The adaptive changes in the isoenzyme pattern of myosin from hypertrophied rat myocardium as a result of pressure overload and physical training.

The distribution of cardiac myosin isoenzymes is altered as a result of pressure overload and physical training. Using polyacrylamide gel electrophoresis in sodium pyrophosphate, it was found that myosin from left ventricles of adult rats exists in three polymorphic forms, V1, V2 and V3. Cardiac hypertrophy due to renal hypertension (Goldblatt II) led to a shift of the isoenzymes towards V3, whereas swimming training resulted in an opposite redistribution. The isoenzyme V1 predominated, only traces of V2 and V3 were detectable. The changes in the isoenzyme distribution were reflected in an altered ATPase activity of myofibrils. In a representative sample of the Goldblatt rats, the activity was reduced by 11%, and the swimming training led to an increase by 10%. Changes in myofibrillar ATPase can, therefore, be traced to alterations in the isoenzyme pattern of myosin. The polymorphism of myosin has a two-faced aspect as regards cardiac performance. For example, a shift towards V3 is expected to increase the economy for tension development during isovolumetric contraction at the expense of a reduced maximum speed of ventricular contraction.