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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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Related references

Macaulay, S.L.; Armstrong, J.M.; Bornstein, J., 1983: Regulation of glycogen synthase activity in muscle by a C-terminal part sequence of human growth hormone. The synthetic peptide hGH 177-191, corresponding to the last 15 residues at the carboxyl terminus of human pituitary growth hormone, promotes the conversion of glycogen synthase a to glycogen synthase b in muscle. When injected, the peptide was fo...

Bornstein, J.; Ng, F.M.; Heng, D.; Wong, K.P., 1983: Metabolic actions of pituitary growth hormone. I. Inhibition of acetyl CoA carboxylase by human growth hormone and a carboxyl terminal part sequence acting through a second messenger. Evidence is presented showing that human growth hormone (hGH) and its part sequence hGH 172-191 inhibit acetyl CoA carboxylase and hence fatty acid synthesis by interacting with adipocyte and hepatocyte plasma membranes, resulting in the release o...

Bornstein, J.; Ng, F.M.; Heng, D.; Wong, K.P., 1983: Metabolic actions of pituitary growth hormone 1. inhibition of acetyl coenzyme a carboxylase by human growth hormone and a carboxyl terminal part sequence acting through a second messenger. Evidence is presented showing that human growth hormone (hGH) and its part sequence hGH 172-191 inhibit acetyl CoA carboxylase, and hence fatty acid synthesis by interacting with adipocyte and hepatocyte plasma membranes, resulting in the release...

Anonymous, 2013: Akt2 influences glycogen synthase activity in human skeletal muscle through regulation of NH2-terminal sites 2 + 2a phosphorylation. Type 2 diabetes is characterized by reduced muscle glycogen synthesis. The key enzyme in this process, glycogen synthase (GS), is activated via proximal insulin signaling, but the exact molecular events remain unknown. Previously, we demonstrated...

Friedrichsen, M.; Birk, J.B.; Richter, E.A.; Ribel-Madsen, R.; Pehmøller, C.; Hansen, B.Falck.; Beck-Nielsen, H.; Hirshman, M.F.; Goodyear, L.J.; Vaag, A.; Poulsen, P.; Wojtaszewski, Jørgen.F.P., 2013: Akt2 influences glycogen synthase activity in human skeletal muscle through regulation of NH₂-terminal (sites 2 + 2a) phosphorylation. Type 2 diabetes is characterized by reduced muscle glycogen synthesis. The key enzyme in this process, glycogen synthase (GS), is activated via proximal insulin signaling, but the exact molecular events remain unknown. We previously demonstrated t...

Anonymous, 2013: Akt2 influences glycogen synthase activity in human skeletal muscle through regulation of NH2-terminal sites 2+2a phosphorylation. Type 2 diabetes is characterized by reduced muscle glycogen synthesis. The key enzyme in this process, glycogen synthase (GS), is activated via proximal insulin signaling, but the exact molecular events remain unknown. We previously demonstrated t...

Wade J.D.; N.F.M.; Bornstein J., 1978: The solid phase synthesis and biological activity of the carboxyl terminal 177 191 sequence of human growth hormone. Proceedings of the Australian Biochemical Society (11): 16

Bak J.F.; Moller N.; Schmidt O., 1990: Effects of growth hormone on insulin receptor and glycogen synthase activity in human muscle. Diabetologia 33(SUPPL): A29

Vardanis, A.; Hudson, A.J., 1991: Regulation of glycogen synthesis in human skeletal muscle: does cellular glycogen control glycogen synthase phosphatase activity?. Contrary to the accepted feedback control mechanism of glycogen biosynthesis in skeletal muscle, evidence is presented here leading to the conclusion that glycogen does not control the activity of glycogen synthase phosphatase in intact human skel...

Rylatt, D.B.; Aitken, A.; Bilham, T.; Condon, G.D.; Embi, N.; Cohen, P., 1980: Glycogen synthase from rabbit skeletal muscle. Amino acid sequence at the sites phosphorylated by glycogen synthase kinase-3, and extension of the N-terminal sequence containing the site phosphorylated by phosphorylase kinase. Glycogen synthase kinase-3 phosphorylates three serine residues on glycogen synthase (sites 3a, 3b and 3c) which are all located in the same nine-amino-acid segment of the polypeptide chain. The sequence in this region is: Arg-Tyr-Pro-Arg-Pro-Ala-...