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(Circulation Research. 1996;79:222-226.)
© 1996 American Heart Association, Inc.

Articles

Maximal Actomyosin ATPase Activity and In Vitro Myosin Motility Are Unaltered in Human Mitral Regurgitation Heart Failure

The-Tin T. Nguyen, Eric Hayes, Louis A. Mulieri, Bruce J. Leavitt, Henk E.D.J. ter Keurs, Norman R. Alpert, David M. Warshaw

the Department of Medicine and Medical Physiology (T.-T.T.N., H.E.D.J. ter K.), University of Calgary (Canada), and the Department of Molecular Physiology and Biophysics (E.H., L.A.M., N.R.A., D.M.W.) and the Department of Medicine (B.J.L.), College of Medicine, University of Vermont, Burlington.

Myofibrillar but not actomyosin ATPase is depressed in failing myocardium from patients with dilated cardiomyopathy. Since there is a similar depression of myofibrillar ATPase in mitral regurgitation myocardium, we investigated whether or not the hydrolytic and mechanical performances of myosin are altered by comparing the maximal actomyosin ATPase activity and the in vitro myosin motility of myocardial myosin from patients with mitral regurgitation heart failure with that of patients with normal ventricular function. The results show that there is no significant difference (P>.05) between nonfailing and failing values for either the maximal actomyosin ATPase activity (0.3 s^-1·head^-1) or the myosin motility (1 µm/s). These observations suggest that changes, other than in the myosin heavy chain, contribute to the altered myocardial performance in mitral regurgitation myocardium.

Key Words: actin filament • biopsy • cardiomyopathy • cardiac muscle • crossbridge

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