The pathways of protein synthesis and degradation in normal heart and during development and regression of cardiac hypertrophy
Sims, J.M.; Patzer, B.; Kumudavalli-Reddy, M.; Martin, A.F.; Rabinowitz, M.; Zak, R.
Recent Advances in Studies on Cardiac Structure and Metabolism 12: 19-28
1976
ISSN/ISBN: 0363-5872 PMID: 145638 Document Number: 102755
The half-life of cardiac myosin heavy chains (HC) was determined, with leucyl-tRNA as precursor, to be 5.4 days. Myosin HC are labeled more rapidly than actin; myosin light chains (LC1 and LC2) are labeled more slowly than HC. The observed differences are attributable to heterogeneity in the half-lives, e.g., actin, and to the effect of dilution by the existing macromolecular precursor pool (LC1 and LC2). Cardiac and skeletal muscle contain a population of filaments that can be released from myofibrils by ATP-relaxing solution. The easily released filaments (ERF) are devoid of alpha-actinin and M-protein. Labeling of ERF is more rapid than that of residual myofibrils. Cardiac and skeletal muscle contains calcium-activated neutral protease, which selectively removes alpha-actinin when incubated with isolated myofibrils. During development of pressure-induced cardiac hypertrophy, the labeling of LC2 is increased. In regressing cardiac hypertrophy the activities of free and total cathepsin D and of acidic RNase are unaltered.