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SUMMARY
Changes in the concentrations of free amino acids in intracellular fluids and blood plasma were measured in rats treated with cortisol. Increasing age raised the concentrations of free amino acids in plasma, while in liver, with the exception of glycine and alanine, decreased concentrations were observed. Cortisol treatment reduced free amino acid levels in plasma and liver which suggested a progressive catabolism of body proteins and increased protein synthesis in the liver. In skeletal muscle of control rats the free amino acid concentrations increased during the experimental period. Cortisol increased the concentration of certain amino acids and decreased that of others due to an increased protein turnover in muscle.
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SUMMARY
Although cortisol slightly inhibited the incorporation of 2-14C]glycine into the proteins of rat skin samples incubated in vitro, addition of the hormone to the storage medium had a marked protective effect on protein and DNA metabolism. The incorporation of [2-14C]glycine into the proteins, and to a lesser degree that of [6-3H]thymidine into DNA, were stimulated when the incubated skin had been exposed to cortisol during storage. The skin samples stored in buffer containing cortisol transported α-aminoisobutyric acid more effectively; this was concluded to be due to a stabilizing effect of cortisol on the cell membrane. During storage protein catabolism and possibly protein turnover were stimulated by cortisol.
