期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 425, 期 2, 页码 242-248出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2004.03.003
关键词
glucose uptake; glycogen synthesis; phosphorylase; lactate; fibroblasts
The effects of glucose starvation on glycogen synthase (GS) activity and protein expression were investigated. Fibroblasts were cultured in medium supplemented with either glucose or pyruvate. Pyruvate-cultured cells exhibited UDP-glucose contents that amounted to similar to10% of those in cells cultured with glucose. GS activity, protein and mRNA amounts in pyruvate-cultured cells were decreased to similar to35, 60, and 60%, respectively, of values in glucose-cultured cells. Incubation of extracts from glucose-cultured cells with radioactive UDP-glucose resulted in substantial binding of ligand to inummoprecipitated GS. However, binding in immunoprecipitates from pyruvate-cultured cells was decreased to similar to25% of values in glucose-cultured cells. These data indicate that glucose starvation and the subsequent depletion of UDP-glucose result in: (1) inactivation of GS, owing to a decrease in its ability to bind UDP-glucose, and (2) decreased amount of GS protein, owing to a decrease in the levels of GS mRNA. (C) 2004 Elsevier Inc. All rights reserved.
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