PMID: 2510600Nov 15, 1989Paper

Glycogen synthase turnover and phosphorylation in rat H4IIE hepatoma cells

Archives of Biochemistry and Biophysics
D J Armstrong, P J Roach

Abstract

Glycogen synthase was isolated from rat H4IIE hepatoma cells by the use of specific antibodies. Immunoprecipitates from cells grown in the presence of [35S]methionine contained two 35S-labeled polypeptides, designated GS1 and GS2, separable by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Labeling of both species was half-maximal after 3 h and remained constant up to 48 h. When cells were incubated with [32P]-phosphate, 32P was incorporated into both species with similar kinetics, half-maximal labeling occurring after 2-3 h. The steady-state ratio 32P/35S was significantly higher for the lower mobility GS2 polypeptide. Pulse-chase experiments showed that the two subunits followed similar kinetics with respect to 35S-labeling. However, the turnover of 32P on the GS2 subunit was significantly faster (t1/2 approximately 30 min) than that on the GS1 subunit (t1/2 approximately 2 h). We suggest that the two polypeptides represent different phosphorylation states of the glycogen synthase subunit and are rapidly interconverted.

References

Feb 1, 1979·Biochimica Et Biophysica Acta·A W Tan
Sep 19, 1986·Biochimica Et Biophysica Acta·Y WangP J Roach
Sep 1, 1986·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·W J Whelan
Dec 15, 1987·European Journal of Biochemistry·J PitcherP Cohen

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