Cardiac myosin isozyme changes following aortic stenosis in 25 day old rats

1983 ◽  
Vol 15 ◽  
pp. 63
Author(s):  
L BUGAISKY
Keyword(s):  
Aortic Stenosis ◽  
Cardiac Myosin ◽  
Old Rats ◽  
Myosin Isozyme

scholarly journals Lack of Effect of Running Training at Two Intensities on Cardiac Myosin Isozyme Composition in Rats.

2000 ◽  
Vol 50 (6) ◽  
pp. 577-583 ◽  
Author(s):  
Shuichi Machida ◽  
Fumihiko Kariya ◽  
Keizo Kobayashi ◽  
Mitsuo Narusawa
Keyword(s):  
Cardiac Myosin ◽  
Running Training ◽  
Myosin Isozyme

Exercise alters cardiac myosin isozyme distribution in obese Zucker and Wistar rats

1990 ◽  
Vol 69 (1) ◽  
pp. 380-383 ◽  
Author(s):  
G. S. Morris ◽  
K. M. Baldwin ◽  
J. M. Lash ◽  
R. L. Hamlin ◽  
W. M. Sherman
Keyword(s):  
Exercise Training ◽  
Atpase Activity ◽  
Functional Capacity ◽  
Wistar Rats ◽  
Cardiac Contractility ◽  
Cardiac Myosin ◽  
Endurance Exercise Training ◽  
Obese Rats ◽  
Myosin Isozyme ◽  
Glucose Availability

Recent evidence suggests that exercise training may significantly increase the expression of the cardiac myosin isozyme V1 in the diabetic heart, a change associated with improved cardiac functional capacity. To test this hypothesis, cardiac myofibrillar adenosinetriphosphatase (ATPase) activity and myosin isozyme profiles were determined in trained and sedentary male hyperinsulinemic obese Zucker (OZT, OZS) and obese Wistar (OWT, OWS) rats. Lean sedentary (LZS, LWS) animals served as age-matched controls. Myofibrillar ATPase activity and the relative quantity of the high-ATPase isozyme V1 was significantly lower in both strains of sedentary obese rats than in the respective lean sedentary controls (P less than 0.05). Both 5 (OZT) and 10 wk (OWT) of moderate treadmill training increased these markers of cardiac myosin biochemistry in the obese animals (P less than 0.05). Thus, endurance exercise training remodels the cardiac isomyosin profile of hyperinsulinemic rats and, in doing so, may enhance cardiac contractility and functional capacity. Such changes may reflect an improvement in glucose availability and utilization in these hearts.

scholarly journals Cardiac myosin-binding protein C is a novel marker of myocardial injury and fibrosis in aortic stenosis

Heart ◽  
2017 ◽  
Vol 104 (13) ◽  
pp. 1101-1108 ◽  
Author(s):  
Atul Anand ◽  
Calvin Chin ◽  
Anoop S V Shah ◽  
Jacek Kwiecinski ◽  
Alex Vesey ◽  
...  
Keyword(s):  
Aortic Stenosis ◽  
Myocardial Fibrosis ◽  
Protein C ◽  
Myocardial Injury ◽  
Cardiac Myosin ◽  
Sarcomeric Protein ◽  
Myosin Binding Protein ◽  
Myosin Binding Protein C ◽  
Unit Increase ◽  
Myosin Binding

ObjectiveCardiac myosin-binding protein C (cMyC) is an abundant sarcomeric protein and novel highly specific marker of myocardial injury. Myocyte death characterises the transition from hypertrophy to replacement myocardial fibrosis in advanced aortic stenosis. We hypothesised that serum cMyC concentrations would be associated with cardiac structure and outcomes in patients with aortic stenosis.MethodscMyC was measured in two cohorts in which serum had previously been prospectively collected: a mechanism cohort of patients with aortic stenosis (n=161) and healthy controls (n=46) who underwent cardiac MRI, and an outcome cohort with aortic stenosis (n=104) followed for a median of 11.3 years.ResultsIn the mechanism cohort, cMyC concentration correlated with left ventricular mass (adjusted β=11.0 g/m2 per log unit increase in cMyC, P<0.001), fibrosis volume (adjusted β=8.0 g, P<0.001) and extracellular volume (adjusted β=1.3%, P=0.01) in patients with aortic stenosis but not in controls. In those with late gadolinium enhancement (LGE) indicative of myocardial fibrosis, cMyC concentrations were higher (32 (21–56) ng/L vs 17 (12–24) ng/L without LGE, P<0.001). cMyC was unrelated to coronary calcium scores. Unadjusted Cox proportional hazards analysis in the outcome cohort showed greater all-cause mortality (HR 1.49 per unit increase in log cMyC, 95% CI 1.11 to 2.01, P=0.009).ConclusionsSerum cMyC concentration is associated with myocardial hypertrophy, fibrosis and an increased risk of mortality in aortic stenosis. The quantification of serum sarcomeric protein concentrations provides objective measures of disease severity and their clinical utility to monitor the progression of aortic stenosis merits further study.Clinical trial registrationNCT1755936; Post-results.

Altered Expression of Cardiac Myosin Isozymes Associated with the Malignant Hyperthermia Genotype in Swine

2000 ◽  
Vol 93 (5) ◽  
pp. 1312-1319 ◽  
Author(s):  
Ying-Ming Liou ◽  
Meei Jyh Jiang ◽  
Ming-Che Wu
Keyword(s):  
Atpase Activity ◽  
Malignant Hyperthermia ◽  
Myofibrillar Atpase ◽  
Cardiac Myosin ◽  
Long Term Effects ◽  
Altered Expression ◽  
Cardiac Symptoms ◽  
Myofibrillar Atpase Activity ◽  
Malignant Hyperthermia Susceptible ◽  
Myosin Isozyme

Background Anesthetic-induced malignant hyperthermia (MH) in humans and pigs is associated with dramatic alterations in cardiac function. However, it remains controversial as to whether MH-associated cardiac symptoms represent a primary difference of myocardium or a secondary alteration consequent to increases in the hyperthermic stress. Here the authors describe changes in myosin isoform expression in the hearts of MH-susceptible pigs with and without prior exposure to halothane. Methods One group of pigs was diagnosed as MH susceptible by halothane challenge and Hal-1843 nucleotide examination. To determine if there is an effect of halothane exposure, another group of pigs was diagnosed by simple MH genotyping without exposure to halothane. After diagnosis and genotyping, animals with and without exposure to halothane were killed to study cardiac myosin isozyme distributions, cardiac myofibrillar adenosine triphosphatase (ATPase) activity, and the steepness of the Ca2+-ATPase activity relation in the hearts of normal and susceptible pigs. The altered myosin isozyme expression was analyzed by pyrophosphate gel electrophoresis. Results Malignant hyperthermia-susceptible animals with the prior halothane challenge showed an increased V1 myosin (-44%) expression, increased myofibrillar ATPase activity (-25%) and increased steepness of the Ca2+-ATPase activity relation. Without exposure to halothane, no change of myofibrillar ATPase activity was found in the hearts of different genotyped pigs, but there was a small increase in expression of V1 myosin (-5%) in the mutant (TT). Conclusions The potential modulation of V1 myosin expression occurs in the hearts of MH-susceptible pigs. The added stress by halothane challenge would further cause a V3 --&gt; V1 shift, which may be attributed to the long-term effects of hyperthermic stress.

Effects of exercise on cardiac myosin isozyme composition during the aging process

1988 ◽  
Vol 64 (2) ◽  
pp. 880-883 ◽  
Author(s):  
R. P. Farrar ◽  
J. W. Starnes ◽  
G. D. Cartee ◽  
P. Y. Oh ◽  
H. L. Sweeney
Keyword(s):  
Atpase Activity ◽  
Exercise Program ◽  
Cardiac Performance ◽  
Fischer 344 Rats ◽  
Cardiac Myosin ◽  
Equal Distribution ◽  
Fischer 344 ◽  
Age Related ◽  
Myosin Isozyme ◽  
Effects Of Aging

The effects of aging and exercise on isoforms of cardiac myosin and Ca2+-activated actomyosin adenosinetriphosphatase (ATPase) activity were examined in Fischer 344 rats. Rats were divided into running (R) and age-matched sedentary (S) groups. The groups initiated their exercise program at either 3, 4, or 18 mo of age. Rats were killed at 10, 12, 24, or 27 mo of age. ATPase activity decreased 25% in the S group and 28% in the R group from 12 to 27 mo of age. The myosin isozyme patterns shifted in both S and R groups from a predominantly V1 isozyme form (63.8%) at 10 mo of age to a more equal distribution of isozyme forms at 24 mo (V1, V2, and V3 comprising 40.0, 27.8, and 31.9%, respectively). Age-related shifts in myosin composition occurred despite chronic endurance training at an intensity of approximately 75% maximum O2 consumption. Improvement of cardiac performance through training during aging is not accompanied by attenuating shifts in myosin isozyme composition.

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