Protein synthesis and degradation in skeletal muscle of normal and dystrophic hamsters.

Dystrophic hamsters (BIO 53.58) had lower body weights and gastrocnemius muscle weights than normal hamsters (BIO RB). Dystrophic muscle contained less protein than normal muscle. The proportion of collagenous to noncollagenous protein remained unchanged. Loss of protein in the dystrophic muscle was the result of an increase in the rate of protein degradation. This was accompanied by higher activities of two lysosomal proteases, cathepsins B and D. The net effect of the increase in protein degradation was blunted by an increase in the rate of synthesis of total protein and myosin. The faster rate of synthesis in dystrophic muscle was partially due to an increase in the concentration of cellular RNA. Rates of peptide-chain initiation and protein synthesis decreased in muscles of normal hamsters perfused in the absence of insulin. In the presence of insulin, these processes were maintained at higher rates. However, the rate of protein synthesis in dystrophic muscle appeared less insulin-dependent than normal muscle. Protein degradation was inhibited by insulin in both types of muscle.