cAMP regulation of myosin ATPase activity in the maturing rat heart.

Abstract

Calcium-activated myosin adenosine triphosphatase (ATPase) activity has been measured in sections of rat ventricles that were rapidly frozen to preserve the structure and regulatory state of myosin occurring in vivo. These results were related to myosin isozyme composition measured in ventricles by native gel electrophoresis and by quantitative immunocytochemistry. Both total ATPase activity and percent alpha-heavy chain rapidly rise during the first month following birth. However, ATPase activity remains constant at a high level from 1 to 12 months following birth, even though percent alpha-heavy chain declines during this period. The ATPase activity of V1 myosin was specifically determined using sections in which V3 myosin had been completely inhibited by exposure to alkaline pH in the absence of adenosine 5'-triphosphate (ATP). Relative V1 specific activity, taken as the ratio of V1 ATPase activity to percent alpha-heavy chain, doubles in the first 2.0 months after birth and then remains approximately constant at this higher level until at least 4 months after birth. The specific activity of V1 can be further increased by the addition of adenosine-3',5'-cyclic monophosphate (cAMP). This effect of cAMP is age dependent, increasing threefold between 1 and 2 months following birth and then declining as V1 is replaced by V3.