR mutants lead to familial amyloidotic polyneuropathy and familial amyloid cardiomyopathy, with an earlier age of onset. |
| 4703 | 22098747 | Studies of amyloid fibrils of familial amyloidotic polyneuropathy mutant TTR suggest a structure similar to the native state with only a simple opening of a β-strand-loop-strand region exposing the two main β-sheets of the protein for fibril elongation. |
| 4704 | 22098747 | However, we find that the wild-type TTR sequence forms amyloid fibrils that are considerably different from the previously suggested amyloid structure. |
| 4705 | 22098747 | We also find that the TTR amyloid is incapable of binding thyroxine as monitored by either isothermal calorimetry or 1,8-anilinonaphthalene sulfonate competition. |
| 4706 | 22098747 | TTR is found in amyloid deposits of patients with senile systemic amyloidosis. |
| 4707 | 22098747 | TTR mutants lead to familial amyloidotic polyneuropathy and familial amyloid cardiomyopathy, with an earlier age of onset. |
| 4708 | 22098747 | Studies of amyloid fibrils of familial amyloidotic polyneuropathy mutant TTR suggest a structure similar to the native state with only a simple opening of a β-strand-loop-strand region exposing the two main β-sheets of the protein for fibril elongation. |
| 4709 | 22098747 | However, we find that the wild-type TTR sequence forms amyloid fibrils that are considerably different from the previously suggested amyloid structure. |
| 4710 | 22098747 | We also find that the TTR amyloid is incapable of binding thyroxine as monitored by either isothermal calorimetry or 1,8-anilinonaphthalene sulfonate competition. |
| 4711 | 22098747 | TTR is found in amyloid deposits of patients with senile systemic amyloidosis. |
| 4712 | 22098747 | TTR mutants lead to familial amyloidotic polyneuropathy and familial amyloid cardiomyopathy, with an earlier age of onset. |
| 4713 | 22098747 | Studies of amyloid fibrils of familial amyloidotic polyneuropathy mutant TTR suggest a structure similar to the native state with only a simple opening of a β-strand-loop-strand region exposing the two main β-sheets of the protein for fibril elongation. |
| 4714 | 22098747 | However, we find that the wild-type TTR sequence forms amyloid fibrils that are considerably different from the previously suggested amyloid structure. |
| 4715 | 22098747 | We also find that the TTR amyloid is incapable of binding thyroxine as monitored by either isothermal calorimetry or 1,8-anilinonaphthalene sulfonate competition. |
| 4716 | 22165048 | The findings were consistent with nodular cutaneous amyloidosis (NCA) of the amyloid light-type. |
| 4717 | 22178988 | In this study, we compared indexes of peripheral neuropathy and investigated insulin signaling in the sciatic nerve of insulin-deficient mice and amyloid precursor protein (APP) overexpressing transgenic mice. |
| 4718 | 22178988 | Insulin-deficient and APP transgenic mice displayed similar patterns of peripheral neuropathy with decreased motor nerve conduction velocity, thermal hypoalgesia, and loss of tactile sensitivity. |
| 4719 | 22178988 | Phosphorylation of the insulin receptor and glycogen synthase kinase 3β (GSK3β) was similarly affected in insulin-deficient and APP transgenic mice despite significantly different blood glucose and plasma insulin levels, and nerve of both models showed accumulation of Aβ-immunoreactive protein. |
| 4720 | 22183778 | Concentration-dependent transitions govern the subcellular localization of islet amyloid polypeptide. |
| 4721 | 22183778 | Islet amyloid polypeptide (IAPP) is a peptide hormone cosecreted with insulin by pancreatic β-cells. |
| 4722 | 22183778 | Concentration-dependent transitions govern the subcellular localization of islet amyloid polypeptide. |
| 4723 | 22183778 | Islet amyloid polypeptide (IAPP) is a peptide hormone cosecreted with insulin by pancreatic β-cells. |
| 4724 | 22197104 | Here, we demonstrated that HFD markedly deteriorated memory impairment and increased β-amyloid (Aβ) oligomers as well as Aβ deposition in amyloid precursor protein (APP) transgenic mice, which was reversed by exposure to an enriched environment for 10 weeks, despite the continuation of HFD. |
| 4725 | 22206987 | Sensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20. |
| 4726 | 22206987 | Islet amyloid polypeptide (IAPP, amylin) is responsible for amyloid formation in type 2 diabetes and in islet cell transplants. |
| 4727 | 22206987 | Sensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20. |
| 4728 | 22206987 | Islet amyloid polypeptide (IAPP, amylin) is responsible for amyloid formation in type 2 diabetes and in islet cell transplants. |
| 4729 | 22210153 | Amphiphilic adsorption of human islet amyloid polypeptide aggregates to lipid/aqueous interfaces. |
| 4730 | 22238175 | Morin hydrate inhibits amyloid formation by islet amyloid polypeptide and disaggregates amyloid fibers. |
| 4731 | 22238175 | The polypeptide hormone Islet Amyloid Polypeptide (IAPP, amylin) is responsible for islet amyloid formation in type-2 diabetes and in islet cell transplants, where it may contribute to graft failure. |
| 4732 | 22238175 | Morin hydrate inhibits amyloid formation by islet amyloid polypeptide and disaggregates amyloid fibers. |
| 4733 | 22238175 | The polypeptide hormone Islet Amyloid Polypeptide (IAPP, amylin) is responsible for islet amyloid formation in type-2 diabetes and in islet cell transplants, where it may contribute to graft failure. |
| 4734 | 22238252 | Depolymerization of insulin amyloid fibrils by albumin-modified magnetic fluid. |
| 4735 | 22238252 | We have studied the interference of insulin amyloid fibrils with a series of 18 albumin magnetic fluids (MFBSAs) consisting of magnetite nanoparticles modified by different amounts of bovine serum albumin (w/w BSA/Fe₃O₄ from 0.005 up to 15). |
| 4736 | 22238252 | Depolymerization of insulin amyloid fibrils by albumin-modified magnetic fluid. |
| 4737 | 22238252 | We have studied the interference of insulin amyloid fibrils with a series of 18 albumin magnetic fluids (MFBSAs) consisting of magnetite nanoparticles modified by different amounts of bovine serum albumin (w/w BSA/Fe₃O₄ from 0.005 up to 15). |
| 4738 | 22274563 | Apcs, encoding an acute phase response protein serum amyloid P (SAP), is located underneath the linkage peak of Bglu3. |
| 4739 | 22274563 | The Western diet consumption led to a gradual rise in plasma SAP levels, which was accompanied by rising fasting glucose in both B6 and C3H apoE(-/-) mice. |
| 4740 | 22301943 | Deletion of Fas protects islet beta cells from cytotoxic effects of human islet amyloid polypeptide. |
| 4741 | 22301943 | We used islet beta cells as well as two ex vivo models of islet amyloid formation, cultured human islets and hIAPP-expressing transgenic mouse islets with or without beta cell Fas deletion, to test whether: (1) the aggregation of endogenous hIAPP induces Fas upregulation in beta cells; and (2) deletion or blocking of Fas protects beta cells from amyloid toxicity. |
| 4742 | 22301943 | METHODS: INS-1, mouse or human islet cells were cultured with hIAPP alone, or with amyloid inhibitor or Fas antagonist. |
| 4743 | 22301943 | The amyloid inhibitor or Fas antagonist reduced apoptosis in hIAPP-treated beta cells. |
| 4744 | 22301943 | Ad-ProhIAPP-siRNA-mediated amyloid inhibition reduced Fas upregulation and IL-1β immunoreactivity in human and hIAPP-expressing mouse islets. |
| 4745 | 22301943 | Cultured hIAPP-expressing mouse islets with Fas deletion had similar amyloid levels, but lower caspase-3 activation and beta cell apoptosis, and a higher islet beta:alpha cell ratio and insulin response to glucose, compared with islets expressing Fas and hIAPP. |
| 4746 | 22301943 | Deletion of Fas protects islet beta cells from cytotoxic effects of human islet amyloid polypeptide. |
| 4747 | 22301943 | We used islet beta cells as well as two ex vivo models of islet amyloid formation, cultured human islets and hIAPP-expressing transgenic mouse islets with or without beta cell Fas deletion, to test whether: (1) the aggregation of endogenous hIAPP induces Fas upregulation in beta cells; and (2) deletion or blocking of Fas protects beta cells from amyloid toxicity. |
| 4748 | 22301943 | METHODS: INS-1, mouse or human islet cells were cultured with hIAPP alone, or with amyloid inhibitor or Fas antagonist. |
| 4749 | 22301943 | The amyloid inhibitor or Fas antagonist reduced apoptosis in hIAPP-treated beta cells. |
| 4750 | 22301943 | Ad-ProhIAPP-siRNA-mediated amyloid inhibition reduced Fas upregulation and IL-1β immunoreactivity in human and hIAPP-expressing mouse islets. |
| 4751 | 22301943 | Cultured hIAPP-expressing mouse islets with Fas deletion had similar amyloid levels, but lower caspase-3 activation and beta cell apoptosis, and a higher islet beta:alpha cell ratio and insulin response to glucose, compared with islets expressing Fas and hIAPP. |
| 4752 | 22301943 | Deletion of Fas protects islet beta cells from cytotoxic effects of human islet amyloid polypeptide. |
| 4753 | 22301943 | We used islet beta cells as well as two ex vivo models of islet amyloid formation, cultured human islets and hIAPP-expressing transgenic mouse islets with or without beta cell Fas deletion, to test whether: (1) the aggregation of endogenous hIAPP induces Fas upregulation in beta cells; and (2) deletion or blocking of Fas protects beta cells from amyloid toxicity. |
| 4754 | 22301943 | METHODS: INS-1, mouse or human islet cells were cultured with hIAPP alone, or with amyloid inhibitor or Fas antagonist. |
| 4755 | 22301943 | The amyloid inhibitor or Fas antagonist reduced apoptosis in hIAPP-treated beta cells. |
| 4756 | 22301943 | Ad-ProhIAPP-siRNA-mediated amyloid inhibition reduced Fas upregulation and IL-1β immunoreactivity in human and hIAPP-expressing mouse islets. |
| 4757 | 22301943 | Cultured hIAPP-expressing mouse islets with Fas deletion had similar amyloid levels, but lower caspase-3 activation and beta cell apoptosis, and a higher islet beta:alpha cell ratio and insulin response to glucose, compared with islets expressing Fas and hIAPP. |
| 4758 | 22301943 | Deletion of Fas protects islet beta cells from cytotoxic effects of human islet amyloid polypeptide. |
| 4759 | 22301943 | We used islet beta cells as well as two ex vivo models of islet amyloid formation, cultured human islets and hIAPP-expressing transgenic mouse islets with or without beta cell Fas deletion, to test whether: (1) the aggregation of endogenous hIAPP induces Fas upregulation in beta cells; and (2) deletion or blocking of Fas protects beta cells from amyloid toxicity. |
| 4760 | 22301943 | METHODS: INS-1, mouse or human islet cells were cultured with hIAPP alone, or with amyloid inhibitor or Fas antagonist. |
| 4761 | 22301943 | The amyloid inhibitor or Fas antagonist reduced apoptosis in hIAPP-treated beta cells. |
| 4762 | 22301943 | Ad-ProhIAPP-siRNA-mediated amyloid inhibition reduced Fas upregulation and IL-1β immunoreactivity in human and hIAPP-expressing mouse islets. |
| 4763 | 22301943 | Cultured hIAPP-expressing mouse islets with Fas deletion had similar amyloid levels, but lower caspase-3 activation and beta cell apoptosis, and a higher islet beta:alpha cell ratio and insulin response to glucose, compared with islets expressing Fas and hIAPP. |
| 4764 | 22301943 | Deletion of Fas protects islet beta cells from cytotoxic effects of human islet amyloid polypeptide. |
| 4765 | 22301943 | We used islet beta cells as well as two ex vivo models of islet amyloid formation, cultured human islets and hIAPP-expressing transgenic mouse islets with or without beta cell Fas deletion, to test whether: (1) the aggregation of endogenous hIAPP induces Fas upregulation in beta cells; and (2) deletion or blocking of Fas protects beta cells from amyloid toxicity. |
| 4766 | 22301943 | METHODS: INS-1, mouse or human islet cells were cultured with hIAPP alone, or with amyloid inhibitor or Fas antagonist. |
| 4767 | 22301943 | The amyloid inhibitor or Fas antagonist reduced apoptosis in hIAPP-treated beta cells. |
| 4768 | 22301943 | Ad-ProhIAPP-siRNA-mediated amyloid inhibition reduced Fas upregulation and IL-1β immunoreactivity in human and hIAPP-expressing mouse islets. |
| 4769 | 22301943 | Cultured hIAPP-expressing mouse islets with Fas deletion had similar amyloid levels, but lower caspase-3 activation and beta cell apoptosis, and a higher islet beta:alpha cell ratio and insulin response to glucose, compared with islets expressing Fas and hIAPP. |
| 4770 | 22301943 | Deletion of Fas protects islet beta cells from cytotoxic effects of human islet amyloid polypeptide. |
| 4771 | 22301943 | We used islet beta cells as well as two ex vivo models of islet amyloid formation, cultured human islets and hIAPP-expressing transgenic mouse islets with or without beta cell Fas deletion, to test whether: (1) the aggregation of endogenous hIAPP induces Fas upregulation in beta cells; and (2) deletion or blocking of Fas protects beta cells from amyloid toxicity. |
| 4772 | 22301943 | METHODS: INS-1, mouse or human islet cells were cultured with hIAPP alone, or with amyloid inhibitor or Fas antagonist. |
| 4773 | 22301943 | The amyloid inhibitor or Fas antagonist reduced apoptosis in hIAPP-treated beta cells. |
| 4774 | 22301943 | Ad-ProhIAPP-siRNA-mediated amyloid inhibition reduced Fas upregulation and IL-1β immunoreactivity in human and hIAPP-expressing mouse islets. |
| 4775 | 22301943 | Cultured hIAPP-expressing mouse islets with Fas deletion had similar amyloid levels, but lower caspase-3 activation and beta cell apoptosis, and a higher islet beta:alpha cell ratio and insulin response to glucose, compared with islets expressing Fas and hIAPP. |
| 4776 | 22334700 | Islet amyloid polypeptide triggers limited complement activation and binds complement inhibitor C4b-binding protein, which enhances fibril formation. |
| 4777 | 22334700 | Islet amyloid polypeptide (IAPP) is synthesized in pancreatic β-cells and co-secreted with insulin. |
| 4778 | 22334700 | Furthermore, IAPP also bound complement inhibitors factor H and C4b-binding protein (C4BP). |
| 4779 | 22334700 | Immunostaining of pancreatic sections from type 2 diabetic patients revealed the presence of complement factors in the islets and varying degree of co-localization between IAPP fibrils and C1q, C3d, as well as C4BP and factor H but not membrane attack complex. |
| 4780 | 22334700 | Islet amyloid polypeptide triggers limited complement activation and binds complement inhibitor C4b-binding protein, which enhances fibril formation. |
| 4781 | 22334700 | Islet amyloid polypeptide (IAPP) is synthesized in pancreatic β-cells and co-secreted with insulin. |
| 4782 | 22334700 | Furthermore, IAPP also bound complement inhibitors factor H and C4b-binding protein (C4BP). |
| 4783 | 22334700 | Immunostaining of pancreatic sections from type 2 diabetic patients revealed the presence of complement factors in the islets and varying degree of co-localization between IAPP fibrils and C1q, C3d, as well as C4BP and factor H but not membrane attack complex. |
| 4784 | 22355065 | In two islet recipients with no evidence of rejection and still normoglycemic and insulin independent at the first detection of amyloid, β-cell secretory capacity declined over time coincident with increasing amyloid severity and decreasing β-cell area, with both animals eventually becoming hyperglycemic and insulin dependent. |
| 4785 | 22363506 | However, it was extremely thermodynamically stable and did not form amyloid fibrils when subjected to mechanical stress, underlining the importance of oligomerization for insulin stability. |
| 4786 | 22366091 | Silibinin inhibits the toxic aggregation of human islet amyloid polypeptide. |
| 4787 | 22366091 | In type 2 diabetes mellitus (T2DM), misfolded human islet amyloid polypeptide (hIAPP) forms amyloid deposits in pancreatic islets. |
| 4788 | 22366091 | Silibinin inhibits the toxic aggregation of human islet amyloid polypeptide. |
| 4789 | 22366091 | In type 2 diabetes mellitus (T2DM), misfolded human islet amyloid polypeptide (hIAPP) forms amyloid deposits in pancreatic islets. |
| 4790 | 22403710 | In this study, we applied streptozotocin (STZ) to induce experimental diabetes in AD transgenic mice (5XFAD model) and investigated how insulin deficiency affects the β-amyloidogenic processing of amyloid precursor protein (APP). |
| 4791 | 22403710 | Importantly, STZ-induced insulin deficiency upregulated levels of both β-site APP cleaving enzyme 1 (BACE1) and full-length APP in 5XFAD mouse brains, which was accompanied by dramatic elevations in the β-cleaved C-terminal fragment (C99). |
| 4792 | 22403710 | Interestingly, BACE1 mRNA levels were not affected, whereas phosphorylation of the translation initiation factor eIF2α, a mechanism proposed to mediate the post-transcriptional upregulation of BACE1, was significantly elevated in STZ-treated 5XFAD mice. |
| 4793 | 22403710 | Moreover, STZ treatments did not affect levels of Aβ-degrading enzymes such as neprilysin and insulin-degrading enzyme (IDE) in 5XFAD brains. |
| 4794 | 22403710 | Taken together, our findings provide a mechanistic foundation for a link between diabetes and AD by demonstrating that insulin deficiency may change APP processing to favor β-amyloidogenesis via the translational upregulation of BACE1 in combination with elevations in its substrate, APP. |
| 4795 | 22404928 | How type II diabetes-related islet amyloid polypeptide damages lipid bilayers. |
| 4796 | 22404928 | A leading hypothesis for the decimation of insulin-producing β-cells in type 2 diabetes attributes the cause to islet amyloid polypeptide (IAPP) for its deleterious effects on the cell membranes. |
| 4797 | 22404928 | How type II diabetes-related islet amyloid polypeptide damages lipid bilayers. |
| 4798 | 22404928 | A leading hypothesis for the decimation of insulin-producing β-cells in type 2 diabetes attributes the cause to islet amyloid polypeptide (IAPP) for its deleterious effects on the cell membranes. |
| 4799 | 22406002 | In the Sydney Memory and Aging Study, the relationships between remitted depression, current and first onset of symptoms of depression or anxiety (Geriatric Depression Scale and Goldberg Anxiety Scale (GDS, GAS), and markers of systemic inflammation (C-reactive protein (CRP), interleukins-1β, -6, -8, -10, -12, plasminogen activator inhibitor-1 (PAI-1), serum amyloid A, tumor necrosis factor-α, and vascular adhesion molecule-1) were investigated. |
| 4800 | 22406002 | The results show a significant linear relationship between increasing levels of IL-6 and depressive symptoms at baseline only, whereas IL-8 was associated with depressed symptoms at baseline and at 2 years follow-up. |
| 4801 | 22406002 | The findings are suggestive of IL-6 and IL-8 being associated with current symptoms and IL-8 being associated with first onset of depressive symptoms, whereas PAI-1 could be regarded as a marker of remitted depression. |
| 4802 | 22408171 | Translational control of glucose-induced islet amyloid polypeptide production in pancreatic islets. |
| 4803 | 22408171 | Dysfunctional islet amyloid polypeptide (IAPP) biosynthesis and/or processing are thought contribute to formation of islet amyloid in type 2 diabetes. |
| 4804 | 22408171 | Here, it was found that acute exposure to high glucose concentrations coordinately regulated the biosynthesis of pro-IAPP, proinsulin, and its proprotein convertase PC1/3 in normal isolated rat islets, without affecting their respective mRNA levels. |
| 4805 | 22408171 | Translational control of glucose-induced islet amyloid polypeptide production in pancreatic islets. |
| 4806 | 22408171 | Dysfunctional islet amyloid polypeptide (IAPP) biosynthesis and/or processing are thought contribute to formation of islet amyloid in type 2 diabetes. |
| 4807 | 22408171 | Here, it was found that acute exposure to high glucose concentrations coordinately regulated the biosynthesis of pro-IAPP, proinsulin, and its proprotein convertase PC1/3 in normal isolated rat islets, without affecting their respective mRNA levels. |
| 4808 | 22411248 | Some basic research, however, suggests that insulin accelerates Alzheimer-related pathology through its effects on the amyloid beta (Aβ) metabolism and tau phosphorylation.Asymptomatic ischemic lesions in T2DM subjects may lower the threshold for the development of dementia and this may explain the inconsistency between the basic research and clinicopathological studies.More research to elucidate the mechanism of neurodegeneration associated with T2DM is warranted. |
| 4809 | 22425595 | The pathological hallmarks for AD brains are extracellular amyloid plaques formed by β-amyloid peptide (Aβ) and intracellular neurofibrillary tangles consisting of hyperphosphorylated tau protein. |
| 4810 | 22425595 | Activated/phosphorylated c-jun N-terminal kinase (JNK), a tau kinase, was increased in the db/db mouse hippocampus. |
| 4811 | 22425595 | Metformin attenuated the increase of total tau, phospho-tau and activated JNK. |
| 4812 | 22488522 | Here we tested their generic properties and their ability to inhibit other amyloidogenic proteins including α-synuclein, islet amyloid polypeptide, lysozyme, calcitonin, and insulin. |
| 4813 | 22500019 | The two age-prevalent diseases Alzheimer disease and type 2 diabetes mellitus share many common features including the deposition of amyloidogenic proteins, amyloid β protein (Aβ) and amylin (islet amyloid polypeptide), respectively. |
| 4814 | 22500019 | Aβ1-42 and human amylin (hAmylin) increase cytosolic cAMP and Ca(2+), trigger multiple pathways involving the signal transduction mediators protein kinase A, MAPK, Akt, and cFos. |
| 4815 | 22500019 | Amylin receptor antagonist AC253 blocks increases in intracellular Ca(2+), activation of protein kinase A, MAPK, Akt, cFos, and cell death, which occur upon AMY3 activation with hAmylin, Aβ1-42, or their co-application. |
| 4816 | 22504909 | Lipopolysaccharide treatment or high-fat diet led to an increase in circulating serum amyloid (SAA) and α1-acid glycoprotein (AGP), whereas adipsin levels were reduced. |
| 4817 | 22504909 | Mouse models that are protected against diet-induced challenges, such as adiponectin-overexpressing animals or mice treated with PPARγ agonists, displayed lower SAA levels and higher adip-sin levels. |
| 4818 | 22528080 | Here, we review the application of photo-induced cross-linking of unmodified proteins (PICUP) to two disease-related amyloidogenic proteins (1) islet amyloid polypeptide (IAPP), whose toxic oligomers are thought to cause the demise of pancreatic β-cells in type-2 diabetes mellitus and (2) α-synuclein, which aggregates into toxic oligomers and precipitates in Lewy bodies in Parkinson's disease. |
| 4819 | 22542527 | Nucleobindin 1 caps human islet amyloid polypeptide protofibrils to prevent amyloid fibril formation. |
| 4820 | 22542527 | Many human diseases are associated with amyloid fibril deposition, including type 2 diabetes mellitus where human islet amyloid polypeptide (hIAPP) forms fibrils in the pancreas. |
| 4821 | 22542527 | This mode of action appears to be different from other protein-based inhibitors, suggesting that NUCB1 may offer a new approach to inhibiting amyloid formation and disaggregating amyloid fibrils. |
| 4822 | 22542527 | Nucleobindin 1 caps human islet amyloid polypeptide protofibrils to prevent amyloid fibril formation. |
| 4823 | 22542527 | Many human diseases are associated with amyloid fibril deposition, including type 2 diabetes mellitus where human islet amyloid polypeptide (hIAPP) forms fibrils in the pancreas. |
| 4824 | 22542527 | This mode of action appears to be different from other protein-based inhibitors, suggesting that NUCB1 may offer a new approach to inhibiting amyloid formation and disaggregating amyloid fibrils. |
| 4825 | 22542527 | Nucleobindin 1 caps human islet amyloid polypeptide protofibrils to prevent amyloid fibril formation. |
| 4826 | 22542527 | Many human diseases are associated with amyloid fibril deposition, including type 2 diabetes mellitus where human islet amyloid polypeptide (hIAPP) forms fibrils in the pancreas. |
| 4827 | 22542527 | This mode of action appears to be different from other protein-based inhibitors, suggesting that NUCB1 may offer a new approach to inhibiting amyloid formation and disaggregating amyloid fibrils. |
| 4828 | 22579683 | Curcumin modulates the self-assembly of the islet amyloid polypeptide by disassembling α-helix. |
| 4829 | 22579683 | Using solution state (1)H NMR, we demonstrate that curcumin, a planar biphenolic compound found in the Indian spice turmeric, delays the self-assembly of islet amyloid polypeptide to NMR-invisible assemblies. |
| 4830 | 22579683 | Curcumin modulates the self-assembly of the islet amyloid polypeptide by disassembling α-helix. |
| 4831 | 22579683 | Using solution state (1)H NMR, we demonstrate that curcumin, a planar biphenolic compound found in the Indian spice turmeric, delays the self-assembly of islet amyloid polypeptide to NMR-invisible assemblies. |
| 4832 | 22590535 | The VEALYL short peptide from insulin has been confirmed to aggregate amyloid-like fibrils. |
| 4833 | 22654727 | The most important common mechanism between insulin-resistant (type II) diabetes and AD could be impaired insulin signaling; a form of toxic amyloid can damage neuronal insulin receptors and affect insulin signaling and cell survival. |
| 4834 | 22654727 | In addition, a major role for insulin degrading enzyme in the degradation of Aβ peptide has been identified. |
| 4835 | 22693597 | Lipid interaction and membrane perturbation of human islet amyloid polypeptide monomer and dimer by molecular dynamics simulations. |
| 4836 | 22693597 | The aggregation of human islet amyloid polypeptide (hIAPP or amylin) is associated with the pathogenesis of type 2 diabetes mellitus. |
| 4837 | 22693597 | Lipid interaction and membrane perturbation of human islet amyloid polypeptide monomer and dimer by molecular dynamics simulations. |
| 4838 | 22693597 | The aggregation of human islet amyloid polypeptide (hIAPP or amylin) is associated with the pathogenesis of type 2 diabetes mellitus. |
| 4839 | 22732191 | Saccharomyces cerevisiae Hsp104 and Escherichia coli ClpB are Hsp100 family AAA+ chaperones that provide stress tolerance by cooperating with Hsp70 and Hsp40 to solubilize aggregated protein. |
| 4840 | 22732191 | Hsp104 also remodels amyloid in vitro and promotes propagation of amyloid prions in yeast, but ClpB does neither, leading to a view that Hsp104 evolved these activities. |
| 4841 | 22732191 | We express prokaryotic chaperones in yeast to address these issues and find ClpB supports both prion propagation and thermotolerance in yeast if it is modified to interact with yeast Hsp70 or if E. coli Hsp70 and its cognate nucleotide exchange factor (NEF) are present. |
| 4842 | 22732191 | Our findings show prion propagation and thermotolerance in yeast minimally require cooperation of species-specific Hsp100, Hsp70, and NEF with yeast Hsp40. |
| 4843 | 22781911 | The occurrence of islet amyloid polypeptide amyloidosis in Japanese subjects. |
| 4844 | 22787008 | Human islet amyloid polypeptide at the air-aqueous interface: a Langmuir monolayer approach. |
| 4845 | 22787008 | Human islet amyloid polypeptide (hIAPP) is the source of the major component of the amyloid deposits found in the islets of Langerhans of around 95 per cent type 2 diabetic patients. |
| 4846 | 22787008 | Human islet amyloid polypeptide at the air-aqueous interface: a Langmuir monolayer approach. |
| 4847 | 22787008 | Human islet amyloid polypeptide (hIAPP) is the source of the major component of the amyloid deposits found in the islets of Langerhans of around 95 per cent type 2 diabetic patients. |
| 4848 | 22819352 | Levels of amyloid precursor protein, beta-amyloid((1-42)), as well as tau and phospho-tau 181 were significantly enhanced in the cortex of cholesterol-fed rats. |
| 4849 | 22829447 | Altered APP processing in insulin-resistant conditions is mediated by autophagosome accumulation via the inhibition of mammalian target of rapamycin pathway. |
| 4850 | 22829447 | Insulin resistance, one of the major components of type 2 diabetes mellitus (T2DM), is a known risk factor for Alzheimer's disease (AD), which is characterized by an abnormal accumulation of intra- and extracellular amyloid β peptide (Aβ). |
| 4851 | 22829447 | In this study, we examined the effect of high-fat diet-induced insulin resistance on amyloid precursor protein (APP) processing in mouse brains. |
| 4852 | 22829447 | Furthermore, in vitro experiments in insulin-resistant SH-SY5Y cells and primary cortical neurons confirmed the alteration of APP processing by insulin resistance-induced autophagosome accumulation. |
| 4853 | 22829447 | Defects in insulin signal transduction affect autophagic flux by inhibiting the mammalian target of rapamycin pathway, resulting in altered APP processing in these cell culture systems. |
| 4854 | 22829447 | Altered APP processing in insulin-resistant conditions is mediated by autophagosome accumulation via the inhibition of mammalian target of rapamycin pathway. |
| 4855 | 22829447 | Insulin resistance, one of the major components of type 2 diabetes mellitus (T2DM), is a known risk factor for Alzheimer's disease (AD), which is characterized by an abnormal accumulation of intra- and extracellular amyloid β peptide (Aβ). |
| 4856 | 22829447 | In this study, we examined the effect of high-fat diet-induced insulin resistance on amyloid precursor protein (APP) processing in mouse brains. |
| 4857 | 22829447 | Furthermore, in vitro experiments in insulin-resistant SH-SY5Y cells and primary cortical neurons confirmed the alteration of APP processing by insulin resistance-induced autophagosome accumulation. |
| 4858 | 22829447 | Defects in insulin signal transduction affect autophagic flux by inhibiting the mammalian target of rapamycin pathway, resulting in altered APP processing in these cell culture systems. |
| 4859 | 22832314 | Soluble oligomers of human islet amyloid polypeptide (h-IAPP) are believed to be the pathogenic species for type 2 diabetes mellitus. |
| 4860 | 22847497 | Islet amyloid polypeptide in pancreatic islets from type 2 diabetic subjects. |
| 4861 | 22902430 | We tested the effects of two types of three-dimensional scaffolds, collagen matrix (CM) and fibroblast-populated collagen matrix (FPCM), on amyloid formation, viability, and function of isolated islets. |
| 4862 | 22902430 | IL-1β and Fas levels were also reduced in scaffold-embedded islets. |
| 4863 | 22902430 | Moreover, culture in CM and FPCM (but not 2D) preserved insulin, GLUT-2, and PDX-1 mRNA expression. |
| 4864 | 22902430 | FPCM-embedded islets had significantly higher insulin response and lower amyloid formation than CM-embedded islets. |
| 4865 | 22902430 | We tested the effects of two types of three-dimensional scaffolds, collagen matrix (CM) and fibroblast-populated collagen matrix (FPCM), on amyloid formation, viability, and function of isolated islets. |
| 4866 | 22902430 | IL-1β and Fas levels were also reduced in scaffold-embedded islets. |
| 4867 | 22902430 | Moreover, culture in CM and FPCM (but not 2D) preserved insulin, GLUT-2, and PDX-1 mRNA expression. |
| 4868 | 22902430 | FPCM-embedded islets had significantly higher insulin response and lower amyloid formation than CM-embedded islets. |
| 4869 | 22924529 | A few cases of localized insulin-derived amyloid deposits at injection sites have been reported previously, but none had significant epidermal changes. |
| 4870 | 22924529 | The presence of a tumour-like lesion at the injection site should be carefully examined, as injection of insulin into amyloid deposits can result in insulin resistance. |
| 4871 | 22924529 | A few cases of localized insulin-derived amyloid deposits at injection sites have been reported previously, but none had significant epidermal changes. |
| 4872 | 22924529 | The presence of a tumour-like lesion at the injection site should be carefully examined, as injection of insulin into amyloid deposits can result in insulin resistance. |
| 4873 | 22936797 | Overall sulfation of heparan sulfate from pancreatic islet β-TC3 cells increases maximal fibril formation but does not determine binding to the amyloidogenic peptide islet amyloid polypeptide. |
| 4874 | 22936797 | Islet amyloid, a pathologic feature of type 2 diabetes, contains the islet β-cell peptide islet amyloid polypeptide (IAPP) as its unique amyloidogenic component. |
| 4875 | 22936797 | Overall sulfation of heparan sulfate from pancreatic islet β-TC3 cells increases maximal fibril formation but does not determine binding to the amyloidogenic peptide islet amyloid polypeptide. |
| 4876 | 22936797 | Islet amyloid, a pathologic feature of type 2 diabetes, contains the islet β-cell peptide islet amyloid polypeptide (IAPP) as its unique amyloidogenic component. |
| 4877 | 22961553 | In a well-established model of hypercholesterolaemia, the apolipoprotein E knockout mouse, we report increased brain levels of immunoglobulin G and upregulation of activating Fc receptors, predominantly of type IV, in neurons susceptible to amyloid β accumulation. |
| 4878 | 22961553 | These cognition-protective effects were associated with a reduction in synapse loss, tau hyperphosphorylation and intracellular amyloid β accumulation both in cortical and hippocampal pyramidal neurons. |
| 4879 | 22961553 | In vitro, activating Fc receptor engagement caused synapse loss, tau hyperphosphorylation and amyloid β deposition in primary neurons by a mechanism involving mitogen-activated protein kinases and β-site amyloid precursor protein cleaving enzyme 1. |
| 4880 | 22961553 | In a well-established model of hypercholesterolaemia, the apolipoprotein E knockout mouse, we report increased brain levels of immunoglobulin G and upregulation of activating Fc receptors, predominantly of type IV, in neurons susceptible to amyloid β accumulation. |
| 4881 | 22961553 | These cognition-protective effects were associated with a reduction in synapse loss, tau hyperphosphorylation and intracellular amyloid β accumulation both in cortical and hippocampal pyramidal neurons. |
| 4882 | 22961553 | In vitro, activating Fc receptor engagement caused synapse loss, tau hyperphosphorylation and amyloid β deposition in primary neurons by a mechanism involving mitogen-activated protein kinases and β-site amyloid precursor protein cleaving enzyme 1. |
| 4883 | 22961553 | In a well-established model of hypercholesterolaemia, the apolipoprotein E knockout mouse, we report increased brain levels of immunoglobulin G and upregulation of activating Fc receptors, predominantly of type IV, in neurons susceptible to amyloid β accumulation. |
| 4884 | 22961553 | These cognition-protective effects were associated with a reduction in synapse loss, tau hyperphosphorylation and intracellular amyloid β accumulation both in cortical and hippocampal pyramidal neurons. |
| 4885 | 22961553 | In vitro, activating Fc receptor engagement caused synapse loss, tau hyperphosphorylation and amyloid β deposition in primary neurons by a mechanism involving mitogen-activated protein kinases and β-site amyloid precursor protein cleaving enzyme 1. |
| 4886 | 22988095 | O-GlcNAc cycling dramatically modulated the severity of the phenotype in transgenic models of tauopathy, amyloid β-peptide, and polyglutamine expansion. |
| 4887 | 22988095 | Intriguingly, loss of function of O-GlcNAc transferase alleviated, whereas loss of O-GlcNAcase enhanced, the phenotype of multiple neurodegenerative disease models. |
| 4888 | 23011726 | Liraglutide, a novel glucagon-like peptide 1 (GLP-1) analogue that facilitates insulin signalling, is currently approved for use in type 2 diabetes mellitus. |
| 4889 | 23011726 | In the present study, we show that distinctive alterations in the localisation and distribution of the IR and increased levels of insulin receptor substrate (IRS)-1 phosphorylated at serine 616 (IRS-1 pS(616)), a key marker of insulin resistance, are associated with amyloid-β plaque pathology in the frontal cortex of a mouse model of AD, APPSWE/PS1dE9. |
| 4890 | 23011726 | We show that liraglutide treatment for 8 weeks at 25 nmol/kg body weight i.p. once daily in 7-month-old mice significantly decreases IR aberrations in conjunction with a concomitant decrease in amyloid plaque load and levels of IRS-1 pS(616). |
| 4891 | 23011726 | The amelioration of IR aberrations and attenuation of IRS-1 pS(616) upregulation, plaque and glial activation in APPSWE/PS1dE9 mice treated with liraglutide support the investigation of the therapeutic potential of liraglutide and long-lasting GLP-1 agonists in patients with AD. |
| 4892 | 23040364 | It was subsequently observed that several of these conditions were caused by mutations in proteins involved in the innate immune response, including, among others, components of the NLRP3 inflammasome, cytokine receptors (tumour necrosis factor receptor 1 (TNFR1)) and receptor antagonists (interleukin 1 receptor antagonist (IL-1RA)). |
| 4893 | 23040364 | NLRP3 inflammasome activation is induced by islet amyloid polypeptides (IAPPs) in T2D and this condition may, in future, be more commonly treated with targeted anti-cytokine therapies. |
| 4894 | 23040364 | Caspase 1 activation and release of IL-1β/IL-1 family members is central to the pathogenesis of many autoinflammatory syndromes, as evidenced by the effectiveness of anti-IL-1 biologics in treating these disorders. |
| 4895 | 23086037 | In this study, we investigated patterns of NLRP3 inflammasome activation in monocyte-derived macrophages (MDMs) from drug-naïve patients with newly diagnosed type 2 diabetes. |
| 4896 | 23086037 | Type 2 diabetic subjects had significantly increased mRNA and protein expression of NLRP3, apoptosis-associated speck-like protein containing a CARD (ASC), and proinflammatory cytokines in MDMs cultured with autologous sera compared with healthy controls. |
| 4897 | 23086037 | Upregulated interleukin (IL)-1β maturation, IL-18 secretion, and caspase-1 cleavage were observed in MDMs from type 2 diabetic patients after stimulation with various danger molecules (ATP, high-mobility group protein B1, free fatty acids, islet amyloid polypeptide, and monosodium uric acid crystals). |
| 4898 | 23086037 | Mitochondrial reactive oxygen species and NLRP3 were required for IL-1β synthesis in MDMs. |
| 4899 | 23086037 | Finally, 2 months of therapy with the antidiabetic drug metformin significantly inhibited the maturation of IL-1β in MDMs from patients with type 2 diabetes through AMP-activated protein kinase (AMPK) activation. |
| 4900 | 23089868 | We describe the structures and inhibitory properties of ABSMs containing amyloidogenic peptides from the amyloid-β peptide associated with Alzheimer's disease, β(2)-microglobulin associated with dialysis-related amyloidosis, α-synuclein associated with Parkinson's disease, islet amyloid polypeptide associated with type II diabetes, human and yeast prion proteins, and Tau, which forms neurofibrillary tangles. |
| 4901 | 23103794 | The incretin analogue D-Ala2GIP reduces plaque load, astrogliosis and oxidative stress in an APP/PS1 mouse model of Alzheimer's disease. |
| 4902 | 23103794 | Glucose-dependent insulinotropic polypeptide (GIP), an incretin hormone, normalises insulin signalling and also acts as a neuroprotective growth factor. |
| 4903 | 23103794 | D-Ala(2)GIP was injected for 35 days at 25 nmol/kg i.p. once daily in APP/PS1 male mice and wild-type (WT) littermates aged 6, 12 and 19 months. |
| 4904 | 23103794 | D-Ala(2)GIP reduced the amyloid plaque load in 12- and 19-month-old mice, and the inflammation response as shown in the reduction of activated astrocytes in 12- and 19-month old APP/PS1 mice. |
| 4905 | 23103794 | Chronic oxidative stress in the brain was reduced in 12- and 19-month-old mice as shown in the reduction of 8-oxoguanine levels in the cortex of D-Ala(2)GIP-injected APP/PS1 mice. |
| 4906 | 23161913 | Grafted AMyloid-Motif AntiBODIES (gammabodies) presenting hydrophobic peptides from Aβ (Alzheimer's disease), α-Synuclein (Parkinson's disease), and islet amyloid polypeptide (type 2 diabetes) inhibit fibril assembly of each corresponding polypeptide at low substoichiometric concentrations (1:10 gammabody:monomer molar ratio). |
| 4907 | 23180621 | Salvianolic acid B inhibits the amyloid formation of human islet amyloid polypeptide and protects pancreatic beta-cells against cytotoxicity. |
| 4908 | 23180621 | The misfolding of human islet amyloid polypeptide (hIAPP) is regarded as one of the causative factors of type 2 diabetes mellitus (T2DM). |
| 4909 | 23180621 | Salvianolic acid B inhibits the amyloid formation of human islet amyloid polypeptide and protects pancreatic beta-cells against cytotoxicity. |
| 4910 | 23180621 | The misfolding of human islet amyloid polypeptide (hIAPP) is regarded as one of the causative factors of type 2 diabetes mellitus (T2DM). |
| 4911 | 23197723 | PPARγ/RXRα-induced and CD36-mediated microglial amyloid-β phagocytosis results in cognitive improvement in amyloid precursor protein/presenilin 1 mice. |
| 4912 | 23197723 | Evaluation of DSP-8658 in the amyloid precursor protein/presenilin 1 mouse model confirmed an increased microglial Aβ phagocytosis in vivo, which subsequently resulted in a reduction of cortical and hippocampal Aβ levels. |
| 4913 | 23197723 | PPARγ/RXRα-induced and CD36-mediated microglial amyloid-β phagocytosis results in cognitive improvement in amyloid precursor protein/presenilin 1 mice. |
| 4914 | 23197723 | Evaluation of DSP-8658 in the amyloid precursor protein/presenilin 1 mouse model confirmed an increased microglial Aβ phagocytosis in vivo, which subsequently resulted in a reduction of cortical and hippocampal Aβ levels. |
| 4915 | 23225004 | Islet amyloid polypeptide: aggregation and fibrillogenesis in vitro and its inhibition. |
| 4916 | 23225004 | The development of type 2 diabetes mellitus is associated with the dysfunction of b-cells which is correlated to the formation of deposits consisting of the islet amyloid polypeptide (IAPP). |
| 4917 | 23225004 | Islet amyloid polypeptide: aggregation and fibrillogenesis in vitro and its inhibition. |
| 4918 | 23225004 | The development of type 2 diabetes mellitus is associated with the dysfunction of b-cells which is correlated to the formation of deposits consisting of the islet amyloid polypeptide (IAPP). |
| 4919 | 23229548 | Matrix metalloproteinase-9 reduces islet amyloid formation by degrading islet amyloid polypeptide. |
| 4920 | 23229548 | Deposition of islet amyloid polypeptide (IAPP) as amyloid is a pathological hallmark of the islet in type 2 diabetes, which is toxic to β-cells. |
| 4921 | 23229548 | We previously showed that the enzyme neprilysin reduces islet amyloid deposition and thereby reduces β-cell apoptosis, by inhibiting fibril formation. |
| 4922 | 23229548 | Two other enzymes, matrix metalloproteinase (MMP)-2 and MMP-9, are extracellular gelatinases capable of degrading another amyloidogenic peptide, Aβ, the constituent of amyloid deposits in Alzheimer disease. |
| 4923 | 23229548 | We therefore investigated whether MMP-2 and MMP-9 play a role in reducing islet amyloid deposition. |
| 4924 | 23229548 | MMP-2 and MMP-9 mRNA were present in mouse islets but only MMP-9 activity was detectable. |
| 4925 | 23229548 | In an islet culture model where human IAPP (hIAPP) transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increased amyloid formation and the resultant β-cell apoptosis. |
| 4926 | 23229548 | In contrast, a specific MMP-2 inhibitor had no effect on either amyloid deposition or β-cell apoptosis. |
| 4927 | 23229548 | Thus, MMP-9 constitutes an endogenous islet protease that limits islet amyloid deposition and its toxic effects via degradation of hIAPP. |
| 4928 | 23229548 | Because islet MMP-9 mRNA levels are decreased in type 2 diabetic subjects, islet MMP-9 activity may also be decreased in human type 2 diabetes, thereby contributing to increased islet amyloid deposition and β-cell loss. |
| 4929 | 23229548 | Approaches to increase islet MMP-9 activity could reduce or prevent amyloid deposition and its toxic effects in type 2 diabetes. |
| 4930 | 23229548 | Matrix metalloproteinase-9 reduces islet amyloid formation by degrading islet amyloid polypeptide. |
| 4931 | 23229548 | Deposition of islet amyloid polypeptide (IAPP) as amyloid is a pathological hallmark of the islet in type 2 diabetes, which is toxic to β-cells. |
| 4932 | 23229548 | We previously showed that the enzyme neprilysin reduces islet amyloid deposition and thereby reduces β-cell apoptosis, by inhibiting fibril formation. |
| 4933 | 23229548 | Two other enzymes, matrix metalloproteinase (MMP)-2 and MMP-9, are extracellular gelatinases capable of degrading another amyloidogenic peptide, Aβ, the constituent of amyloid deposits in Alzheimer disease. |
| 4934 | 23229548 | We therefore investigated whether MMP-2 and MMP-9 play a role in reducing islet amyloid deposition. |
| 4935 | 23229548 | MMP-2 and MMP-9 mRNA were present in mouse islets but only MMP-9 activity was detectable. |
| 4936 | 23229548 | In an islet culture model where human IAPP (hIAPP) transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increased amyloid formation and the resultant β-cell apoptosis. |
| 4937 | 23229548 | In contrast, a specific MMP-2 inhibitor had no effect on either amyloid deposition or β-cell apoptosis. |
| 4938 | 23229548 | Thus, MMP-9 constitutes an endogenous islet protease that limits islet amyloid deposition and its toxic effects via degradation of hIAPP. |
| 4939 | 23229548 | Because islet MMP-9 mRNA levels are decreased in type 2 diabetic subjects, islet MMP-9 activity may also be decreased in human type 2 diabetes, thereby contributing to increased islet amyloid deposition and β-cell loss. |
| 4940 | 23229548 | Approaches to increase islet MMP-9 activity could reduce or prevent amyloid deposition and its toxic effects in type 2 diabetes. |
| 4941 | 23229548 | Matrix metalloproteinase-9 reduces islet amyloid formation by degrading islet amyloid polypeptide. |
| 4942 | 23229548 | Deposition of islet amyloid polypeptide (IAPP) as amyloid is a pathological hallmark of the islet in type 2 diabetes, which is toxic to β-cells. |
| 4943 | 23229548 | We previously showed that the enzyme neprilysin reduces islet amyloid deposition and thereby reduces β-cell apoptosis, by inhibiting fibril formation. |
| 4944 | 23229548 | Two other enzymes, matrix metalloproteinase (MMP)-2 and MMP-9, are extracellular gelatinases capable of degrading another amyloidogenic peptide, Aβ, the constituent of amyloid deposits in Alzheimer disease. |
| 4945 | 23229548 | We therefore investigated whether MMP-2 and MMP-9 play a role in reducing islet amyloid deposition. |
| 4946 | 23229548 | MMP-2 and MMP-9 mRNA were present in mouse islets but only MMP-9 activity was detectable. |
| 4947 | 23229548 | In an islet culture model where human IAPP (hIAPP) transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increased amyloid formation and the resultant β-cell apoptosis. |
| 4948 | 23229548 | In contrast, a specific MMP-2 inhibitor had no effect on either amyloid deposition or β-cell apoptosis. |
| 4949 | 23229548 | Thus, MMP-9 constitutes an endogenous islet protease that limits islet amyloid deposition and its toxic effects via degradation of hIAPP. |
| 4950 | 23229548 | Because islet MMP-9 mRNA levels are decreased in type 2 diabetic subjects, islet MMP-9 activity may also be decreased in human type 2 diabetes, thereby contributing to increased islet amyloid deposition and β-cell loss. |
| 4951 | 23229548 | Approaches to increase islet MMP-9 activity could reduce or prevent amyloid deposition and its toxic effects in type 2 diabetes. |
| 4952 | 23229548 | Matrix metalloproteinase-9 reduces islet amyloid formation by degrading islet amyloid polypeptide. |
| 4953 | 23229548 | Deposition of islet amyloid polypeptide (IAPP) as amyloid is a pathological hallmark of the islet in type 2 diabetes, which is toxic to β-cells. |
| 4954 | 23229548 | We previously showed that the enzyme neprilysin reduces islet amyloid deposition and thereby reduces β-cell apoptosis, by inhibiting fibril formation. |
| 4955 | 23229548 | Two other enzymes, matrix metalloproteinase (MMP)-2 and MMP-9, are extracellular gelatinases capable of degrading another amyloidogenic peptide, Aβ, the constituent of amyloid deposits in Alzheimer disease. |
| 4956 | 23229548 | We therefore investigated whether MMP-2 and MMP-9 play a role in reducing islet amyloid deposition. |
| 4957 | 23229548 | MMP-2 and MMP-9 mRNA were present in mouse islets but only MMP-9 activity was detectable. |
| 4958 | 23229548 | In an islet culture model where human IAPP (hIAPP) transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increased amyloid formation and the resultant β-cell apoptosis. |
| 4959 | 23229548 | In contrast, a specific MMP-2 inhibitor had no effect on either amyloid deposition or β-cell apoptosis. |
| 4960 | 23229548 | Thus, MMP-9 constitutes an endogenous islet protease that limits islet amyloid deposition and its toxic effects via degradation of hIAPP. |
| 4961 | 23229548 | Because islet MMP-9 mRNA levels are decreased in type 2 diabetic subjects, islet MMP-9 activity may also be decreased in human type 2 diabetes, thereby contributing to increased islet amyloid deposition and β-cell loss. |
| 4962 | 23229548 | Approaches to increase islet MMP-9 activity could reduce or prevent amyloid deposition and its toxic effects in type 2 diabetes. |
| 4963 | 23229548 | Matrix metalloproteinase-9 reduces islet amyloid formation by degrading islet amyloid polypeptide. |
| 4964 | 23229548 | Deposition of islet amyloid polypeptide (IAPP) as amyloid is a pathological hallmark of the islet in type 2 diabetes, which is toxic to β-cells. |
| 4965 | 23229548 | We previously showed that the enzyme neprilysin reduces islet amyloid deposition and thereby reduces β-cell apoptosis, by inhibiting fibril formation. |
| 4966 | 23229548 | Two other enzymes, matrix metalloproteinase (MMP)-2 and MMP-9, are extracellular gelatinases capable of degrading another amyloidogenic peptide, Aβ, the constituent of amyloid deposits in Alzheimer disease. |
| 4967 | 23229548 | We therefore investigated whether MMP-2 and MMP-9 play a role in reducing islet amyloid deposition. |
| 4968 | 23229548 | MMP-2 and MMP-9 mRNA were present in mouse islets but only MMP-9 activity was detectable. |
| 4969 | 23229548 | In an islet culture model where human IAPP (hIAPP) transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increased amyloid formation and the resultant β-cell apoptosis. |
| 4970 | 23229548 | In contrast, a specific MMP-2 inhibitor had no effect on either amyloid deposition or β-cell apoptosis. |
| 4971 | 23229548 | Thus, MMP-9 constitutes an endogenous islet protease that limits islet amyloid deposition and its toxic effects via degradation of hIAPP. |
| 4972 | 23229548 | Because islet MMP-9 mRNA levels are decreased in type 2 diabetic subjects, islet MMP-9 activity may also be decreased in human type 2 diabetes, thereby contributing to increased islet amyloid deposition and β-cell loss. |
| 4973 | 23229548 | Approaches to increase islet MMP-9 activity could reduce or prevent amyloid deposition and its toxic effects in type 2 diabetes. |
| 4974 | 23229548 | Matrix metalloproteinase-9 reduces islet amyloid formation by degrading islet amyloid polypeptide. |
| 4975 | 23229548 | Deposition of islet amyloid polypeptide (IAPP) as amyloid is a pathological hallmark of the islet in type 2 diabetes, which is toxic to β-cells. |
| 4976 | 23229548 | We previously showed that the enzyme neprilysin reduces islet amyloid deposition and thereby reduces β-cell apoptosis, by inhibiting fibril formation. |
| 4977 | 23229548 | Two other enzymes, matrix metalloproteinase (MMP)-2 and MMP-9, are extracellular gelatinases capable of degrading another amyloidogenic peptide, Aβ, the constituent of amyloid deposits in Alzheimer disease. |
| 4978 | 23229548 | We therefore investigated whether MMP-2 and MMP-9 play a role in reducing islet amyloid deposition. |
| 4979 | 23229548 | MMP-2 and MMP-9 mRNA were present in mouse islets but only MMP-9 activity was detectable. |
| 4980 | 23229548 | In an islet culture model where human IAPP (hIAPP) transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increased amyloid formation and the resultant β-cell apoptosis. |
| 4981 | 23229548 | In contrast, a specific MMP-2 inhibitor had no effect on either amyloid deposition or β-cell apoptosis. |
| 4982 | 23229548 | Thus, MMP-9 constitutes an endogenous islet protease that limits islet amyloid deposition and its toxic effects via degradation of hIAPP. |
| 4983 | 23229548 | Because islet MMP-9 mRNA levels are decreased in type 2 diabetic subjects, islet MMP-9 activity may also be decreased in human type 2 diabetes, thereby contributing to increased islet amyloid deposition and β-cell loss. |
| 4984 | 23229548 | Approaches to increase islet MMP-9 activity could reduce or prevent amyloid deposition and its toxic effects in type 2 diabetes. |
| 4985 | 23229548 | Matrix metalloproteinase-9 reduces islet amyloid formation by degrading islet amyloid polypeptide. |
| 4986 | 23229548 | Deposition of islet amyloid polypeptide (IAPP) as amyloid is a pathological hallmark of the islet in type 2 diabetes, which is toxic to β-cells. |
| 4987 | 23229548 | We previously showed that the enzyme neprilysin reduces islet amyloid deposition and thereby reduces β-cell apoptosis, by inhibiting fibril formation. |
| 4988 | 23229548 | Two other enzymes, matrix metalloproteinase (MMP)-2 and MMP-9, are extracellular gelatinases capable of degrading another amyloidogenic peptide, Aβ, the constituent of amyloid deposits in Alzheimer disease. |
| 4989 | 23229548 | We therefore investigated whether MMP-2 and MMP-9 play a role in reducing islet amyloid deposition. |
| 4990 | 23229548 | MMP-2 and MMP-9 mRNA were present in mouse islets but only MMP-9 activity was detectable. |
| 4991 | 23229548 | In an islet culture model where human IAPP (hIAPP) transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increased amyloid formation and the resultant β-cell apoptosis. |
| 4992 | 23229548 | In contrast, a specific MMP-2 inhibitor had no effect on either amyloid deposition or β-cell apoptosis. |
| 4993 | 23229548 | Thus, MMP-9 constitutes an endogenous islet protease that limits islet amyloid deposition and its toxic effects via degradation of hIAPP. |
| 4994 | 23229548 | Because islet MMP-9 mRNA levels are decreased in type 2 diabetic subjects, islet MMP-9 activity may also be decreased in human type 2 diabetes, thereby contributing to increased islet amyloid deposition and β-cell loss. |
| 4995 | 23229548 | Approaches to increase islet MMP-9 activity could reduce or prevent amyloid deposition and its toxic effects in type 2 diabetes. |
| 4996 | 23229548 | Matrix metalloproteinase-9 reduces islet amyloid formation by degrading islet amyloid polypeptide. |
| 4997 | 23229548 | Deposition of islet amyloid polypeptide (IAPP) as amyloid is a pathological hallmark of the islet in type 2 diabetes, which is toxic to β-cells. |
| 4998 | 23229548 | We previously showed that the enzyme neprilysin reduces islet amyloid deposition and thereby reduces β-cell apoptosis, by inhibiting fibril formation. |
| 4999 | 23229548 | Two other enzymes, matrix metalloproteinase (MMP)-2 and MMP-9, are extracellular gelatinases capable of degrading another amyloidogenic peptide, Aβ, the constituent of amyloid deposits in Alzheimer disease. |
| 5000 | 23229548 | We therefore investigated whether MMP-2 and MMP-9 play a role in reducing islet amyloid deposition. |
| 5001 | 23229548 | MMP-2 and MMP-9 mRNA were present in mouse islets but only MMP-9 activity was detectable. |
| 5002 | 23229548 | In an islet culture model where human IAPP (hIAPP) transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increased amyloid formation and the resultant β-cell apoptosis. |
| 5003 | 23229548 | In contrast, a specific MMP-2 inhibitor had no effect on either amyloid deposition or β-cell apoptosis. |
| 5004 | 23229548 | Thus, MMP-9 constitutes an endogenous islet protease that limits islet amyloid deposition and its toxic effects via degradation of hIAPP. |
| 5005 | 23229548 | Because islet MMP-9 mRNA levels are decreased in type 2 diabetic subjects, islet MMP-9 activity may also be decreased in human type 2 diabetes, thereby contributing to increased islet amyloid deposition and β-cell loss. |
| 5006 | 23229548 | Approaches to increase islet MMP-9 activity could reduce or prevent amyloid deposition and its toxic effects in type 2 diabetes. |
| 5007 | 23229548 | Matrix metalloproteinase-9 reduces islet amyloid formation by degrading islet amyloid polypeptide. |
| 5008 | 23229548 | Deposition of islet amyloid polypeptide (IAPP) as amyloid is a pathological hallmark of the islet in type 2 diabetes, which is toxic to β-cells. |
| 5009 | 23229548 | We previously showed that the enzyme neprilysin reduces islet amyloid deposition and thereby reduces β-cell apoptosis, by inhibiting fibril formation. |
| 5010 | 23229548 | Two other enzymes, matrix metalloproteinase (MMP)-2 and MMP-9, are extracellular gelatinases capable of degrading another amyloidogenic peptide, Aβ, the constituent of amyloid deposits in Alzheimer disease. |
| 5011 | 23229548 | We therefore investigated whether MMP-2 and MMP-9 play a role in reducing islet amyloid deposition. |
| 5012 | 23229548 | MMP-2 and MMP-9 mRNA were present in mouse islets but only MMP-9 activity was detectable. |
| 5013 | 23229548 | In an islet culture model where human IAPP (hIAPP) transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increased amyloid formation and the resultant β-cell apoptosis. |
| 5014 | 23229548 | In contrast, a specific MMP-2 inhibitor had no effect on either amyloid deposition or β-cell apoptosis. |
| 5015 | 23229548 | Thus, MMP-9 constitutes an endogenous islet protease that limits islet amyloid deposition and its toxic effects via degradation of hIAPP. |
| 5016 | 23229548 | Because islet MMP-9 mRNA levels are decreased in type 2 diabetic subjects, islet MMP-9 activity may also be decreased in human type 2 diabetes, thereby contributing to increased islet amyloid deposition and β-cell loss. |
| 5017 | 23229548 | Approaches to increase islet MMP-9 activity could reduce or prevent amyloid deposition and its toxic effects in type 2 diabetes. |
| 5018 | 23229548 | Matrix metalloproteinase-9 reduces islet amyloid formation by degrading islet amyloid polypeptide. |
| 5019 | 23229548 | Deposition of islet amyloid polypeptide (IAPP) as amyloid is a pathological hallmark of the islet in type 2 diabetes, which is toxic to β-cells. |
| 5020 | 23229548 | We previously showed that the enzyme neprilysin reduces islet amyloid deposition and thereby reduces β-cell apoptosis, by inhibiting fibril formation. |
| 5021 | 23229548 | Two other enzymes, matrix metalloproteinase (MMP)-2 and MMP-9, are extracellular gelatinases capable of degrading another amyloidogenic peptide, Aβ, the constituent of amyloid deposits in Alzheimer disease. |
| 5022 | 23229548 | We therefore investigated whether MMP-2 and MMP-9 play a role in reducing islet amyloid deposition. |
| 5023 | 23229548 | MMP-2 and MMP-9 mRNA were present in mouse islets but only MMP-9 activity was detectable. |
| 5024 | 23229548 | In an islet culture model where human IAPP (hIAPP) transgenic mouse islets develop amyloid but nontransgenic islets do not, a broad spectrum MMP inhibitor (GM6001) and an MMP-2/9 inhibitor increased amyloid formation and the resultant β-cell apoptosis. |
| 5025 | 23229548 | In contrast, a specific MMP-2 inhibitor had no effect on either amyloid deposition or β-cell apoptosis. |
| 5026 | 23229548 | Thus, MMP-9 constitutes an endogenous islet protease that limits islet amyloid deposition and its toxic effects via degradation of hIAPP. |
| 5027 | 23229548 | Because islet MMP-9 mRNA levels are decreased in type 2 diabetic subjects, islet MMP-9 activity may also be decreased in human type 2 diabetes, thereby contributing to increased islet amyloid deposition and β-cell loss. |
| 5028 | 23229548 | Approaches to increase islet MMP-9 activity could reduce or prevent amyloid deposition and its toxic effects in type 2 diabetes. |
| 5029 | 23262664 | The glucagon-like peptide-1 receptor agonist exenatide restores impaired pro-islet amyloid polypeptide processing in cultured human islets: implications in type 2 diabetes and islet transplantation. |
| 5030 | 23266002 | Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology. |
| 5031 | 23266002 | Amyloid formation in the pancreas by islet amyloid polypeptide (IAPP) leads to β-cell death and dysfunction, contributing to islet transplant failure and to type-2 diabetes. |
| 5032 | 23266002 | Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology. |
| 5033 | 23266002 | Amyloid formation in the pancreas by islet amyloid polypeptide (IAPP) leads to β-cell death and dysfunction, contributing to islet transplant failure and to type-2 diabetes. |
| 5034 | 23267797 | Rosiglitazone treatment does not decrease amyloid deposition in transplanted islets from transgenic mice expressing human islet amyloid polypeptide. |
| 5035 | 23267797 | We previously showed that amyloid deposition following transplantation of islets from human islet amyloid polypeptide (hIAPP) transgenic mice resulted in ß-cell loss and that rosiglitazone treatment decreased islet amyloid deposition and preserved ß-cell area in the endogenous pancreas of hIAPP transgenic mice. |
| 5036 | 23267797 | Rosiglitazone treatment does not decrease amyloid deposition in transplanted islets from transgenic mice expressing human islet amyloid polypeptide. |
| 5037 | 23267797 | We previously showed that amyloid deposition following transplantation of islets from human islet amyloid polypeptide (hIAPP) transgenic mice resulted in ß-cell loss and that rosiglitazone treatment decreased islet amyloid deposition and preserved ß-cell area in the endogenous pancreas of hIAPP transgenic mice. |
| 5038 | 23300647 | We studied the potential protective effect of adiponectin (an adipokine with insulin-sensitizing, anti-inflammatory and anti-oxidant properties) against Aβ neurotoxicity in human neuroblastoma cells (SH-SY5Y) transfected with the Swedish amyloid precursor protein (Sw-APP) mutant, which overproduced Aβ with abnormal intracellular Aβ accumulation. |
| 5039 | 23300647 | Our results revealed that Sw-APP transfected SH-SY5Y cells expressed both adiponectin receptor 1 and 2, and had increased AMP-activated protein kinase (AMPK) activation and enhanced nuclear factor-kappa B (NF-κB) activation compared to control empty-vector transfected SH-SY5Y cells. |
| 5040 | 23300647 | This neuroprotective action of adiponectin against Aβ neurotoxicity-induced cytotoxicity under oxidative stress involved 1) AMPK activation mediated via the endosomal adaptor protein APPL1 (adaptor protein with phosphotyrosine binding, pleckstrin homology domains and leucine zipper motif) and possibly 2) suppression of NF-κB activation. |
| 5041 | 23335292 | However, the native GLP-1 can be rapidly degraded by the enzyme dipeptidyl peptidase IV (DPP IV); the neuroprotective mechanism of GLP-1 in the central nervous system is still an open question, and whether GLP-1 can prevent amyloid β (Aβ)-induced synaptic dysfunction and calcium disorder is still unclear. |
| 5042 | 23337872 | Amyloid formation by the neuropancreatic hormone, islet amyloid polypeptide (IAPP or amylin), one of the most amyloidogenic sequences known, leads to islet amyloidosis in type 2 diabetes and to islet transplant failure. |
| 5043 | 23349537 | The islet in type 2 diabetes (T2DM) is characterized by a deficit in β-cells, increased β-cell apoptosis, and extracellular amyloid deposits derived from islet amyloid polypeptide (IAPP). |
| 5044 | 23362012 | Diabetes-induced increased levels of amyloid β protein and phosphorylated tau were not significantly affected by the treatments. |
| 5045 | 23372685 | Bisphenol A accelerates toxic amyloid formation of human islet amyloid polypeptide: a possible link between bisphenol A exposure and type 2 diabetes. |
| 5046 | 23372685 | Human islet amyloid polypeptide (hIAPP) is a hormone synthesized and secreted by the pancreatic β-cells. |
| 5047 | 23372685 | Bisphenol A accelerates toxic amyloid formation of human islet amyloid polypeptide: a possible link between bisphenol A exposure and type 2 diabetes. |
| 5048 | 23372685 | Human islet amyloid polypeptide (hIAPP) is a hormone synthesized and secreted by the pancreatic β-cells. |
| 5049 | 23380070 | The major protein component of islet amyloid is the polypeptide hormone known as islet amyloid polypeptide (IAPP, or amylin). |
| 5050 | 23435449 | Conformationally restricted short peptides inhibit human islet amyloid polypeptide (hIAPP) fibrillization. |
| 5051 | 23437776 | Optimization of peptide hydroxamate inhibitors of insulin-degrading enzyme reveals marked substrate-selectivity. |
| 5052 | 23437776 | Insulin-degrading enzyme (IDE) is an atypical zinc-metallopeptidase that degrades insulin and the amyloid ß-protein and is strongly implicated in the pathogenesis of diabetes and Alzheimer's disease. |
| 5053 | 23457571 | Amylin is an endocrine hormone that accumulates in amyloid plaques in patients with advanced type 2 diabetes. |
| 5054 | 23478327 | We describe mechanisms of action for combinations of glucagon-like peptide 1, glucagon, gastric inhibitory polypeptide, gastrin, islet amyloid polypeptide and leptin, which enhance weight loss whilst preserving glucoregulatory efficacy in experimental models of obesity and T2DM. |
| 5055 | 23479452 | Attenuation of the insulin amyloid aggregation in presence of Fe3O4-based magnetic fluids. |
| 5056 | 23479452 | Insulin amyloid aggregates have been reported in a patient with diabetes undergoing treatment by injection of insulin. |
| 5057 | 23479452 | We have investigated the interference of insulin amyloid aggregation with two Fe3O4-based magnetic fluids. |
| 5058 | 23479452 | The magnetic fluids are able to inhibit insulin amyloid fibrillization and promote disassembly of amyloid fibrils. |
| 5059 | 23479452 | Attenuation of the insulin amyloid aggregation in presence of Fe3O4-based magnetic fluids. |
| 5060 | 23479452 | Insulin amyloid aggregates have been reported in a patient with diabetes undergoing treatment by injection of insulin. |
| 5061 | 23479452 | We have investigated the interference of insulin amyloid aggregation with two Fe3O4-based magnetic fluids. |
| 5062 | 23479452 | The magnetic fluids are able to inhibit insulin amyloid fibrillization and promote disassembly of amyloid fibrils. |
| 5063 | 23479452 | Attenuation of the insulin amyloid aggregation in presence of Fe3O4-based magnetic fluids. |
| 5064 | 23479452 | Insulin amyloid aggregates have been reported in a patient with diabetes undergoing treatment by injection of insulin. |
| 5065 | 23479452 | We have investigated the interference of insulin amyloid aggregation with two Fe3O4-based magnetic fluids. |
| 5066 | 23479452 | The magnetic fluids are able to inhibit insulin amyloid fibrillization and promote disassembly of amyloid fibrils. |
| 5067 | 23479452 | Attenuation of the insulin amyloid aggregation in presence of Fe3O4-based magnetic fluids. |
| 5068 | 23479452 | Insulin amyloid aggregates have been reported in a patient with diabetes undergoing treatment by injection of insulin. |
| 5069 | 23479452 | We have investigated the interference of insulin amyloid aggregation with two Fe3O4-based magnetic fluids. |
| 5070 | 23479452 | The magnetic fluids are able to inhibit insulin amyloid fibrillization and promote disassembly of amyloid fibrils. |
| 5071 | 23493863 | Membrane disordering is not sufficient for membrane permeabilization by islet amyloid polypeptide: studies of IAPP(20-29) fragments. |
| 5072 | 23493863 | Human islet amyloid polypeptide protein (human-IAPP) is believed to play a crucial role in this process by forming small aggregates that exhibit toxicity by disrupting the cell membrane. |
| 5073 | 23493863 | Membrane disordering is not sufficient for membrane permeabilization by islet amyloid polypeptide: studies of IAPP(20-29) fragments. |
| 5074 | 23493863 | Human islet amyloid polypeptide protein (human-IAPP) is believed to play a crucial role in this process by forming small aggregates that exhibit toxicity by disrupting the cell membrane. |
| 5075 | 23493869 | Owing to the presence of various types of osmolytes in the cellular environment, this study focuses on the impact of stabilizing (TMAO and betaine) as well as destabilizing (urea) cosolvents on the aggregation and fibrillation reaction of the highly amyloidogenic islet amyloid polypeptide (IAPP). |
| 5076 | 23499750 | The misfolding of human islet amyloid polypeptide (hIAPP) is regarded as a causative factor of type 2 diabetes mellitus (T2DM). |
| 5077 | 23505632 | Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide. |
| 5078 | 23505632 | The aggregation of human islet amyloid polypeptide (hIAPP) has been linked to beta-cell death in type II diabetes. |
| 5079 | 23505632 | Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide. |
| 5080 | 23505632 | The aggregation of human islet amyloid polypeptide (hIAPP) has been linked to beta-cell death in type II diabetes. |
| 5081 | 23519103 | Human islet amyloid polypeptide (hIAPP) is the major component of amyloid deposits found in the pancreas of type II diabetic patients. |
| 5082 | 23519103 | Remarkably, different simulations lead to the same binding orientation stabilized by electrostatic and H-bonding interactions, with residues R11, F15 and S19 oriented towards membrane and hydrophobic residues L12, A13, L16 and V17 exposed to solvent. |
| 5083 | 23526456 | New insights into the roles of sulfated glycosaminoglycans in islet amyloid polypeptide amyloidogenesis and cytotoxicity. |
| 5084 | 23526456 | Particularly, GAGs were shown to enhance fibrillogenesis of the islet amyloid polypeptide (IAPP), a peptide hormone whose aggregation is associated with Type-II diabetes pathogenesis. |
| 5085 | 23526456 | New insights into the roles of sulfated glycosaminoglycans in islet amyloid polypeptide amyloidogenesis and cytotoxicity. |
| 5086 | 23526456 | Particularly, GAGs were shown to enhance fibrillogenesis of the islet amyloid polypeptide (IAPP), a peptide hormone whose aggregation is associated with Type-II diabetes pathogenesis. |
| 5087 | 23528352 | Inhibition of human islet amyloid polypeptide or amylin aggregation by two manganese-salen derivatives. |
| 5088 | 23528352 | Aggregation of human islet amyloid polypeptide (IAPP) into pancreatic fibrillar deposits has been postulated to be one of the main contributors to impaired insulin secretion and pancreatic β-cell death in approximately 90% of type 2 diabetic patients. |
| 5089 | 23528352 | Inhibition of human islet amyloid polypeptide or amylin aggregation by two manganese-salen derivatives. |
| 5090 | 23528352 | Aggregation of human islet amyloid polypeptide (IAPP) into pancreatic fibrillar deposits has been postulated to be one of the main contributors to impaired insulin secretion and pancreatic β-cell death in approximately 90% of type 2 diabetic patients. |
| 5091 | 23546612 | We recorded age, sex, BMI, waist/hip ratio, diabetes duration, HbA1c, CVE history, serum amyloid A (SAA), TSH, total (T) and free (F) T4 and T3, reverse T3 (rT3) and TT3/rT3 ratio. |
| 5092 | 23568101 | D-Ala2GIP facilitated synaptic plasticity in AβPP/PS1 and WT mice and reduced the number of amyloid plaques and activated microglia in the cortex of AβPP/PS1 mice. |
| 5093 | 23579860 | A foldamer approach to targeting membrane bound helical states of islet amyloid polypeptide. |
| 5094 | 23579860 | A small molecule, protein mimetic based approach is shown to specifically inhibit lipid catalysed self-assembly of islet amyloid polypeptide (IAPP). |
| 5095 | 23579860 | A foldamer approach to targeting membrane bound helical states of islet amyloid polypeptide. |
| 5096 | 23579860 | A small molecule, protein mimetic based approach is shown to specifically inhibit lipid catalysed self-assembly of islet amyloid polypeptide (IAPP). |
| 5097 | 23603201 | Pharmacological agents, such as dipeptidyl peptidase-4 (DPP-4) inhibitors, which increase the level of glucagon-like peptide-1 (GLP-1) and ameliorate T2D, have become valuable candidates as disease modifying agents in the treatment of AD. |
| 5098 | 23603201 | In addition, endogenous GLP-1 levels decrease amyloid beta (Aβ) peptide and tau phosphorylation in AD. |
| 5099 | 23603201 | The effect of the DPP-4 inhibitor on hippocampal GLP-1 levels, Aβ burden, tau phosphorylation, inflammatory markers and memory retention were evaluated. |
| 5100 | 23603201 | The results reveal an attenuation of Aβ, tau phosphorylation and inflammatory markers and an improvement in hippocampal GLP-1 and memory retention following treatment. |
| 5101 | 23603201 | This remarkable therapeutic effect of Saxagliptin mediated through DPP-4 inhibition demonstrates a unique mechanism for Aβ and tau clearance by increasing GLP-1 levels and reverses the behavioural deficits and pathology observed in AD. |
| 5102 | 23607096 | Amylin is primarily responsible for classifying type II diabetes as an amyloid (protein misfolding) disease as it has great potential to aggregate into toxic nanoparticles, thereby resulting in loss of pancreatic β-cells. |
| 5103 | 23611340 | Deposition of human amylin or islet amyloid polypeptide (hIAPP) within the β-cells of the pancreatic islet of Langerhans is implicated in the etiology of type 2 diabetes mellitus (T2Dm). |
| 5104 | 23707791 | Pharmacological activation of AMPK suppresses inflammatory response evoked by IL-6 signalling in mouse liver and in human hepatocytes. |
| 5105 | 23707791 | Interleukin-6 (IL-6) induces inflammatory signalling in liver, leading to impaired insulin action in hepatocytes. |
| 5106 | 23707791 | In this study, we demonstrate that pharmacological activation of AMP-activated protein kinase (AMPK) represses IL-6-stimulated expression of proinflammatory markers serum amyloid A (Saa) as well as suppressor of cytokine signalling 3 (Socs3) in mouse liver. |
| 5107 | 23707791 | Further studies using the human hepatocellular carcinoma cell line HepG2 suggest that AMPK inhibits IL-6 signalling by repressing IL-6-stimulated phosphorylation of several downstream components of the pathway such as Janus kinase 1 (JAK1), SH2-domain containing protein tyrosine phosphatase 2 (SHP2) and signal transducer and activator of transcription 3 (STAT3). |
| 5108 | 23707791 | In summary, inhibition of IL-6 signalling cascade in liver by the metabolic master switch of the body, AMPK, supports the role of this kinase as a crucial point of convergence of metabolic and inflammatory pathways in hepatocytes. |
| 5109 | 23707907 | Evaluation of membrane models and their composition for islet amyloid polypeptide-membrane aggregation. |
| 5110 | 23707907 | Human islet amyloid polypeptide (IAPP) forms amyloid fibrils in the pancreatic islets of patients suffering from type 2 diabetes mellitus (T2DM). |
| 5111 | 23707907 | Evaluation of membrane models and their composition for islet amyloid polypeptide-membrane aggregation. |
| 5112 | 23707907 | Human islet amyloid polypeptide (IAPP) forms amyloid fibrils in the pancreatic islets of patients suffering from type 2 diabetes mellitus (T2DM). |
| 5113 | 23713771 | Molecular characterization of the hetero-assembly of β-amyloid peptide with islet amyloid polypeptide. |
| 5114 | 23713771 | We have recently identified in vitro a high affinity interaction between β-amyloid peptide (Aβ) of AD and islet amyloid polypeptide (IAPP) of T2D which results in the formation of non-fibrillar and non-cytotoxic Aβ-IAPP hetero-oligomers. |
| 5115 | 23713771 | Molecular characterization of the hetero-assembly of β-amyloid peptide with islet amyloid polypeptide. |
| 5116 | 23713771 | We have recently identified in vitro a high affinity interaction between β-amyloid peptide (Aβ) of AD and islet amyloid polypeptide (IAPP) of T2D which results in the formation of non-fibrillar and non-cytotoxic Aβ-IAPP hetero-oligomers. |
| 5117 | 23719722 | This phenomenon is accompanied by attenuated receptor expression of insulin and insulin-like growth factor, enhanced serine phosphorylation of insulin receptor substrate-1, and impaired transport of insulin across the blood-brain barrier. |
| 5118 | 23719722 | These results, in conjunction with the finding that insulin mitigates hippocampal synapse vulnerability to beta amyloid, a peptide thought to be causative in the development of AD, provide a strong rationale for hypothesizing that pharmacological strategies bolstering brain insulin signaling, such as intranasal administration of insulin, could have significant potential in the treatment and prevention of AD. |
| 5119 | 23729543 | Mutations in SLC29A3 lead to pigmentary hypertrichosis and non-autoimmune insulin-dependent diabetes mellitus (PHID) and H syndromes, familial Rosai-Dorfman disease, and histiocytosis-lymphadenopathy plus syndrome. |
| 5120 | 23729543 | PHID syndrome is a novel monogenic autoinflammatory syndrome (AIS) associated with severe elevation of serum amyloid. |
| 5121 | 23729543 | In contrast to other AIS, blockade of interleukin-1 and tumor necrosis-α was ineffective. |
| 5122 | 23736544 | The dipeptidyl peptidase-4 (DPP-4) inhibitor sitagliptin is an attractive therapy for diabetes, as it increases insulin release and may preserve β-cell mass. |
| 5123 | 23736544 | However, sitagliptin also increases β-cell release of human islet amyloid polypeptide (hIAPP), the peptide component of islet amyloid, which is cosecreted with insulin. |
| 5124 | 23736544 | Islet amyloid deposition, β-cell mass, insulin release, and measures of exocrine pancreas pathology were determined. |
| 5125 | 23736544 | The dipeptidyl peptidase-4 (DPP-4) inhibitor sitagliptin is an attractive therapy for diabetes, as it increases insulin release and may preserve β-cell mass. |
| 5126 | 23736544 | However, sitagliptin also increases β-cell release of human islet amyloid polypeptide (hIAPP), the peptide component of islet amyloid, which is cosecreted with insulin. |
| 5127 | 23736544 | Islet amyloid deposition, β-cell mass, insulin release, and measures of exocrine pancreas pathology were determined. |
| 5128 | 23745697 | Islet amyloid polypeptide and diabetes. |
| 5129 | 23745697 | Islet amyloid polypeptide (IAPP, amylin) is a 37 amino acid residue hormone expressed mainly by pancreatic islet beta cells and to less extent by some gastrointestinal endocrine cells and by certain regions in central nervous system. |
| 5130 | 23745697 | In these tissues calcitonin receptors and receptor activity-modifying proteins (RAMPs) 1 and 3, creating high affinity IAPP receptors have been identified. |
| 5131 | 23745697 | Islet amyloid polypeptide and diabetes. |
| 5132 | 23745697 | Islet amyloid polypeptide (IAPP, amylin) is a 37 amino acid residue hormone expressed mainly by pancreatic islet beta cells and to less extent by some gastrointestinal endocrine cells and by certain regions in central nervous system. |
| 5133 | 23745697 | In these tissues calcitonin receptors and receptor activity-modifying proteins (RAMPs) 1 and 3, creating high affinity IAPP receptors have been identified. |
| 5134 | 23755253 | In this study, we used molecular dynamics simulations to explore the effects of three kinds of carbon nanomaterials including graphene, carbon nanotube and C₆₀ on the aggregation behavior of islet amyloid polypeptide fragment 22-28 (IAPP₂₂₋₂₈). |
| 5135 | 23758815 | Human islet amyloid polypeptide (hIAPP) is highly amyloidogenic, whereas its homologs in rodents are non-amyloidogenic. |
| 5136 | 23776068 | In addition, for the first time, we identified several differentially regulated plasma proteins between healthy control and diabetic rats, including apolipoprotein E, fetuin B, α-1-acid glycoprotein, β-2-glycoprotein 1, 3-hydroxyanthranilate 3,4-dioxygenase, and serum amyloid P-component. |
| 5137 | 23776430 | Genetic associations of type 2 diabetes with islet amyloid polypeptide processing and degrading pathways in asian populations. |
| 5138 | 23776430 | Islet amyloid polypeptide (IAPP) is highly conserved and co-secreted with insulin with over 40% of autopsy cases of T2D showing islet amyloid formation due to IAPP aggregation. |
| 5139 | 23776430 | Amongst the tag SNPs, rs1583645 in carboxypeptidase E (CPE) and rs6583813 in insulin degrading enzyme (IDE) were associated with 1.09 to 1.28 fold increased risk of T2D (P Meta = 9.4×10(-3) and 0.02 respectively) in a meta-analysis of East Asians. |
| 5140 | 23776430 | Genetic associations of type 2 diabetes with islet amyloid polypeptide processing and degrading pathways in asian populations. |
| 5141 | 23776430 | Islet amyloid polypeptide (IAPP) is highly conserved and co-secreted with insulin with over 40% of autopsy cases of T2D showing islet amyloid formation due to IAPP aggregation. |
| 5142 | 23776430 | Amongst the tag SNPs, rs1583645 in carboxypeptidase E (CPE) and rs6583813 in insulin degrading enzyme (IDE) were associated with 1.09 to 1.28 fold increased risk of T2D (P Meta = 9.4×10(-3) and 0.02 respectively) in a meta-analysis of East Asians. |
| 5143 | 23780880 | Insulin, which can deposit at the injection sites in the treatment of diabetes, and islet amyloid polypeptide (IAPP), which can form amyloid fibrils in the islets of Langerhans in diabetes type 2, are kept nonaggregated by charge-based interactions with C-peptide at defined stoichiometries. |
| 5144 | 23794448 | Amylin deposition in the brain: A second amyloid in Alzheimer disease? |
| 5145 | 23796517 | Thermodynamic and structural determinants of differential Pdx1 binding to elements from the insulin and IAPP promoters. |
| 5146 | 23796517 | In adult mammals, the production of insulin and other peptide hormones, such as the islet amyloid polypeptide (IAPP), is limited to β-cells due to tissue-specific expression of a set of transcription factors, the best known of which is pancreatic duodenal homeobox protein 1 (Pdx1). |
| 5147 | 23796517 | Strikingly, while Pdx1 responsive elements in the human insulin promoter conform to the pentanucleotide 5'-CTAAT-3' sequence, the Pdx1 responsive elements in the human iapp promoter all contain a substitution to 5'-TTAAT-3'. |
| 5148 | 23796517 | Taken together, our results suggest a molecular mechanism for differential Pdx1 affinity to elements from the insulin and iapp promoter sequences. |
| 5149 | 23798407 | Here, we present a unique approach, based on combined analysis of four complementary relaxation-based NMR experiments, to probe directly the "dark" NMR-invisible state of the model, intrinsically disordered, polypeptide amyloid β (Aβ40) bound to GroEL. |
| 5150 | 23812099 | CD36 coordinates NLRP3 inflammasome activation by facilitating intracellular nucleation of soluble ligands into particulate ligands in sterile inflammation. |
| 5151 | 23812099 | Particulate ligands, including cholesterol crystals and amyloid fibrils, induce production of interleukin 1β (IL-1β) dependent on the cytoplasmic sensor NLRP3 in atherosclerosis, Alzheimer's disease and diabetes. |
| 5152 | 23812099 | Consequently, macrophages that lacked CD36 failed to elicit IL-1β production in response to those ligands, and targeting CD36 in atherosclerotic mice resulted in lower serum concentrations of IL-1β and accumulation of cholesterol crystals in plaques. |
| 5153 | 23816568 | Recent research has found that increased GSK3β activity is linked to the pathogenesis of AD through amyloid beta (Aβ), phosphorylated tau and mitochondrial dysfunction. |
| 5154 | 23837729 | 1,3-Oxazines as BACE1 and/or BACE2 inhibitors: a patent evaluation (WO2012156284). |
| 5155 | 23837729 | This patent review covers the contents of Hoffman-La Roche and Siena Biotech's patent application WO2012156284 titled '1,3-Oxazines as BACE1 and/or BACE2 Inhibitors.' |
| 5156 | 23837729 | Beta-site amyloid precursor protein-converting enzyme (BACE1) and BACE2 activities are reported to support the claimed compounds' use as therapeutics for Alzheimer's disease and type II diabetes, respectively. |
| 5157 | 23844373 | Researchers have proposed that amyloid precursor protein 17 peptide (APP17 peptide), an active fragment of amyloid precursor protein (APP) in the nervous system, has therapeutic effects on neurodegeneration. |
| 5158 | 23844373 | Meanwhile, the insulin signaling was markedly increased as shown by increased phosphorylation of Akt and enhanced GLUT4 activation. |
| 5159 | 23922768 | The study presented here focuses on the self-association of the type-2 diabetes mellitus related human islet amyloid polypeptide (hIAPP) in various crowded environments including network-forming macromolecular crowding reagents and protein crowders. |
| 5160 | 23927287 | The human Islet Amyloid Polypeptide (hIAPP) is the major constituent of amyloid deposits in pancreatic islets of type-II diabetes. |
| 5161 | 23952054 | Here, we present evidence that two structurally and physiologically unrelated amyloidogenic peptides, the islet amyloid polypeptide (IAPP, the peptide comprising the amyloid aggregates in type II diabetes) and an amyloidogenic determinant of the prion protein (PrP), give rise to a significantly distinct fibrillation pathway when they are incubated together in the presence of membrane bilayers. |
| 5162 | 23966942 | Amylin (islet amyloid polypeptide) and amyloid-beta (Aβ) protein, which are deposited within pancreatic islets of diabetics and brains of Alzheimer's patients respectively, share many biophysical and physiological properties. |
| 5163 | 23968537 | Benzothiazole aniline tetra(ethylene glycol) and 3-amino-1,2,4-triazole inhibit neuroprotection against amyloid peptides by catalase overexpression in vitro. |
| 5164 | 23968537 | The antioxidant enzyme catalase is a neuroprotective amyloid binding protein. |
| 5165 | 23968537 | Herein the effects of catalase overexpression in SH-SY5Y neuronal cells on the toxicity of amyloid-β (Aβ), amyloid-Bri (ABri), amyloid-Dan (ADan), amylin (IAPP), and prion protein (PrP) peptides were determined. |
| 5166 | 23968537 | The catalase inhibitor 3-amino-1,2,4-triazole (3-AT) and catalase-amyloid interaction inhibitor benzothiazole aniline tetra(ethylene glycol) (BTA-EG4) significantly enhanced neurotoxicity of amyloid peptides in catalase overexpressing neuronal cells. |
| 5167 | 23968537 | Kisspeptin 45-50 had additive neuroprotective actions against the Aβ peptide in catalase overexpressing cells. |
| 5168 | 23968537 | Use of BTA-EG4, or compounds that inhibit catalase binding to amyloid peptides, as potential therapeutics for Neurodegenerative diseases may therefore result in unwanted effects. |
| 5169 | 23968537 | Benzothiazole aniline tetra(ethylene glycol) and 3-amino-1,2,4-triazole inhibit neuroprotection against amyloid peptides by catalase overexpression in vitro. |
| 5170 | 23968537 | The antioxidant enzyme catalase is a neuroprotective amyloid binding protein. |
| 5171 | 23968537 | Herein the effects of catalase overexpression in SH-SY5Y neuronal cells on the toxicity of amyloid-β (Aβ), amyloid-Bri (ABri), amyloid-Dan (ADan), amylin (IAPP), and prion protein (PrP) peptides were determined. |
| 5172 | 23968537 | The catalase inhibitor 3-amino-1,2,4-triazole (3-AT) and catalase-amyloid interaction inhibitor benzothiazole aniline tetra(ethylene glycol) (BTA-EG4) significantly enhanced neurotoxicity of amyloid peptides in catalase overexpressing neuronal cells. |
| 5173 | 23968537 | Kisspeptin 45-50 had additive neuroprotective actions against the Aβ peptide in catalase overexpressing cells. |
| 5174 | 23968537 | Use of BTA-EG4, or compounds that inhibit catalase binding to amyloid peptides, as potential therapeutics for Neurodegenerative diseases may therefore result in unwanted effects. |
| 5175 | 23968537 | Benzothiazole aniline tetra(ethylene glycol) and 3-amino-1,2,4-triazole inhibit neuroprotection against amyloid peptides by catalase overexpression in vitro. |
| 5176 | 23968537 | The antioxidant enzyme catalase is a neuroprotective amyloid binding protein. |
| 5177 | 23968537 | Herein the effects of catalase overexpression in SH-SY5Y neuronal cells on the toxicity of amyloid-β (Aβ), amyloid-Bri (ABri), amyloid-Dan (ADan), amylin (IAPP), and prion protein (PrP) peptides were determined. |
| 5178 | 23968537 | The catalase inhibitor 3-amino-1,2,4-triazole (3-AT) and catalase-amyloid interaction inhibitor benzothiazole aniline tetra(ethylene glycol) (BTA-EG4) significantly enhanced neurotoxicity of amyloid peptides in catalase overexpressing neuronal cells. |
| 5179 | 23968537 | Kisspeptin 45-50 had additive neuroprotective actions against the Aβ peptide in catalase overexpressing cells. |
| 5180 | 23968537 | Use of BTA-EG4, or compounds that inhibit catalase binding to amyloid peptides, as potential therapeutics for Neurodegenerative diseases may therefore result in unwanted effects. |
| 5181 | 23968537 | Benzothiazole aniline tetra(ethylene glycol) and 3-amino-1,2,4-triazole inhibit neuroprotection against amyloid peptides by catalase overexpression in vitro. |
| 5182 | 23968537 | The antioxidant enzyme catalase is a neuroprotective amyloid binding protein. |
| 5183 | 23968537 | Herein the effects of catalase overexpression in SH-SY5Y neuronal cells on the toxicity of amyloid-β (Aβ), amyloid-Bri (ABri), amyloid-Dan (ADan), amylin (IAPP), and prion protein (PrP) peptides were determined. |
| 5184 | 23968537 | The catalase inhibitor 3-amino-1,2,4-triazole (3-AT) and catalase-amyloid interaction inhibitor benzothiazole aniline tetra(ethylene glycol) (BTA-EG4) significantly enhanced neurotoxicity of amyloid peptides in catalase overexpressing neuronal cells. |
| 5185 | 23968537 | Kisspeptin 45-50 had additive neuroprotective actions against the Aβ peptide in catalase overexpressing cells. |
| 5186 | 23968537 | Use of BTA-EG4, or compounds that inhibit catalase binding to amyloid peptides, as potential therapeutics for Neurodegenerative diseases may therefore result in unwanted effects. |
| 5187 | 23973293 | Liraglutide can reverse memory impairment, synaptic loss and reduce plaque load in aged APP/PS1 mice, a model of Alzheimer's disease. |
| 5188 | 23973293 | The incretin hormone Glucagon-like peptide-1 (GLP-1) facilitates insulin signalling, and long-lasting analogues such as liraglutide (Victoza(®)) are on the market as type 2 diabetes treatments. |
| 5189 | 23973293 | We have previously shown that liraglutide improved cognitive function, reduced amyloid plaque deposition, inflammation, overall APP and oligomer levels and enhanced LTP when injected peripherally for two months in 7 month old APPswe/PS1ΔE9 (APP/PS1) mice. |
| 5190 | 23973293 | Accordingly, 14-month-old APP/PS1 and littermate control mice were injected with Liraglutide (25 nmol/kg bw) ip. for 2 months. |
| 5191 | 23973293 | Spatial memory was improved by Liraglutide-treatment in APP/PS1 mice compared with APP/PS1 saline-treated mice. |
| 5192 | 23973293 | LTP was significantly enhanced in APP/PS1 liraglutide-treated mice compared with APP/PS1 saline mice, corroborated with increased synapse numbers in hippocampus and cortex. |
| 5193 | 23973293 | Total brain APP and beta-amyloid oligomer levels were reduced in Liraglutide-treated APP/PS1 mice while IDE levels were increased. |
| 5194 | 23994331 | Serum amyloid A is independently related to apolipoprotein A-I but not to HDL-cholesterol in patients with angina pectoris. |
| 5195 | 24010666 | The formation of human islet amyloid polypeptide (hIAPP) is implicated in the loss of pancreatic β-cells in type II diabetes. |
| 5196 | 24015785 | Using thioflavin T fluorescence and electron microscopy, we demonstrate that the outcome of seeding on human islet amyloid polypeptide amyloidogenesis is dependent upon whether the AWI is present or absent and is dictated by seed type. |
| 5197 | 17609417 | Insulin facilitates the hepatic clearance of plasma amyloid beta-peptide (1 40) by intracellular translocation of low-density lipoprotein receptor-related protein 1 (LRP-1) to the plasma membrane in hepatocytes. |
| 5198 | 17609417 | The hepatic clearance of amyloid beta-peptide (1-40) [Abeta(1-40)] from plasma, which is largely mediated by low-density lipoprotein receptor-related protein (LRP-1), is suggested to play a role in preventing Abeta(1-40) accumulation in the brain. |
| 5199 | 17609417 | Epidemiological investigations suggest a high incidence of cerebral Abeta deposition in insulin-resistant type II diabetes mellitus. |
| 5200 | 17609417 | The purpose of this study was to clarify the effect of insulin on the hepatic clearance of Abeta(1-40). |
| 5201 | 17609417 | LRP-1 expression on the hepatic plasma membrane was increased in a time-dependent manner by portal infusion of insulin and was 2.2-fold greater than that in nontreated controls after a 10-min infusion, whereas the expression in whole lysate was not affected by insulin treatment. |
| 5202 | 17609417 | The apparent hepatic uptake of [(125)I]Abeta(1-40) was also induced by insulin in a time-dependent manner. |
| 5203 | 17609417 | The increase in [(125)I]Abeta(1-40) uptake by insulin was concentration-dependent (EC(50) = 230 pM) and was completely abolished by receptor-associated protein (2 muM), an LRP-1 inhibitor. |
| 5204 | 17609417 | In conclusion, plasma insulin facilitates LRP-1 translocation to the hepatic plasma membrane from the intracellular pool, resulting in significant enhancement of hepatic Abeta(1-40) uptake from the circulating blood. |
| 5205 | 17609417 | Insulin facilitates the hepatic clearance of plasma amyloid beta-peptide (1 40) by intracellular translocation of low-density lipoprotein receptor-related protein 1 (LRP-1) to the plasma membrane in hepatocytes. |
| 5206 | 17609417 | The hepatic clearance of amyloid beta-peptide (1-40) [Abeta(1-40)] from plasma, which is largely mediated by low-density lipoprotein receptor-related protein (LRP-1), is suggested to play a role in preventing Abeta(1-40) accumulation in the brain. |
| 5207 | 17609417 | Epidemiological investigations suggest a high incidence of cerebral Abeta deposition in insulin-resistant type II diabetes mellitus. |
| 5208 | 17609417 | The purpose of this study was to clarify the effect of insulin on the hepatic clearance of Abeta(1-40). |
| 5209 | 17609417 | LRP-1 expression on the hepatic plasma membrane was increased in a time-dependent manner by portal infusion of insulin and was 2.2-fold greater than that in nontreated controls after a 10-min infusion, whereas the expression in whole lysate was not affected by insulin treatment. |
| 5210 | 17609417 | The apparent hepatic uptake of [(125)I]Abeta(1-40) was also induced by insulin in a time-dependent manner. |
| 5211 | 17609417 | The increase in [(125)I]Abeta(1-40) uptake by insulin was concentration-dependent (EC(50) = 230 pM) and was completely abolished by receptor-associated protein (2 muM), an LRP-1 inhibitor. |
| 5212 | 17609417 | In conclusion, plasma insulin facilitates LRP-1 translocation to the hepatic plasma membrane from the intracellular pool, resulting in significant enhancement of hepatic Abeta(1-40) uptake from the circulating blood. |