Protein synthesis versus energy state in contracting muscles of perfused rat hindlimb

A. C. Bylund-Fellenius, K. M. Ojamaa, K. E. Flaim, J. B. Li, S. J. Wassner and L. S. Jefferson The goal of these studies was to evaluate acute changes in protein metabolism in skeletal muscle in response to contractile activity. Rates of protein synthesis were measured by following L-[U-14C]phenylalanine incorporation into protein in muscles of the perfused rat hindlimb at rest, during 10 min of maximal isometric muscle contractions, and during 10 min of recovery. Synthesis measurements were carried out under conditions that ensured that the specific radioactivity of the tRNA-bound precursor amino acid was equal to that of extracellular phenylalanine. Protein degradation was estimated by measuring the release of Nt-methylhistidine. Rates of synthesis were markedly inhibited in response to muscle contractions in tibialis anterior, gastrocnemius, and plantaris but were unaffected in soleus. Rates of synthesis returned toward those observed in the resting condition during the recovery period. Rates of degradation were also markedly inhibited in response to muscle contractions. Decreased rates of synthesis correlated with reduced tissue contents of ATP and creatine phosphate, a reduced ATP/ADP, and an elevated tissue content of lactate. The results demonstrate that isometric contractions in muscles consisting of a high proportion of fast glycolytic fibers result in a marked depression in rates of protein synthesis that may be due to an altered energy state.