Protein synthesis and degradation in biopsies of rat skeletal muscle.

The use of 20- to 40-mg biopsies of rat skeletal muscle to measure protein synthesis and degradation rates in vitro was investigated and compared to that of the intact extensor digitorum longus (EDL) and soleus muscles. During incubations in oxygenated Krebs-Ringer bicarbonate buffer with glucose, insulin, 23 amino acids at 10 times rat plasma levels, and [14C]tyrosine, the specific activity of intracellular tyrosine approximated that of the incubation medium and was constant in the biopsy, the EDL, and the soleus. The rate of incorporation of tyrosine into the protein of the biopsy was constant for 3 hr and was 39 and 32% of the rates of the EDL and soleus, respectively. The rate of release of tyrosine from protein in the biopsy during incubations in buffer with glucose and cycloheximide was constant for 3 hr and was intermediate between the rates of the EDL and soleus. The effects of starvation on the in vitro protein metabolism of the biopsy were the same as on the intact muscles. The 42% decrease in synthesis and the 53% increase in degradation in the biopsy were intermediate between the changes measured in the EDL and soleus muscles. The ability of this technique to identify proportional changes in the in vitro protein synthesis and degradation rates makes this a valid technique suitable for the measurement of changes of in vitro protein metabolism using serial biopsies from larger animals, including man.