# |
PMID |
Sentence |
1 |
1380870
|
Dynamics of 7B2 and galanin expression in solitary magnocellular hypothalamic vasopressin neurons of the homozygous Brattleboro rat.
|
2 |
1380870
|
The phenotypic expression of coexisting peptides in mutant magnocellular VP cells shows a differential pattern. 7B2 is one of the peptides which is not detectable, whereas there is a clear galanin expression.
|
3 |
1380870
|
Here we report the presence of 7B2 and galanin in these heterozygous cells, which suggests that for the expression of 7B2, but not for that of galanin, the relative amount of mutant VP precursor must be diminished.
|
4 |
1380870
|
Dynamics of 7B2 and galanin expression in solitary magnocellular hypothalamic vasopressin neurons of the homozygous Brattleboro rat.
|
5 |
1380870
|
The phenotypic expression of coexisting peptides in mutant magnocellular VP cells shows a differential pattern. 7B2 is one of the peptides which is not detectable, whereas there is a clear galanin expression.
|
6 |
1380870
|
Here we report the presence of 7B2 and galanin in these heterozygous cells, which suggests that for the expression of 7B2, but not for that of galanin, the relative amount of mutant VP precursor must be diminished.
|
7 |
1380870
|
Dynamics of 7B2 and galanin expression in solitary magnocellular hypothalamic vasopressin neurons of the homozygous Brattleboro rat.
|
8 |
1380870
|
The phenotypic expression of coexisting peptides in mutant magnocellular VP cells shows a differential pattern. 7B2 is one of the peptides which is not detectable, whereas there is a clear galanin expression.
|
9 |
1380870
|
Here we report the presence of 7B2 and galanin in these heterozygous cells, which suggests that for the expression of 7B2, but not for that of galanin, the relative amount of mutant VP precursor must be diminished.
|
10 |
3065775
|
The pancreatic 7B2 concentration was significantly high in ob/ob mice (p less than 0.05, versus the concentration in their lean littermates, and the decrease observed in older NOD mice, appeared to parallel their insulin reserve.
|
11 |
3143472
|
In mutant Brattleboro rats, which have aberrant AVP, which results in diabetes insipidus, 7B2 appears to be markedly decreased in vasopressinergic neurons and absent in their corresponding neurohypophyseal terminals.
|
12 |
9011109
|
In contrast, following intravenous glucagon infusion, serum 7B2 levels increased only in diabetic patients treated with oral hypoglycemic agents (n = 20) and did not increase in controls (n = 5): the group having the highest insulin secretion activity in the present study, nor in diet or insulin-treated diabetic patients.
|
13 |
9011109
|
These data suggest that an extra-pancreatic source which produces the observed serum 7B2 increase following oral glucose intake can not be excluded and that 7B2 may not be secreted concomitantly with insulin from the pancreatic beta cell in response to intravenous glucagon injection.
|
14 |
9011109
|
In contrast, following intravenous glucagon infusion, serum 7B2 levels increased only in diabetic patients treated with oral hypoglycemic agents (n = 20) and did not increase in controls (n = 5): the group having the highest insulin secretion activity in the present study, nor in diet or insulin-treated diabetic patients.
|
15 |
9011109
|
These data suggest that an extra-pancreatic source which produces the observed serum 7B2 increase following oral glucose intake can not be excluded and that 7B2 may not be secreted concomitantly with insulin from the pancreatic beta cell in response to intravenous glucagon injection.
|
16 |
9814487
|
The vasopressin precursor is not processed in the hypothalamus of Wolfram syndrome patients with diabetes insipidus: evidence for the involvement of PC2 and 7B2.
|
17 |
9814487
|
Wolfram syndrome (WS) is characterized by optic atrophy, insulin-dependent diabetes mellitus, vasopressin (VP)-sensitive diabetes insipidus, and neurosensory hearing loss.
|
18 |
9814487
|
In addition, the proprotein convertase PC2 and the molecular chaperone 7B2 were absent.
|
19 |
9814487
|
As expression of PC2 and 7B2 was detected in the nearby nucleus basalis of Meynert of one WS patient and in the anterior lobe of the other WS patient, the absence of the two proteins in the paraventricular nucleus was not due to mutations in their genes.
|
20 |
9814487
|
The vasopressin precursor is not processed in the hypothalamus of Wolfram syndrome patients with diabetes insipidus: evidence for the involvement of PC2 and 7B2.
|
21 |
9814487
|
Wolfram syndrome (WS) is characterized by optic atrophy, insulin-dependent diabetes mellitus, vasopressin (VP)-sensitive diabetes insipidus, and neurosensory hearing loss.
|
22 |
9814487
|
In addition, the proprotein convertase PC2 and the molecular chaperone 7B2 were absent.
|
23 |
9814487
|
As expression of PC2 and 7B2 was detected in the nearby nucleus basalis of Meynert of one WS patient and in the anterior lobe of the other WS patient, the absence of the two proteins in the paraventricular nucleus was not due to mutations in their genes.
|
24 |
9814487
|
The vasopressin precursor is not processed in the hypothalamus of Wolfram syndrome patients with diabetes insipidus: evidence for the involvement of PC2 and 7B2.
|
25 |
9814487
|
Wolfram syndrome (WS) is characterized by optic atrophy, insulin-dependent diabetes mellitus, vasopressin (VP)-sensitive diabetes insipidus, and neurosensory hearing loss.
|
26 |
9814487
|
In addition, the proprotein convertase PC2 and the molecular chaperone 7B2 were absent.
|
27 |
9814487
|
As expression of PC2 and 7B2 was detected in the nearby nucleus basalis of Meynert of one WS patient and in the anterior lobe of the other WS patient, the absence of the two proteins in the paraventricular nucleus was not due to mutations in their genes.
|
28 |
10389844
|
To explore the role of chronically elevated free fatty acids (FFAs) in the pathogenesis of the hyperproinsulinemia of type 2 diabetes, we have investigated the effect of FFAs on proinsulin processing and prohormone convertases PC2 and PC1/PC3 in MIN6 cells cultured in Dulbecco's modified Eagle's medium with or without 0.5 mmol/l FFA mixture (palmitic acid:oleic acid = 1:2).
|
29 |
10389844
|
The biosynthesis and secretion of proinsulin and insulin were analyzed by comparing the incorporation of [3H]Leu and [35S]Met.
|
30 |
10389844
|
Levels of cellular PC2 and PC3 analyzed by Western blotting were decreased by 23 and 15%, respectively.
|
31 |
10389844
|
However, PC2, PC3, proinsulin, and 7B2 mRNA levels were not altered by FFA exposure.
|
32 |
10389844
|
To test for an effect on the biosynthesis of PC2, PC3, proinsulin, and 7B2, a protein required for PC2 activation, MIN6 cells were labeled with [35S]Met for 10-15 min, followed by a prolonged chase.
|
33 |
10389844
|
Similar inhibitory effects were noted on the processing of proPC3, proinsulin, and 7B2.
|
34 |
10389844
|
In conclusion, prolonged exposure of beta-cells to FFAs may affect the biosynthesis and posttranslational processing of proinsulin, PC2, PC3, and 7B2, and thereby contribute to the hyperproinsulinemia of type 2 diabetes.
|
35 |
10389844
|
To explore the role of chronically elevated free fatty acids (FFAs) in the pathogenesis of the hyperproinsulinemia of type 2 diabetes, we have investigated the effect of FFAs on proinsulin processing and prohormone convertases PC2 and PC1/PC3 in MIN6 cells cultured in Dulbecco's modified Eagle's medium with or without 0.5 mmol/l FFA mixture (palmitic acid:oleic acid = 1:2).
|
36 |
10389844
|
The biosynthesis and secretion of proinsulin and insulin were analyzed by comparing the incorporation of [3H]Leu and [35S]Met.
|
37 |
10389844
|
Levels of cellular PC2 and PC3 analyzed by Western blotting were decreased by 23 and 15%, respectively.
|
38 |
10389844
|
However, PC2, PC3, proinsulin, and 7B2 mRNA levels were not altered by FFA exposure.
|
39 |
10389844
|
To test for an effect on the biosynthesis of PC2, PC3, proinsulin, and 7B2, a protein required for PC2 activation, MIN6 cells were labeled with [35S]Met for 10-15 min, followed by a prolonged chase.
|
40 |
10389844
|
Similar inhibitory effects were noted on the processing of proPC3, proinsulin, and 7B2.
|
41 |
10389844
|
In conclusion, prolonged exposure of beta-cells to FFAs may affect the biosynthesis and posttranslational processing of proinsulin, PC2, PC3, and 7B2, and thereby contribute to the hyperproinsulinemia of type 2 diabetes.
|
42 |
10389844
|
To explore the role of chronically elevated free fatty acids (FFAs) in the pathogenesis of the hyperproinsulinemia of type 2 diabetes, we have investigated the effect of FFAs on proinsulin processing and prohormone convertases PC2 and PC1/PC3 in MIN6 cells cultured in Dulbecco's modified Eagle's medium with or without 0.5 mmol/l FFA mixture (palmitic acid:oleic acid = 1:2).
|
43 |
10389844
|
The biosynthesis and secretion of proinsulin and insulin were analyzed by comparing the incorporation of [3H]Leu and [35S]Met.
|
44 |
10389844
|
Levels of cellular PC2 and PC3 analyzed by Western blotting were decreased by 23 and 15%, respectively.
|
45 |
10389844
|
However, PC2, PC3, proinsulin, and 7B2 mRNA levels were not altered by FFA exposure.
|
46 |
10389844
|
To test for an effect on the biosynthesis of PC2, PC3, proinsulin, and 7B2, a protein required for PC2 activation, MIN6 cells were labeled with [35S]Met for 10-15 min, followed by a prolonged chase.
|
47 |
10389844
|
Similar inhibitory effects were noted on the processing of proPC3, proinsulin, and 7B2.
|
48 |
10389844
|
In conclusion, prolonged exposure of beta-cells to FFAs may affect the biosynthesis and posttranslational processing of proinsulin, PC2, PC3, and 7B2, and thereby contribute to the hyperproinsulinemia of type 2 diabetes.
|
49 |
10389844
|
To explore the role of chronically elevated free fatty acids (FFAs) in the pathogenesis of the hyperproinsulinemia of type 2 diabetes, we have investigated the effect of FFAs on proinsulin processing and prohormone convertases PC2 and PC1/PC3 in MIN6 cells cultured in Dulbecco's modified Eagle's medium with or without 0.5 mmol/l FFA mixture (palmitic acid:oleic acid = 1:2).
|
50 |
10389844
|
The biosynthesis and secretion of proinsulin and insulin were analyzed by comparing the incorporation of [3H]Leu and [35S]Met.
|
51 |
10389844
|
Levels of cellular PC2 and PC3 analyzed by Western blotting were decreased by 23 and 15%, respectively.
|
52 |
10389844
|
However, PC2, PC3, proinsulin, and 7B2 mRNA levels were not altered by FFA exposure.
|
53 |
10389844
|
To test for an effect on the biosynthesis of PC2, PC3, proinsulin, and 7B2, a protein required for PC2 activation, MIN6 cells were labeled with [35S]Met for 10-15 min, followed by a prolonged chase.
|
54 |
10389844
|
Similar inhibitory effects were noted on the processing of proPC3, proinsulin, and 7B2.
|
55 |
10389844
|
In conclusion, prolonged exposure of beta-cells to FFAs may affect the biosynthesis and posttranslational processing of proinsulin, PC2, PC3, and 7B2, and thereby contribute to the hyperproinsulinemia of type 2 diabetes.
|
56 |
10816641
|
Emphasis on PC1, PC2/7B2, POMC and the novel enzyme SKI-1.
|
57 |
10816641
|
Processing of POMC at dibasic residues is tissue-specific and is performed by either PC1 alone (resulting in ACTH and beta LPH, anterior pituitary corticotrophes) or by a combination of PC1 and PC2 (yielding alpha MSH and beta END, pituitary neurointermediate lobe and hypothalamus).
|
58 |
10816641
|
Structure-function studies of these enzymes demonstrated the presence of N- and C-terminal domains, as well as specific amino acids within the catalytic segment that influence the degree of activity of each enzyme and the interaction of PC2 with 7B2.
|
59 |
10816641
|
The phenotypic consequences of the absence of genetic expression of either PC1 or PC2 are now explored using knockout mice and in human patients suffering from obesity and diabetes.
|
60 |
10816641
|
Emphasis on PC1, PC2/7B2, POMC and the novel enzyme SKI-1.
|
61 |
10816641
|
Processing of POMC at dibasic residues is tissue-specific and is performed by either PC1 alone (resulting in ACTH and beta LPH, anterior pituitary corticotrophes) or by a combination of PC1 and PC2 (yielding alpha MSH and beta END, pituitary neurointermediate lobe and hypothalamus).
|
62 |
10816641
|
Structure-function studies of these enzymes demonstrated the presence of N- and C-terminal domains, as well as specific amino acids within the catalytic segment that influence the degree of activity of each enzyme and the interaction of PC2 with 7B2.
|
63 |
10816641
|
The phenotypic consequences of the absence of genetic expression of either PC1 or PC2 are now explored using knockout mice and in human patients suffering from obesity and diabetes.
|
64 |
11086001
|
We report the identification of betaIV spectrin, a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512.
|
65 |
11086001
|
The betaIV spectrin gene is located on human and mouse chromosomes 19q13.13 and 7b2, respectively.
|
66 |
11086001
|
In brain, betaIV spectrin is enriched in myelinated neurons, where it colocalizes with ankyrin(G) 480/270-kD at axon initial segments and nodes of Ranvier.
|
67 |
12475375
|
Immunofluorescence microscopy comparing GK and Wistar control rat pancreata revealed marked changes in the distribution of alpha-cells and pronounced beta-cell heterogeneity in the expression patterns of insulin, prohormone convertases PC1, PC2, carboxypeptidase E (CPE) and the PC-binding proteins 7B2 and ProSAAS.
|
68 |
12475375
|
Western blot analyses of isolated islets revealed little difference in PC1 and CPE expression but PC2 immunoreactivity was markedly lower in the GK islets.
|
69 |
12475375
|
No differences were seen in the biosynthesis and post-translational modification of PC1, PC2 or CPE following incubation of islets in 16.7 mM glucose, but incubation in 3.3 mM glucose resulted in decreased PC2 biosynthesis in the GK islets.
|
70 |
15618358
|
Role of carboxypeptidase E in processing of pro-islet amyloid polypeptide in {beta}-cells.
|
71 |
15618358
|
Islet amyloid polypeptide (IAPP; amylin) is a peptide hormone that is cosecreted with insulin from beta-cells.
|
72 |
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.
|
73 |
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.
|
74 |
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.
|
75 |
15618358
|
Role of carboxypeptidase E in processing of pro-islet amyloid polypeptide in {beta}-cells.
|
76 |
15618358
|
Islet amyloid polypeptide (IAPP; amylin) is a peptide hormone that is cosecreted with insulin from beta-cells.
|
77 |
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.
|
78 |
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.
|
79 |
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.
|