Regulation of protein synthesis and degradation during in vitro cardiac work.

Abstract

Cardiac work increased protein synthesis in hearts supplied glucose (mixture 1), glucose-insulin-glucagon-lactate-beta-hydroxybutyrate (mixture 2) or palmitate-beta-hydroxybutyrate-glucose (mixture 3). In hearts provided mixture 1, acceleration of synthesis involved increased rates of peptide chain initiation. In these hearts intracellular concentrations of 5 amino acids decreased and 13 others were unchanged, indicating that faster protein synthesis did not depend on increased amino acid availability. In hearts supplied mixtures 2, 3, or 4 (lactate-glucose-insulin), intracellular concentrations of branched-chain amino acids were decreased by work, whereas intracellular levels of some acidic and neutral amino acids increased. Protein degradation was decreased by work in hearts supplied mixtures 1 and 2, but not mixtures 3 and 4. In hearts provided mixture 1, nitrogen balance was negative, but less so in working preparations. Nitrogen balance was zero or positive in working hearts provided mixtures 2 and 4. These studies indicated that in hearts supplied some, but not all, of the substrate mixtures, cardiac work maintained efficiently of protein synthesis and inhibited protein degradation. An improved method for perfusion of working hearts with albumin-containing buffer is described.