STUDIES ON PROTEIN SYNTHESIS AND AMINO ACID COMPARTMENTATION

用放射性标记法测定体内蛋白质合成速率

In vivo measurements of rates of protein synthesis with radiolabeled precursors are problematic because of uncertainties about the relative contribution of unlabeled amino acids derived from protein breakdown to the precursor pool for protein synthesis. The quantitative autoradiographic method for the determination of local rates of cerebral protein synthesis (lCPS) in vivo with a carboxyl-labeled, aliphatic, branched-chain amino acid as tracer takes into account recycling of the unlabeled species of the tracer amino acid. Rates of cerebral protein synthesis in rats have been shown to increase in regenerating nerve nuclei and decrease in most brain regions during postnatal brain development and with senescence. Cocaine treatment changes lCPS in selective brain regions; the direction of the changes depends on the history of treatment. Studies of normal sleep in monkeys indicate that slow wave sleep is linked with increased rates of lCPS in many brain regions. In hibernating ground squirrels, lCPS is profoundly and reversibly reduced throughout the brain. Light thiopental anesthesia in rats results in widespread but very small decreases in rates of cerebral protein synthesis. In general, changes in lCPS may mark brain regions undergoing long-term adjustments in response to a drug, a treatment, or a change in physiological state. Studies of recycling and lCPS under valine-flooding conditions demonstrate compartmentation of amino acids for protein synthesis. Even when plasma valine concentrations are increased 100 fold, protein degradation continues to supply a significant portion of valine for protein synthesis and an increased portion of leucine.