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Regulation of glycogen synthase activity in muscle by a carboxyl terminal part sequence of human growth hormone


, : Regulation of glycogen synthase activity in muscle by a carboxyl terminal part sequence of human growth hormone. Archives of Biochemistry & Biophysics 224(1): 365-371

The synthetic peptide hGH [human growth hormone] 177-191, corresponding to the last 15 residues at the carboxyl terminus of pituitary growth hGH, promotes the conversion of glycogen synthase a to glycogen b in muscle. When injected, the peptide produced inactivation of glycogen synthase phosphatase activity in rat skeletal muscle. The time course of phosphatase inactivation was closely correlated with that for glycogen synthase. The peptide had no effect either on muscle 3',5'-cAMP levels or on synthase kinase activity. These results can be explained in terms of a dynamic cycle of interconversion of synthase between active and inactive forms, by the simultaneous action of synthase kinases and synthase phosphatases. A decrease in the ratio of phosphatase to kinase activity would result in a decrease in the steady-state level of synthase a activity.

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