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Gene Information
Gene symbol: MYH7
Gene name: myosin, heavy chain 7, cardiac muscle, beta
HGNC ID: 7577
Synonyms: CMD1S
Related Genes
Related Sentences
| # | PMID | Sentence |
| 1 | 1488051 | Effects of exercise training and diabetes on cardiac myosin heavy chain composition. |
| 2 | 1488051 | This study determined whether the beneficial effects of exercise training on the diabetic heart previously observed are associated with alterations in ventricular myosin heavy chain (MHC) isoform composition. |
| 3 | 1488051 | After 10 wks, ventricular MHC isoenzyme protein composition was analyzed for MHC composition using gel electrophoresis. alpha-MHC and beta-MHC mRNA were determined by Northern and slot blot hybridization techniques. |
| 4 | 1488051 | The results indicate that treadmill exercise training of diabetic rat does not prevent the diabetes-induced shift in MHC composition towards the beta-MHC isoform, thus it is unlikely that the beneficial effects of exercise training on the diabetic heart, previously shown, are due to a normalization of the myosin isoform composition. |
| 5 | 1488051 | Effects of exercise training and diabetes on cardiac myosin heavy chain composition. |
| 6 | 1488051 | This study determined whether the beneficial effects of exercise training on the diabetic heart previously observed are associated with alterations in ventricular myosin heavy chain (MHC) isoform composition. |
| 7 | 1488051 | After 10 wks, ventricular MHC isoenzyme protein composition was analyzed for MHC composition using gel electrophoresis. alpha-MHC and beta-MHC mRNA were determined by Northern and slot blot hybridization techniques. |
| 8 | 1488051 | The results indicate that treadmill exercise training of diabetic rat does not prevent the diabetes-induced shift in MHC composition towards the beta-MHC isoform, thus it is unlikely that the beneficial effects of exercise training on the diabetic heart, previously shown, are due to a normalization of the myosin isoform composition. |
| 9 | 1590733 | Hypertrophic cardiomyopathy: failure to demonstrate mutations in exon 13 of the cardiac beta myosin heavy-chain gene. |
| 10 | 1590733 | Familial hypertrophic cardiomyopathy (FHCM) has been linked to the cardiac beta-myosin heavy-chain (MHC) genes on chromosome 14 (14q1), and a missense mutation within exon 13 of the beta MHC gene has been implicated in the pathogenesis of the disease. |
| 11 | 1590733 | Hypertrophic cardiomyopathy: failure to demonstrate mutations in exon 13 of the cardiac beta myosin heavy-chain gene. |
| 12 | 1590733 | Familial hypertrophic cardiomyopathy (FHCM) has been linked to the cardiac beta-myosin heavy-chain (MHC) genes on chromosome 14 (14q1), and a missense mutation within exon 13 of the beta MHC gene has been implicated in the pathogenesis of the disease. |
| 13 | 1838254 | For the example of myosin heavy chain expression, it is shown that metabolic signals exist which reflect the fuel flux and substrate utilization of the heart muscle cell. |
| 14 | 2634555 | Influence of thyroid hormone on myosin heavy chain mRNA and other messenger RNAs in the rat heart. |
| 15 | 2634555 | The level of myosin heavy chain (MHC) alpha mRNA and of MHC-beta mRNA was quantitated in the rat heart using a specific cDNA probe. |
| 16 | 2634555 | Influence of thyroid hormone on myosin heavy chain mRNA and other messenger RNAs in the rat heart. |
| 17 | 2634555 | The level of myosin heavy chain (MHC) alpha mRNA and of MHC-beta mRNA was quantitated in the rat heart using a specific cDNA probe. |
| 18 | 3062185 | In the rat heart diabetes mellitus leads to a change in myosin heavy chain (MHC) mRNAs and corresponding alterations in myosin isoenzymes as well as a decrease in total cardiac protein synthesis. |
| 19 | 3062185 | However, it is still unknown whether cardiac proteins other than MHC are altered by diabetes and if so whether these abnormalities are mediated by insulin deficiency. |
| 20 | 6232163 | Hormone-induced alterations in myosin isoenzyme predominance are mediated through changes in the formation of two isoforms of myosin heavy chain. |
| 21 | 6232163 | Changes in the expression of different myosin heavy chain genes are most likely responsible for the thyroid hormone and insulin-induced alterations in myosin isoenzyme predominance. |
| 22 | 6232163 | Investigation of the control of myosin heavy chain formation can provide further insights into the hormonal control of a multigene family as well as broaden our understanding of the molecular events which result in altered cardiac contractility. |
| 23 | 6232163 | Hormone-induced alterations in myosin isoenzyme predominance are mediated through changes in the formation of two isoforms of myosin heavy chain. |
| 24 | 6232163 | Changes in the expression of different myosin heavy chain genes are most likely responsible for the thyroid hormone and insulin-induced alterations in myosin isoenzyme predominance. |
| 25 | 6232163 | Investigation of the control of myosin heavy chain formation can provide further insights into the hormonal control of a multigene family as well as broaden our understanding of the molecular events which result in altered cardiac contractility. |
| 26 | 6232163 | Hormone-induced alterations in myosin isoenzyme predominance are mediated through changes in the formation of two isoforms of myosin heavy chain. |
| 27 | 6232163 | Changes in the expression of different myosin heavy chain genes are most likely responsible for the thyroid hormone and insulin-induced alterations in myosin isoenzyme predominance. |
| 28 | 6232163 | Investigation of the control of myosin heavy chain formation can provide further insights into the hormonal control of a multigene family as well as broaden our understanding of the molecular events which result in altered cardiac contractility. |
| 29 | 6365901 | It was found that peptide maps obtained from cardiac myosin heavy chains of hypothyroid and diabetic rats were identical but differed from the maps of myosin heavy chain from control and hormone-treated animals. |
| 30 | 6365901 | These results indicate that the myosin heavy chain RNA species present in the hypothyroid heart is also expressed during insulin deficiency but differs from the species expressed in normal animals. |
| 31 | 6365901 | The expression of the two myosin heavy chain RNA species found in the rat cardiac ventricle appears to be independently regulated by these two hormones. |
| 32 | 6365901 | It was found that peptide maps obtained from cardiac myosin heavy chains of hypothyroid and diabetic rats were identical but differed from the maps of myosin heavy chain from control and hormone-treated animals. |
| 33 | 6365901 | These results indicate that the myosin heavy chain RNA species present in the hypothyroid heart is also expressed during insulin deficiency but differs from the species expressed in normal animals. |
| 34 | 6365901 | The expression of the two myosin heavy chain RNA species found in the rat cardiac ventricle appears to be independently regulated by these two hormones. |
| 35 | 6365901 | It was found that peptide maps obtained from cardiac myosin heavy chains of hypothyroid and diabetic rats were identical but differed from the maps of myosin heavy chain from control and hormone-treated animals. |
| 36 | 6365901 | These results indicate that the myosin heavy chain RNA species present in the hypothyroid heart is also expressed during insulin deficiency but differs from the species expressed in normal animals. |
| 37 | 6365901 | The expression of the two myosin heavy chain RNA species found in the rat cardiac ventricle appears to be independently regulated by these two hormones. |
| 38 | 7481069 | Effects of enalapril treatment on gene expression of smooth muscle myosin heavy chain isoforms in glomeruli of diabetic rats. |
| 39 | 8361080 | The contents of myosin heavy chain, myosin light chain 2, actin, troponin-I in 125-week-old rats decreased compared with those of 12-week-old rats. |
| 40 | 8361080 | Myosin heavy chain, which is one component of myosin, interacts with actin and changes chemical energy to mechanical energy. |
| 41 | 8361080 | The contents of myosin heavy chain, myosin light chain 2, actin, troponin-I in 125-week-old rats decreased compared with those of 12-week-old rats. |
| 42 | 8361080 | Myosin heavy chain, which is one component of myosin, interacts with actin and changes chemical energy to mechanical energy. |
| 43 | 8569762 | This diminished calcium sensitivity along with shifts in cardiac myosin heavy chain (V1-->V3) may be partially responsible for the impaired cardiac function in the hearts of chronic diabetic rats. |
| 44 | 8602116 | Skeletal muscles were additionally analyzed for myosin heavy chain distribution. |
| 45 | 8602116 | Neither the native myosin isoform nor the myosin heavy chain (MHC) distribution profiles of the skeletal muscles were altered by the diabetic state. |
| 46 | 8602116 | Skeletal muscles were additionally analyzed for myosin heavy chain distribution. |
| 47 | 8602116 | Neither the native myosin isoform nor the myosin heavy chain (MHC) distribution profiles of the skeletal muscles were altered by the diabetic state. |
| 48 | 8603771 | Specific antibodies to myosin heavy chain isoforms (SM1, SM2, SMemb), caldesmon, and alpha-smooth muscle actin and cDNAs for SMemb were used. |
| 49 | 8731086 | Expression of a nonmuscle myosin heavy chain in glomerular cells differentiates various types of glomerular disease in rats. |
| 50 | 8731086 | To characterize the phenotypic modulation of mesangial and glomerular epithelial cells, we investigated the expression of a nonmuscle type myosin heavy chain, SMemb, and alpha-smooth muscle actin (alpha-SM actin) in rat experimental glomerular diseases, which included anti-Thy 1 nephritis, 5/6 nephrectomy, diabetes, and anti-glomerular basement membrane nephritis. |
| 51 | 8731086 | Expression of a nonmuscle myosin heavy chain in glomerular cells differentiates various types of glomerular disease in rats. |
| 52 | 8731086 | To characterize the phenotypic modulation of mesangial and glomerular epithelial cells, we investigated the expression of a nonmuscle type myosin heavy chain, SMemb, and alpha-smooth muscle actin (alpha-SM actin) in rat experimental glomerular diseases, which included anti-Thy 1 nephritis, 5/6 nephrectomy, diabetes, and anti-glomerular basement membrane nephritis. |
| 53 | 9052888 | To characterize the molecular mechanism of cardiac and renal complications in non-insulin-dependent diabetes mellitus (NIDDM), we examined the gene expression of Otsuka Long-Evans Tokushima Fatty (OLETF) rats, a new animal model for human NIDDM, at the ages of 14 weeks (prediabetic stage), 30 weeks (NIDDM stage), and 54 weeks (IDDM stage). |
| 54 | 9052888 | In 14-week-old OLETF rats, cardiac mRNAs for transforming growth factor-beta1 (TGF-beta1) and extracellular matrix, including collagen types I, III, and IV and laminin, were significantly increased compared with control rats (Long-Evans Tokushima Otsuka rats). |
| 55 | 9052888 | Cardiac beta-myosin heavy chain (MHC) mRNA of OLETF was increased at 30 and 54 weeks of age, whereas alpha-MHC mRNA of OLETF was inversely decreased at 54 weeks. |
| 56 | 9140815 | Therefore, we determined the separate and combined effects of thyroid hormone (T3) and insulin treatment on rodent cardiac myosin heavy chain (MHC) expression using a model of combined thyroid deficiency (Tx) and diabetes (D). |
| 57 | 9140815 | The combination of Tx and D completely transformed cardiac isomyosin expression such that the fast alpha-myosin heavy chain (MHC) was completely repressed at both the protein and mRNA level of expression; whereas, the slow beta-MHC was upregulated to constitute 100% of the total MHC pool, based on both protein and mRNA analyses. |
| 58 | 9140815 | Daily low doses of exogenous T3 treatment (3 micrograms/kg b.w. i.p.). in the absence of insulin treatment, partially restored expression of the alpha-MHC, while inhibiting expression of the beta-isoform. |
| 59 | 9140815 | Furthermore, when exogenous T3 was administered in conjunction with insulin, the effect on MHC mRNA expression was greater than that of T3 alone, thus suggesting the existence of interaction between T3 and insulin action in the regulation of MHC mRNA expression. |
| 60 | 9140815 | Collectively, these findings suggest that: (a) thyroid state is a dominant regulator of cardiac isomyosin phenotype: and (b) insulin does not exert any regulatory influence on cardiac MHC expression in a severe thyroid deficient state, instead it requires a critical level of circulating T3 in order to be effective in blunting MHC transformation associated with diabetes. |
| 61 | 9140815 | It is thus concluded that the regulation of cardiac MHC by insulin is a complex mechanism involving interaction of insulin with subcellular factors likely to have impact on the specific action of T3. |
| 62 | 9176186 | Previous studies show that diabetes induces marked transformations in cardiac myosin heavy chain (MHC) gene expression that are somehow linked to the cellular action of thyroid hormone 3,5,3'-triiodothyronine (T3). |
| 63 | 9217870 | This diminished calcium sensitivity along with shifts in cardiac myosin heavy chain (V1-->V3) could contribute to the impaired cardiac function in the hearts of chronic diabetic rats. |
| 64 | 9217870 | It has also been reported that sarcomeric proteins such as myosin light chain-2 (MLC-2) and troponin I (TnI) could be involved in regulating muscle contraction and in calcium sensitivity. |
| 65 | 9231659 | Skeletal muscle myosin heavy chain synthesis in type 1 diabetes. |
| 66 | 9231659 | We measured the fractional synthesis rates of myosin heavy chain (MHC), the principal muscle contractile protein, and mixed muscle protein (MMP) in six type 1 diabetic patients during insulin deprivation and insulin treatment. |
| 67 | 9231659 | Skeletal muscle myosin heavy chain synthesis in type 1 diabetes. |
| 68 | 9231659 | We measured the fractional synthesis rates of myosin heavy chain (MHC), the principal muscle contractile protein, and mixed muscle protein (MMP) in six type 1 diabetic patients during insulin deprivation and insulin treatment. |
| 69 | 9256480 | Up-regulation of mRNAs for fetal type myosin heavy chain, atrial natriuretic factor, c-fos, transforming growth factor, and collagens was also observed. |
| 70 | 9843753 | Isolation of human skeletal muscle myosin heavy chain and actin for measurement of fractional synthesis rates. |
| 71 | 9843753 | Using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), we have developed a simple method to isolate myosin heavy chain (MHC) and actin from small (60-80 mg) human skeletal muscle samples for the determination of their fractional synthesis rates. |
| 72 | 9843753 | Isolation of human skeletal muscle myosin heavy chain and actin for measurement of fractional synthesis rates. |
| 73 | 9843753 | Using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), we have developed a simple method to isolate myosin heavy chain (MHC) and actin from small (60-80 mg) human skeletal muscle samples for the determination of their fractional synthesis rates. |
| 74 | 10093642 | Combined cytophotometric and morphometric analysis of muscle fibre properties and myosin heavy chain electrophoresis were performed on extensor digitorum longus and soleus muscles from healthy rats and rats with streptozotocin-induced diabetes. |
| 75 | 10093642 | This is supported by reduced slow and increased fast myosin heavy chain isoforms. |
| 76 | 10093642 | Combined cytophotometric and morphometric analysis of muscle fibre properties and myosin heavy chain electrophoresis were performed on extensor digitorum longus and soleus muscles from healthy rats and rats with streptozotocin-induced diabetes. |
| 77 | 10093642 | This is supported by reduced slow and increased fast myosin heavy chain isoforms. |
| 78 | 10569179 | The steady-state mRNA abundance for alpha-myosin heavy chain in the heart was decreased at 2 and 3 weeks but was unchanged at 5 and 6 weeks, whereas mRNA levels for beta-myosin heavy chain remained elevated during 2-6 weeks after inducing diabetes. |
| 79 | 10580427 | Increases in phosphorylation of the myosin II heavy chain, but not regulatory light chains, correlate with insulin secretion in rat pancreatic islets and RINm5F cells. |
| 80 | 10580427 | Although cytoskeletal proteins such as myosin II are implicated in the control of insulin secretion, their precise role is poorly understood. |
| 81 | 10580427 | In both the insulin-secreting cell line RINm5F and rat pancreatic islets, the RLC was basally phosphorylated on the myosin light chain kinase sites (Ser19/Thr18). |
| 82 | 10580427 | Like the other insulin secretagogues, however, PMA did promote serine phosphorylation of the myosin heavy chain (MHC) in RINm5F cells. |
| 83 | 10580427 | Phosphopeptide mapping suggested that the same peptide was phosphorylated under both PMA and glyceraldehyde stimulation, which further extends our previous study of the Ca2+-dependent phosphorylation of this protein (Wilson JR, Ludowyke RI, Biden TJ: Nutrient stimulation results in a rapid Ca2+-dependent threonine phosphorylation of myosin heavy chain in rat pancreatic islets and RINm5F cells. |
| 84 | 10580427 | Overall, our results demonstrate that in RINm5F cells and rat pancreatic islets, MHC phosphorylation correlates better with insulin secretion than phosphorylation of the RLC. |
| 85 | 10580427 | We therefore propose that in beta-cells, in contrast to other secretory cells, phosphorylation of the MHC is more important than that of the RLC for regulation of the myosin II protein complex during insulin secretion. |
| 86 | 10580427 | Increases in phosphorylation of the myosin II heavy chain, but not regulatory light chains, correlate with insulin secretion in rat pancreatic islets and RINm5F cells. |
| 87 | 10580427 | Although cytoskeletal proteins such as myosin II are implicated in the control of insulin secretion, their precise role is poorly understood. |
| 88 | 10580427 | In both the insulin-secreting cell line RINm5F and rat pancreatic islets, the RLC was basally phosphorylated on the myosin light chain kinase sites (Ser19/Thr18). |
| 89 | 10580427 | Like the other insulin secretagogues, however, PMA did promote serine phosphorylation of the myosin heavy chain (MHC) in RINm5F cells. |
| 90 | 10580427 | Phosphopeptide mapping suggested that the same peptide was phosphorylated under both PMA and glyceraldehyde stimulation, which further extends our previous study of the Ca2+-dependent phosphorylation of this protein (Wilson JR, Ludowyke RI, Biden TJ: Nutrient stimulation results in a rapid Ca2+-dependent threonine phosphorylation of myosin heavy chain in rat pancreatic islets and RINm5F cells. |
| 91 | 10580427 | Overall, our results demonstrate that in RINm5F cells and rat pancreatic islets, MHC phosphorylation correlates better with insulin secretion than phosphorylation of the RLC. |
| 92 | 10580427 | We therefore propose that in beta-cells, in contrast to other secretory cells, phosphorylation of the MHC is more important than that of the RLC for regulation of the myosin II protein complex during insulin secretion. |
| 93 | 10909963 | Based on myosin heavy chain (MHC) expression, fibers were pooled into 3 groups (MHC I, MHC IIA, and MHC IIX), and the GLUT4 content of 15-40 pooled fibers was determined using SDS-PAGE and immunological detection. |
| 94 | 10909963 | Two weeks of exercise training increased (P < 0.05) the peak power output of the knee extensors by 13%, the maximal activities of citrate synthase and 3-hydroxyacyl-CoA dehydrogenase by 21 and 18%, respectively, and the GLUT4 protein content by 26% in a muscle homogenate. |
| 95 | 11133928 | Effects of different activity and inactivity paradigms on myosin heavy chain gene expression in striated muscle. |
| 96 | 11133928 | The goal of this mini-review is to summarize findings concerning the role that different models of muscular activity and inactivity play in altering gene expression of the myosin heavy chain (MHC) family of motor proteins in mammalian cardiac and skeletal muscle. |
| 97 | 11133928 | Effects of different activity and inactivity paradigms on myosin heavy chain gene expression in striated muscle. |
| 98 | 11133928 | The goal of this mini-review is to summarize findings concerning the role that different models of muscular activity and inactivity play in altering gene expression of the myosin heavy chain (MHC) family of motor proteins in mammalian cardiac and skeletal muscle. |
| 99 | 11557574 | Altered K(+) channel gene expression in diabetic rat ventricle: isoform switching between Kv4.2 and Kv1.4. |
| 100 | 11557574 | Kv1.4 mRNA levels increased 179% relative to controls, whereas Kv4.3 mRNA levels were unaffected. |
| 101 | 11557574 | Immunohistochemistry and Western blot analysis of the diabetic heart showed that the density of the Kv4.2 protein decreased, whereas Kv1.4 protein increased. |
| 102 | 11557574 | Thus isoform switching from Kv4.2 to Kv1.4 is most likely the mechanism underlying the slower kinetics of transient outward K(+) current observed in the diabetic ventricle. |
| 103 | 11557574 | Brain Kv1.4, Kv4.2, or Kv4.3 mRNA levels were unaffected by diabetes. |
| 104 | 11557574 | Myosin heavy chain (MHC) gene expression was altered with a 32% decrease in alpha-MHC mRNA and a 259% increase in beta-MHC mRNA levels in diabetic ventricle. |
| 105 | 11557574 | Low-dose insulin-like growth factor-II (IGF-II) treatment during the last 6 of the 12 wk of diabetes (DM + IGF) protected against these changes in MHC mRNAs despite continued hyperglycemia and body weight loss. |
| 106 | 11723046 | Fractional synthesis rate (FSR) of mitochondrial and cytoplasmic proteins in liver, heart, and skeletal muscle, as well as myosin heavy chain (MHC) in muscle, were measured using L-[1-(13)C]leucine as a tracer. |
| 107 | 11851361 | STZ increased humoral (glucose and non-esterified fatty acids) and heart gene expression (myosin heavy chain beta, pyruvate dehydrogenase kinase 4 and uncoupling protein 3) markers of diabetes. |
| 108 | 11915909 | Using stable isotope tracer methodologies and mass spectrometric detection, we observed: (a) 76-92-year-old physically frail and 62-74-year-old middle-age adults have lower mixed muscle protein synthetic rates than 20-32-year-old men and women; (b) 2 weeks and 3 months of weightlifting exercise increased the synthetic rate of myosin heavy chain (MHC) and mixed muscle proteins to a similar magnitude in frail, middle-age, and young women and men; (c) Serum myostatin-immunoreactive protein levels were elevated in physically frail women and were inversely correlated with lean mass. |
| 109 | 12552126 | To explore the role of peroxisome proliferator-activated receptor alpha (PPARalpha)-mediated derangements in myocardial metabolism in the pathogenesis of diabetic cardiomyopathy, insulinopenic mice with PPARalpha deficiency (PPARalpha(-/-)) or cardiac-restricted overexpression [myosin heavy chain (MHC)-PPAR] were characterized. |
| 110 | 12851393 | Role of antisense RNA in coordinating cardiac myosin heavy chain gene switching. |
| 111 | 12851393 | A novel mechanism of regulation of cardiac alpha and beta myosin heavy chain gene by naturally occurring antisense transcription was elucidated via pre-mRNA analysis. |
| 112 | 12851393 | Herein, we report the expression of an antisense beta myosin heavy chain RNA in the normal rodent myocardium. |
| 113 | 12851393 | Our results demonstrate that the beta-alpha myosin heavy chain intergenic DNA possesses a bidirectional transcriptional activity, one direction transcribing the alpha gene, and the opposite direction transcribing the antisense beta RNA. |
| 114 | 12851393 | Role of antisense RNA in coordinating cardiac myosin heavy chain gene switching. |
| 115 | 12851393 | A novel mechanism of regulation of cardiac alpha and beta myosin heavy chain gene by naturally occurring antisense transcription was elucidated via pre-mRNA analysis. |
| 116 | 12851393 | Herein, we report the expression of an antisense beta myosin heavy chain RNA in the normal rodent myocardium. |
| 117 | 12851393 | Our results demonstrate that the beta-alpha myosin heavy chain intergenic DNA possesses a bidirectional transcriptional activity, one direction transcribing the alpha gene, and the opposite direction transcribing the antisense beta RNA. |
| 118 | 12851393 | Role of antisense RNA in coordinating cardiac myosin heavy chain gene switching. |
| 119 | 12851393 | A novel mechanism of regulation of cardiac alpha and beta myosin heavy chain gene by naturally occurring antisense transcription was elucidated via pre-mRNA analysis. |
| 120 | 12851393 | Herein, we report the expression of an antisense beta myosin heavy chain RNA in the normal rodent myocardium. |
| 121 | 12851393 | Our results demonstrate that the beta-alpha myosin heavy chain intergenic DNA possesses a bidirectional transcriptional activity, one direction transcribing the alpha gene, and the opposite direction transcribing the antisense beta RNA. |
| 122 | 12897182 | Muscle strength (239 +/- 43 vs. 208 +/- 33 N m), quadriceps area (8463 +/- 453 vs. 7763 +/- 329 mm2) and glycogen content (458 +/- 22 vs. 400 +/- 26 mmol (kg dry weight muscle)(-1)) decreased, while myosin heavy chain isoform IIX increased 4-fold in dT vs. |
| 123 | 12933346 | Gender differences in myosin heavy chain-beta and phosphorylated phospholamban in diabetic rat hearts. |
| 124 | 12933346 | The objective of this study was to determine whether a gender difference exists in myosin heavy chain (MHC) isoform or sarcoplasmic reticulum protein levels in diabetic rat hearts. |
| 125 | 12933346 | Insulin treatment completely normalized blood glucose level, cardiac SERCA2a and PLB protein levels, and the decrease in MHC-beta levels in both male and female diabetic rats. |
| 126 | 12933346 | Insulin treatment completely normalized serum insulin and almost completely normalized phosphorylation of PLB at serine 16 in male diabetic rats. |
| 127 | 12933346 | Also, insulin treatment almost completely normalized phosphorylation of PLB at threonine 17 in female diabetic rats; however, the increase was significantly greater than that identified for insulin-treated male diabetic rats. |
| 128 | 12933346 | We conclude that higher levels of MHC-beta and dephosphorylated PLB may contribute to more contractile dysfunction in male than in female diabetic rat hearts, and that phosphorylation of PLB at threonine 17 is more responsive to insulin in female diabetic rat hearts. |
| 129 | 12933346 | Gender differences in myosin heavy chain-beta and phosphorylated phospholamban in diabetic rat hearts. |
| 130 | 12933346 | The objective of this study was to determine whether a gender difference exists in myosin heavy chain (MHC) isoform or sarcoplasmic reticulum protein levels in diabetic rat hearts. |
| 131 | 12933346 | Insulin treatment completely normalized blood glucose level, cardiac SERCA2a and PLB protein levels, and the decrease in MHC-beta levels in both male and female diabetic rats. |
| 132 | 12933346 | Insulin treatment completely normalized serum insulin and almost completely normalized phosphorylation of PLB at serine 16 in male diabetic rats. |
| 133 | 12933346 | Also, insulin treatment almost completely normalized phosphorylation of PLB at threonine 17 in female diabetic rats; however, the increase was significantly greater than that identified for insulin-treated male diabetic rats. |
| 134 | 12933346 | We conclude that higher levels of MHC-beta and dephosphorylated PLB may contribute to more contractile dysfunction in male than in female diabetic rat hearts, and that phosphorylation of PLB at threonine 17 is more responsive to insulin in female diabetic rat hearts. |
| 135 | 12941780 | In hearts from citrate-treated control rats, angiotensin II-stimulated [(3)H]phenylalanine incorporation and atrial natriuretic peptide and beta-myosin heavy chain mRNA expression were prevented by B-type natriuretic peptide (BNP), bradykinin, the ACE inhibitor ramiprilat, and the neutral endopeptidase inhibitor candoxatrilat. |
| 136 | 15001437 | Depressed cardiac tension cost in experimental diabetes is due to altered myosin heavy chain isoform expression. |
| 137 | 15153434 | It may partner with junD, NF-kB, PEM, SMAD3, RPA2, FANCD2, NM23beta, nonmuscle myosin heavy chain II-A, GFAP, and/or vimentin. |
| 138 | 15362513 | Therefore, we examined the effects of RAS blockade by enalapril, an angiotensin-converting enzyme inhibitor, and losartan, an angiotensin receptor AT1 antagonist, on cardiac function, myofibrillar and myosin ATPase activity as well as myosin heavy chain (MHC) isozyme expression in diabetic hearts. |
| 139 | 15362513 | Both drugs also attenuated the decrease in myofibrillar Ca2+-ATPase, Mg2+-ATPase and myosin ATPase activity seen in diabetic rats. |
| 140 | 15522914 | Intramyocardial lipid deposition was associated with an up-regulation of peroxisome proliferator-activated receptor alpha (PPARalpha) -regulated genes, myosin heavy chain beta (MHC-beta), and tumor necrosis factor alpha (TNF-alpha). |
| 141 | 15680071 | This study was undertaken to analyse the changes in expression of 5 cardiac genes, including atrial natriuretic peptide, alpha- and beta-myosin heavy chain, and cardiac and skeletal alpha-actin genes, using a rat neonatal model, in which cardiac hypertrophy was induced via maternal diabetes. |
| 142 | 15680071 | In the first 28 days, the level of mRNA for alpha-myosin heavy chain increased slightly, while that for atrial natriuretic peptide and beta-myosin heavy chain decreased continuously similar to the controls, but at a significantly faster rate. |
| 143 | 15680071 | This study was undertaken to analyse the changes in expression of 5 cardiac genes, including atrial natriuretic peptide, alpha- and beta-myosin heavy chain, and cardiac and skeletal alpha-actin genes, using a rat neonatal model, in which cardiac hypertrophy was induced via maternal diabetes. |
| 144 | 15680071 | In the first 28 days, the level of mRNA for alpha-myosin heavy chain increased slightly, while that for atrial natriuretic peptide and beta-myosin heavy chain decreased continuously similar to the controls, but at a significantly faster rate. |
| 145 | 15797988 | We tested the hypothesis whether systemic PPARgamma activation, by changing the metabolic profile in a model of insulin resistance and type 2 diabetes (the ZDF rat) in vivo, improves contractile function of the heart in vitro. |
| 146 | 15797988 | In ZDF-V hearts, transcript levels of PPARalpha-regulated genes and of myosin heavy chain-beta were upregulated, whereas GLUT4 was downregulated compared with ZL. |
| 147 | 15797988 | Agonist treatment of ZDF rats reduced PPARalpha-regulated genes and increased transcripts of GLUT4 and GLUT1. |
| 148 | 15797988 | In conclusion, by changing the metabolic profile, reducing myocardial lipid accumulation, and promoting the downregulation of PPARalpha-regulated genes, PPARgamma activation leads to an increased capacity of the myocardium to oxidize glucose and to a tighter coupling of oxidative metabolism and contraction in the setting of insulin resistance and type 2 diabetes. |
| 149 | 15831797 | Single-fiber diameter, Ca(2+)-activated peak force, specific tension, activation threshold, and pCa(50) as well as the myosin heavy chain isoform expression (MHC) were determined. |
| 150 | 15883415 | Decreases in the synthesis rates of many muscle proteins, specifically of myosin heavy chain and mitochondrial proteins, occur with age. |
| 151 | 16046301 | Increased p85/55/50 expression and decreased phosphotidylinositol 3-kinase activity in insulin-resistant human skeletal muscle. |
| 152 | 16046301 | We found a highly significant inverse correlation between in vivo insulin sensitivity (as measured by the glucose infusion rate) and increased protein expression of p85/55/50, protein kinase C (PKC)-theta activity, levels of pSer307 insulin receptor substrate (IRS)-1 and p-Jun NH2-terminal kinase (JNK)-1, and myosin heavy chain IIx fibers. |
| 153 | 16046301 | Increased basal phosphorylation of Ser307 IRS-1 in the obese and type 2 diabetic subjects corresponds with decrease in insulin-stimulated IRS-1 tyrosine phosphorylation, PI 3-kinase activity, and insulin-induced activation of Akt and, more prominently, PKC-zeta/lambda. |
| 154 | 16046301 | In summary, increased expression of the PI 3-kinase adaptor subunits p85/55/50, as well as increased activity of the proinflammatory kinases JNK-1, PKC-theta, and, to a lesser extent, inhibitor of kappaB kinase-beta, are associated with increased basal Ser307 IRS-1 phosphorylation and decreased PI 3-kinase activity and may follow a common pathway to attenuate in vivo insulin sensitivity in insulin-resistant subjects. |
| 155 | 16054675 | This study evaluated mature and immature myosin heavy chain (MHC) isoform immunolocalisation in soleus muscle of diabetic rats with documented motor neuropathy. |
| 156 | 16123338 | Cardiac-specific overexpression of peroxisome proliferator-activated receptor-alpha causes insulin resistance in heart and liver. |
| 157 | 16123338 | Mice with heart-specific overexpression of peroxisome proliferator-activated receptor (PPAR)alpha showed a metabolic and cardiomyopathic phenotype similar to the diabetic heart, and we determined tissue-specific glucose metabolism and insulin action in vivo during hyperinsulinemic-euglycemic clamps in awake myosin heavy chain (MHC)-PPARalpha mice (12-14 weeks of age). |
| 158 | 16123338 | Basal and insulin-stimulated glucose uptake in heart was significantly reduced in the MHC-PPARalpha mice, and cardiac insulin resistance was mostly attributed to defects in insulin-stimulated activities of insulin receptor substrate (IRS)-1-associated phosphatidylinositol (PI) 3-kinase, Akt, and tyrosine phosphorylation of signal transducer and activator of transcription 3 (STAT3). |
| 159 | 16123338 | Interestingly, MHC-PPARalpha mice developed hepatic insulin resistance associated with defects in insulin-mediated IRS-2-associated PI 3-kinase activity, increased hepatic triglyceride, and circulating interleukin-6 levels. |
| 160 | 16123338 | Overall, these findings indicate that increased activity of PPARalpha, as occurs in the diabetic heart, leads to cardiac insulin resistance associated with defects in insulin signaling and STAT3 activity, subsequently leading to reduced cardiac function. |
| 161 | 16124998 | In addition, a decrease in whole body protein turnover, mixed muscle protein synthesis, myosin heavy chain synthesis, and mitochondrial protein synthesis have been reported. |
| 162 | 16205433 | Effect of endurance exercise on myosin heavy chain isoform expression in diabetic rats with peripheral neuropathy. |
| 163 | 16631532 | Metallothionein alleviates cardiac dysfunction in streptozotocin-induced diabetes: role of Ca2+ cycling proteins, NADPH oxidase, poly(ADP-Ribose) polymerase and myosin heavy chain isozyme. |
| 164 | 16631532 | This study was designed to examine the effect of cardiac overexpression of the heavy metal scavenger metallothionein (MT) on cardiac contractile function, intracellular Ca(2+) cycling proteins, stress-activated signaling molecules and the myosin heavy chain (MHC) isozyme in diabetes. |
| 165 | 16631532 | Diabetes enhanced expression of the AT(1) receptor, phospholamban, the p47(phox) NADPH oxidase subunit and poly(ADP-ribose) polymerase (PARP), depressed the level of SERCA2a, Na(+)-Ca(2+) exchanger and triggered a beta-MHC isozyme switch. |
| 166 | 16631532 | Collectively, these data suggest a beneficial effect of MT in the therapeutics of diabetic cardiomyopathy, possibly through a mechanism related to NADPH oxidase, PARP and MHC isozyme switch. |
| 167 | 16631532 | Metallothionein alleviates cardiac dysfunction in streptozotocin-induced diabetes: role of Ca2+ cycling proteins, NADPH oxidase, poly(ADP-Ribose) polymerase and myosin heavy chain isozyme. |
| 168 | 16631532 | This study was designed to examine the effect of cardiac overexpression of the heavy metal scavenger metallothionein (MT) on cardiac contractile function, intracellular Ca(2+) cycling proteins, stress-activated signaling molecules and the myosin heavy chain (MHC) isozyme in diabetes. |
| 169 | 16631532 | Diabetes enhanced expression of the AT(1) receptor, phospholamban, the p47(phox) NADPH oxidase subunit and poly(ADP-ribose) polymerase (PARP), depressed the level of SERCA2a, Na(+)-Ca(2+) exchanger and triggered a beta-MHC isozyme switch. |
| 170 | 16631532 | Collectively, these data suggest a beneficial effect of MT in the therapeutics of diabetic cardiomyopathy, possibly through a mechanism related to NADPH oxidase, PARP and MHC isozyme switch. |
| 171 | 16777978 | C-jun N-terminal kinase mediates tumor necrosis factor-alpha suppression of differentiation in myoblasts. |
| 172 | 16777978 | The stress kinase c-jun N-terminal kinase (JNK) was recently shown to be involved in the pathophysiology of major inflammatory conditions, including Alzheimer's disease, stroke, obesity, and type II diabetes. |
| 173 | 16777978 | Here we used a novel, JNK interacting protein (JIP)-derived JNK peptide inhibitor to establish that JNK suppresses the biological activity of IGF-I in skeletal muscle progenitor cells. |
| 174 | 16777978 | In these myoblasts, TNFalpha and its downstream receptor substrates, neutral-sphingomyelinase (N-SMase) and N-acetyl-d-sphingosine (C2-ceramide), induce JNK kinase activity in a time-dependent manner. |
| 175 | 16777978 | Consistent with these results, TNFalpha induces JNK binding to insulin receptor substrate 1 (IRS-1) but is unable to inhibit IGF-I-induced IRS-1 tyrosine phosphorylation in myoblasts that are treated with the JNK peptide inhibitor. |
| 176 | 16777978 | More importantly, JNK activation induced by TNFalpha, C2-ceramide, and N-SMase is associated with reduced expression of the critical muscle transcription factor myogenin as well as the differentiation marker myosin heavy chain (MHC). |
| 177 | 16777978 | The JNK peptide inhibitor, but not the control peptide, completely reverses this inhibition of both myogenin and MHC. |
| 178 | 16777978 | In the absence of IGF-I, TNFalpha, C2-ceramide, N-SMase and the JNK inhibitor are inactive, as shown by their inability to affect IRS tyrosine phosphorylation and protein expression of myogenin and MHC. |
| 179 | 16777978 | These results establish that the resistance of muscle progenitor cells to IGF-I, which is caused by inflammatory stimuli, is mediated by the JNK stress kinase pathway. |
| 180 | 16885993 | A key mechanism regulating this interaction and subsequent development and maintenance of force is alternative splicing of SM myosin heavy chain (MHC) and 17 kDa essential SM myosin light chain (MLC) pre-mRNAs. |
| 181 | 16935841 | Oxidative balance, advanced glycated end products (AGEs) and AGE receptors, cardiac myogenic factors, and myosin heavy-chain gene expression were determined in the left ventricle of treated and untreated STZ-diabetic rats and ZDF rats. |
| 182 | 16935841 | Nuclear factor-kappaB activation triggered a cascade of signaling, which finally led to the switch in the cardiac myosin heavy-chain (MHC) gene expression from the alpha-MHC isoform to the beta-MHC isoform. |
| 183 | 16935841 | DHEA treatment, by preventing the activation of the oxidative pathways induced by hyperglycemia, counteracted the enhanced AGE receptor activation in the heart of STZ-diabetic rats and ZDF rats and normalized downstream signaling, thus avoiding impairment of the cardiac myogenic factors, heart autonomic nervous system and neural crest derivatives (HAND) and myogenic enhancer factor-2, and the switch in MHC gene expression, which are the early events in diabetic cardiomyopathy. |
| 184 | 16935841 | Oxidative balance, advanced glycated end products (AGEs) and AGE receptors, cardiac myogenic factors, and myosin heavy-chain gene expression were determined in the left ventricle of treated and untreated STZ-diabetic rats and ZDF rats. |
| 185 | 16935841 | Nuclear factor-kappaB activation triggered a cascade of signaling, which finally led to the switch in the cardiac myosin heavy-chain (MHC) gene expression from the alpha-MHC isoform to the beta-MHC isoform. |
| 186 | 16935841 | DHEA treatment, by preventing the activation of the oxidative pathways induced by hyperglycemia, counteracted the enhanced AGE receptor activation in the heart of STZ-diabetic rats and ZDF rats and normalized downstream signaling, thus avoiding impairment of the cardiac myogenic factors, heart autonomic nervous system and neural crest derivatives (HAND) and myogenic enhancer factor-2, and the switch in MHC gene expression, which are the early events in diabetic cardiomyopathy. |
| 187 | 17307996 | Two genes encoding cardiac myosin heavy chain (MHC) isoforms, beta and alpha, are arranged in tandem 4.5 kb apart. |
| 188 | 18037994 | To address its role in myocardial metabolism, we generated transgenic mice with cardiac-specific expression of PPARbeta/delta, driven by the myosin heavy chain (MHC-PPARbeta/delta mice). |
| 189 | 18037994 | In reporter assays, we showed that PPARbeta/delta and PPARalpha exerted differential transcriptional control of the GLUT4 promoter, which may explain the observed isotype-specific effects on glucose uptake. |
| 190 | 18042831 | Protein analysis showed increased levels of the myosin heavy chain, slow fiber type protein, and the complexes I, II, III, IV, and V of the oxidative phosphorylation. |
| 191 | 18199585 | IGF-I alleviates diabetes-induced RhoA activation, eNOS uncoupling, and myocardial dysfunction. |
| 192 | 18199585 | This study was designed to delineate the beneficial effects of IGF-I with a focus on RhoA, Akt, and eNOS coupling. |
| 193 | 18199585 | Diabetes-induced O2(-) accumulation was ablated by the NO synthase (NOS) inhibitor nitro-L-arginine methyl ester (L-NAME), indicating endothelial NOS (eNOS) uncoupling, all of which except heart size were negated by IGF-I. |
| 194 | 18199585 | Diabetes depressed expression of Kv1.2 and dihydrofolate reductase (DHFR), increased beta-myosin heavy-chain expression, stimulated p38 MAPK, and reduced levels of total Akt and phosphorylated Akt/eNOS, all of which with the exception of myosin heavy chain were attenuated by IGF-I. |
| 195 | 18199585 | In addition, Y27632 and the eNOS coupler folate abrogated glucose toxicity-induced PS decline, TR90 prolongation, while it increased O2(-) and decreased NO and Kv1.2 levels. |
| 196 | 18286426 | Studies have demonstrated MSCs transplantation can prevent apoptosis of ischemic heart via upregulation of Akt and eNOS and inhibit myocardial fibrosis of dilated cardiomyopathy by decreasing the expression of matrix metalloproteinase (MMP) in rat models. |
| 197 | 18286426 | Using independent experimental approaches, we showed that MSCs presented in the myocardium 4 weeks after transplantation and some of them were positive for the cardiac markers Troponin T and myosin heavy chain. |
| 198 | 18286426 | Furthermore, MSCs transplantation increased MMP-2 activity and decreased transcriptional level of MMP-9. |
| 199 | 18372234 | Concurrently, we found in D and DS an increase in cardiac beta-myosin heavy chain, atrial natriuretic peptide, skeletal alpha-actin mRNA, type III collagen, and transforming growth factor-beta. |
| 200 | 18372234 | Myocardial angiotensin-converting enzyme (ACE) mRNA levels were increased while ACE2 mRNA levels were decreased in both D and DS groups. |
| 201 | 18372234 | Cardiac angiotensin-1 (AT1) receptor protein levels were unchanged but the levels of phosphorylated (p) ERK and Jun-NH(2)-protein kinase (JNK) were increased in D and DS. |
| 202 | 18372234 | The increase in ACE, the decrease in ACE2, and the increase in cardiac pERK and pJNK suggest an increase in free angiotensin II and AT1R signaling in the diabetic myocardium as a possible mechanism contributing to cardiac remodeling in diabetes. |
| 203 | 18514627 | Changes in enzyme (reduced nicotinamide adenine dinucleotide-dehydrogenase, cytochrome c oxidase) activities and myosin heavy chain (MHC) composition were measured in the left ventricle. |
| 204 | 18566944 | Muscle alterations include gross atrophy and shift to fast myosin heavy chain in the hemiparetic (contralateral) leg muscle; both are related to gait deficit severity. |
| 205 | 18566945 | These gene differences were consistent with reported differences after stroke in areas such as injury and inflammation markers, the myosin heavy chain profile, and high prevalence of impaired glucose tolerance and type 2 diabetes. |
| 206 | 18670098 | Inhibition of monocyte chemoattractant protein-1 by Krüppel-like factor 5 small interfering RNA in the tumor necrosis factor- alpha-activated human umbilical vein endothelial cells. |
| 207 | 18670098 | This study was made to determine whether KLF5 may associate with MCP-1 expression in human umbilical vein endothelial cells (HUVECs) induced by tumor necrosis factor-alpha (TNF-alpha), in terms of the initial events of damaged vascular cells in diabetes. |
| 208 | 18670098 | MCP-1 expression was markedly augmented by the treatment of TNF-alpha to HUVECs, but this augmentation was inhibited by KLF5 small interfering RNA, which primarily suppressed the expression of KLF5 at mRNA levels in the cells. |
| 209 | 18670098 | Though TNF-alpha augmented the levels of endothelin-1 (ET-1) and attenuated those of embryonic form of myosin heavy chain (SMemb) in HUVECs, the inhibition of KLF5 did not affect the levels of these cytokines in the cells. |
| 210 | 18794854 | Multiple common SNPs (allele frequencies ranging from 0.2 to 0.6) in the gene encoding nonmuscle myosin heavy chain type II isoform A (MYH9) were associated with two to four times greater risk of nondiabetic ESRD and accounted for a large proportion of the excess risk of ESRD observed in African compared to European Americans. |
| 211 | 19153477 | Polymorphisms in the nonmuscle myosin heavy chain 9 gene (MYH9) are associated with albuminuria in hypertensive African Americans: the HyperGEN study. |
| 212 | 19158402 | In addition, adult MGsKO mice showed an increased proportion of type I (slow-twitch, oxidative) fibers based on kinetic properties and myosin heavy chain isoforms, despite the fact that these muscles had reduced expression of peroxisome proliferator-activated receptor coactivator protein-1alpha (PGC-1alpha) and reduced mitochondrial content and oxidative capacity. |
| 213 | 19387472 | Linkage to chromosome 22q13, independent of diabetes and hypertension, was detected over a region containing the non-muscle myosin heavy chain type II isoform A (MYH9) gene (LOD score=3.52). |
| 214 | 19567477 | Non-muscle myosin heavy chain 9 gene MYH9 associations in African Americans with clinically diagnosed type 2 diabetes mellitus-associated ESRD. |
| 215 | 19633204 | Dimethylthiourea normalizes velocity-dependent, but not force-dependent, index of ventricular performance in diabetic rats: role of myosin heavy chain isozyme. |
| 216 | 19633204 | Both normalized E(max) (E(maxn)) and afterload-adjusted Q(max) (Q(maxad)) were depressed in diabetic rats, concomitant with altered myosin heavy chain (MHC) isoform composition and its upstream regulators, such as myocyte enhancer factor-2 (MEF-2) and heart autonomic nervous system and neural crest derivatives (HAND). |
| 217 | 19633204 | Dimethylthiourea normalizes velocity-dependent, but not force-dependent, index of ventricular performance in diabetic rats: role of myosin heavy chain isozyme. |
| 218 | 19633204 | Both normalized E(max) (E(maxn)) and afterload-adjusted Q(max) (Q(maxad)) were depressed in diabetic rats, concomitant with altered myosin heavy chain (MHC) isoform composition and its upstream regulators, such as myocyte enhancer factor-2 (MEF-2) and heart autonomic nervous system and neural crest derivatives (HAND). |
| 219 | 19684093 | The CAAT-binding transcription factor 1/nuclear factor 1 binding site is important in beta-myosin heavy chain antisense promoter regulation in rats. |
| 220 | 19684093 | The rat heart expresses two myosin heavy chain (MHC) isoforms, beta and alpha; these genes are arranged in tandem on the same chromosome. |
| 221 | 19684093 | In the present paper, we demonstrate with electrophoretic mobility shift analyses that ventricular nuclear proteins are interacting with a nuclear factor 1/CAAT-binding transcription factor 1 (NF1/CTF1) binding site, and a supershift assay indicates that the protein binding at this site is antigenetically related to the CTF1/NF1 factor. |
| 222 | 19684093 | Moreover, a mutation of the CTF1/NF1 site within the 559 bp promoter region nearly abolished promoter activity in vivo in control, STZ- and PTU-treated rats. |
| 223 | 19684093 | The CAAT-binding transcription factor 1/nuclear factor 1 binding site is important in beta-myosin heavy chain antisense promoter regulation in rats. |
| 224 | 19684093 | The rat heart expresses two myosin heavy chain (MHC) isoforms, beta and alpha; these genes are arranged in tandem on the same chromosome. |
| 225 | 19684093 | In the present paper, we demonstrate with electrophoretic mobility shift analyses that ventricular nuclear proteins are interacting with a nuclear factor 1/CAAT-binding transcription factor 1 (NF1/CTF1) binding site, and a supershift assay indicates that the protein binding at this site is antigenetically related to the CTF1/NF1 factor. |
| 226 | 19684093 | Moreover, a mutation of the CTF1/NF1 site within the 559 bp promoter region nearly abolished promoter activity in vivo in control, STZ- and PTU-treated rats. |
| 227 | 19738937 | The sarcoplasmic reticulum Ca(2+)-ATPase (SERCA) isoforms are normally expressed in coordination with the corresponding myosin heavy chain (MyHC) isoforms in the fibers of skeletal muscle but this coordination is often disrupted in pathological conditions. |
| 228 | 19801494 | Consistent with metabolic perturbation, and a switch to fatty acid oxidation from glucose oxidation in Ins2WT/C96Y hearts, expression of mitochondrial long-chain acyl-CoA dehydrogenase and pyruvate dehydrogenase kinase isoform 4 were increased. |
| 229 | 19801494 | Insulin treatment reversed the diastolic dysfunction, the elevated B-type natriuretic peptide and beta-myosin heavy chain, and the reduced sarcoplasmic reticulum Ca2+-ATPase 2a levels with abolition of cardiac lipotoxicity. |
| 230 | 20090419 | We have examined gene expression changes and studied histone H3 and H4 acetylation as well as dimethylation of lysine 4 on histone H3 on promoters of alpha-Myosin heavy chain gene (alpha-MHC), beta-Myosin heavy chain gene (beta-MHC), Atrial natriuretic peptide gene (ANp), B-type natriuretic peptide gene (BNP) and Sarcoplasmic reticulum Ca(2+) ATPase gene (SERCA2a). |
| 231 | 20347640 | Novel genetic analysis methods and recently identified major kidney disease susceptibility genes are discussed, including novel perspectives for categorizing complex forms of nephropathy based on the expanding spectrum of non-muscle myosin heavy chain 9 gene-associated disease. |
| 232 | 20930262 | Our findings indicate that doxorubicin modulates the expression of the hypertrophy-associated genes, ventricular myosin light chain-2, the alpha isoform of myosin heavy chain and atrial natriuretic peptide, an effect which is augmented by Trichostatin A. |
| 233 | 21074826 | Admixture mapping recently identified the nonmuscle myosin heavy chain 9 gene (MYH9) as a susceptibility factor strongly associated with several nondiabetic etiologies of end-stage renal disease in African Americans, less strongly with diabetes-associated end-stage renal disease. |
| 234 | 21136853 | In T1DM with DN, beta-actin and three isoforms of tubulin beta-2 chain, tropomodulin-3, and LASP-1 were decreased, whereas two tubulin beta-4 chain isoforms, one alpha actinin-4 isoform, membrane-organizing extension spike protein (MOESIN), FLJ00279 (corresponding to a fragment of myosin heavy chain, non-muscle type A), vinculin, a tropomyosin isoform, and the macrophage capping protein were increased. |
| 235 | 21216827 | Expression of genes encoding various L-type Ca(2+) channel proteins (Cacna1c, Cacna1g, Cacna1h and Cacna2d1) and cardiac muscle proteins (Myh7) were upregulated, and genes encoding intracellular Ca(2+) transport regulatory proteins (Atp2a2 and Calm1) and some cardiac muscle proteins (Myh6, Myl2, Actc1, Tnni3, Tnn2, and Tnnc1) were downregulated in ZDF heart compared with control heart. |
| 236 | 21216827 | A change in the expression of genes encoding myosin heavy chain and L-type Ca(2+) channel proteins might partly underlie alterations in the time course of contraction and Ca(2+) transients in ventricular myocytes from ZDF rats. |
| 237 | 21216827 | Expression of genes encoding various L-type Ca(2+) channel proteins (Cacna1c, Cacna1g, Cacna1h and Cacna2d1) and cardiac muscle proteins (Myh7) were upregulated, and genes encoding intracellular Ca(2+) transport regulatory proteins (Atp2a2 and Calm1) and some cardiac muscle proteins (Myh6, Myl2, Actc1, Tnni3, Tnn2, and Tnnc1) were downregulated in ZDF heart compared with control heart. |
| 238 | 21216827 | A change in the expression of genes encoding myosin heavy chain and L-type Ca(2+) channel proteins might partly underlie alterations in the time course of contraction and Ca(2+) transients in ventricular myocytes from ZDF rats. |
| 239 | 21321124 | We sought to evaluate the metabolic and functional consequences of chronic suppression of GO in heart as modeled by transgenic mice with cardiac-specific overexpression of pyruvate dehydrogenase kinase 4 (myosin heavy chain (MHC)-PDK4 mice), an inhibitor of pyruvate dehydrogenase. |
| 240 | 21321124 | The expression of the known AMP-activated protein kinase target, peroxisome proliferator-activated receptor γ coactivator-1α (PGC-1α), a master regulator of mitochondrial function and biogenesis, was also activated in the MHC-PDK4 heart. |
| 241 | 21417718 | The diabetic rat heart and high glucose conditions increased the ratio of myosin heavy-chain isoform β to α indicative of diseased states; thus, this model system captures some molecular aspects of diabetic cardiomyopathy. |
| 242 | 21436590 | Here, we show that the α-isoform of myosin heavy chain (α-MyHC, which is encoded by the gene Myh6) is the pathogenic autoantigen for CD4+ T cells in a spontaneous mouse model of myocarditis. |
| 243 | 21478152 | Resistin promotes cardiac hypertrophy via the AMP-activated protein kinase/mammalian target of rapamycin (AMPK/mTOR) and c-Jun N-terminal kinase/insulin receptor substrate 1 (JNK/IRS1) pathways. |
| 244 | 21478152 | Resistin has been suggested to be involved in the development of diabetes and insulin resistance. |
| 245 | 21478152 | Therefore, we wanted to elucidate the mechanisms associated with resistin-induced cardiac hypertrophy and myocardial insulin resistance. |
| 246 | 21478152 | Overexpression of resistin using adenoviral vector in neonatal rat ventricular myocytes was associated with inhibition of AMP-activated protein kinase (AMPK) activity, activation of tuberous sclerosis complex 2/mammalian target of rapamycin (mTOR) pathway, and increased cell size, [(3)H]leucine incorporation (i.e. protein synthesis) and mRNA expression of the hypertrophic marker genes, atrial natriuretic factor, brain natriuretic peptide, and β-myosin heavy chain. |
| 247 | 21478152 | Activation of AMPK with 5-aminoimidazole-4-carbozamide-1-β-D-ribifuranoside or inhibition of mTOR with rapamycin or mTOR siRNA attenuated these resistin-induced changes. |
| 248 | 21478152 | Furthermore, resistin increased serine phosphorylation of insulin receptor substrate (IRS1) through the activation of the apoptosis signal-regulating kinase 1/c-Jun N-terminal Kinase (JNK) pathway, a module known to stimulate insulin resistance. |
| 249 | 21478152 | Inhibition of JNK (with JNK inhibitor SP600125 or using dominant-negative JNK) reduced serine 307 phosphorylation of IRS1. |
| 250 | 21478152 | Resistin also stimulated the activation of p70(S6K), a downstream kinase target of mTOR, and increased phosphorylation of the IRS1 serine 636/639 residues, whereas treatment with rapamycin reduced the phosphorylation of these residues. |
| 251 | 21478152 | These data demonstrate that resistin induces cardiac hypertrophy and myocardial insulin resistance, possibly via the AMPK/mTOR/p70(S6K) and apoptosis signal-regulating kinase 1/JNK/IRS1 pathways. |
| 252 | 21765056 | The HFNC group demonstrated a myosin heavy chain (MHC) isoform switch from fast MHC-α to slow MHC-β, which was prevented in the HFSAT group. |
| 253 | 21849968 | Hemoglobin S, non-muscle myosin heavy chain 9 (MYH9), and apolipoprotein L1 (APOL1) risk variants were genotyped in 3258 unrelated African Americans: 1085 with non-diabetic ESRD, 996 with type 2 diabetes-associated ESRD, and 1177 controls. |
| 254 | 21849968 | Since APOL1 is strongly associated with ESRD in African Americans, interactions between APOL1 and MYH9 risk variants and hemoglobin S were assessed using case-only and case-control centered two-way logistic regression interaction analyses. |
| 255 | 21849968 | In addition, no evidence of APOL1 or MYH9 interactions with sickle cell trait was detected. |
| 256 | 22031600 | This study explored the role of the NADPH oxidase Nox4 as a source of reactive oxygen species (ROS) involved in the development of diabetic cardiomyopathy. |
| 257 | 22031600 | NADPH oxidase activity, ROS generation, and the expression of Nox4, but Nox1 or Nox2, were increased in left ventricular tissue of the diabetic rats. |
| 258 | 22031600 | Expression of molecular markers of hypertrophy and myofibrosis including fibronectin, collagen, α-smooth muscle actin, and β-myosin heavy chain were also increased. |
| 259 | 22031600 | Exposure of cultured cardiac myocytes to 25 mM glucose [high glucose (HG)] increased NADPH oxidase activity, the expression of Nox4, and molecular markers of cardiac injury. |
| 260 | 22311732 | Tadalafil reversed the coordinated alterations of cytoskeletal/contractile proteins such as myosin light chain (MLY) 2 and 4, myosin heavy chain α and myosin-binding protein C which contributes to contractile dysfunction. |
| 261 | 22311732 | The expression of intermediate filament protein vimentin and extra-cellular matrix proteins like cysteine and glycine rich protein-3 and collagen type VI α were upregulated in db/db mice indicating cardiac remodeling in diabetes. |
| 262 | 22311732 | Tadalafil also enhanced antioxidant enzyme glutathione S-transferase Kappa-1 (GSKT-1) and downregulated redox regulatory chaperones like heat shock protein 8 (HSPA8), and 75 kD glucose regulatory protein (75GRP). |
| 263 | 22396201 | A novel method to measure glucose uptake and myosin heavy chain isoform expression of single fibers from rat skeletal muscle. |
| 264 | 22396201 | Fiber type (myosin heavy chain [MHC] isoform) and glucose uptake were determined for each single fiber. |
| 265 | 22396201 | A novel method to measure glucose uptake and myosin heavy chain isoform expression of single fibers from rat skeletal muscle. |
| 266 | 22396201 | Fiber type (myosin heavy chain [MHC] isoform) and glucose uptake were determined for each single fiber. |
| 267 | 22592762 | The cavernous tissue segments were subjected to quantitative real-time polymerase chain reaction to determine the expressions of smooth muscle α-actin (SMA), SM myosin heavy chain (SMMHC), smoothelin, calponin and myocardin. |
| 268 | 22592762 | Cell contractility in vitro and western blot analysis of SMA and SMMHC in the cavernous tissues and cells were determined. |
| 269 | 22592762 | Compared with the control group (n=8) and the diabetes mellitus group (n=5), the expressions of SMA, calponin, SMMHC, smoothelin and myocardin mRNA were decreased in the cavernous tissues in rats of the diabetic erectile dysfunction group (n=15; P=0.001 and 0.02, P=0.014 and 0.012, both P<0.001, P=0.005 and <0.001, P=0.003 and 0.035, respectively). |
| 270 | 22592762 | The levels of SMA and SMMHC proteins showed a significant decrease in cavernous tissues and cultured cells in rats of the diabetic erectile dysfunction group. |
| 271 | 23029549 | We created mice with cardiac specific expression of human AR (hAR) using the α-myosin heavy chain (MHC) promoter and studied these animals during aging and with reduced fatty acid (FA) oxidation. hAR transgenic expression did not alter cardiac function or glucose and FA oxidation gene expression in young mice. |
| 272 | 23196711 | To define the role of Astragalus Polysaccharides (APS) treatment for PPARα-mediated lipotoxicity in the pathogenesis of diabetic cardiomyopathy, myosin heavy chain [MHC]-PPARα mice with high-fat diet were administrated with APS or vehicle for 16 weeks. |
| 273 | 23285077 | Polymorphisms in the non-muscle myosin heavy chain gene (MYH9) are associated with lower glomerular filtration rate in mixed ancestry diabetic subjects from South Africa. |
| 274 | 23342106 | To determine if Mtor plays a role during mouse cardiac development, cardiomyocyte specific Mtor deletion was achieved using α myosin heavy chain (α-MHC) driven Cre recombinase. |
| 275 | 23349479 | In contrast, myosin heavy chain promoter (MHC)-ATGL mice were resistant to diabetes-induced increases in intramyocardial TAG levels, lipotoxicity, and cardiac dysfunction. |
| 276 | 23567901 | To determine why this occurs, we studied the effects of FO in mice with heart failure either due to transgenic expression of the lipid uptake protein acyl CoA synthetase 1 (ACS1) or overexpression of the transcription factor peroxisomal proliferator-activated receptor (PPAR) γ via the cardiac-specific myosin heavy chain (MHC) promoter. |
| 277 | 23567901 | Compared with control mice fed with NPD, ACS1, and MHC-PPARγ, mice fed with NPD had reduced cardiac function and survival with cardiac fibrosis. |
| 278 | 23776349 | Pilot study of an association between a common variant in the non-muscle myosin heavy chain 9 (MYH9) gene and type 2 diabetic nephropathy in a Taiwanese population. |
| 279 | 23776349 | Recent studies have demonstrated that the myosin, heavy chain 9, non-muscle (MYH9) gene is associated with ESRD in African Americans. |
| 280 | 23776349 | Pilot study of an association between a common variant in the non-muscle myosin heavy chain 9 (MYH9) gene and type 2 diabetic nephropathy in a Taiwanese population. |
| 281 | 23776349 | Recent studies have demonstrated that the myosin, heavy chain 9, non-muscle (MYH9) gene is associated with ESRD in African Americans. |
| 282 | 23942549 | After thirteen weeks of treatment, metabolic changes were observed; additionally, the switching of muscle fiber types was also apparent through myosin heavy chain remodeling, implying that changes are occurring at the molecular level. |
| 283 | 24012810 | Increased myocardial short-range forces in a rodent model of diabetes reflect elevated content of β myosin heavy chain. |
| 284 | 24012810 | The STZ-induced increase in short-ranges forces is thus unlikely to reflect changes to titin and/or collagen filaments. |
| 285 | 24012810 | Gel electrophoresis showed that STZ increased the relative expression of β myosin heavy chain. |
| 286 | 24012810 | Increased myocardial short-range forces in a rodent model of diabetes reflect elevated content of β myosin heavy chain. |
| 287 | 24012810 | The STZ-induced increase in short-ranges forces is thus unlikely to reflect changes to titin and/or collagen filaments. |
| 288 | 24012810 | Gel electrophoresis showed that STZ increased the relative expression of β myosin heavy chain. |