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Phosphorylase regulates the association of glycogen synthase with a proteoglycogen substrate in hepatocytes

Lookup NU author(s): Dr Anna Tavridou, Professor Loranne Agius


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Changes in the glucosylation state of the glycogen primer, glycogenin, or its association with glycogen synthase are potential sites for regulation of glycogen synthesis. In this study we found no evidence for hormonal control of the glucosylation state of glycogenin in hepatocytes. However, using a modified glycogen synthase assay that separates the product into acid-soluble (glycogen) and acid-insoluble (proteoglycogen) fractions we found that insulin and glucagon increase and decrease, respectively, the association of glycogen synthase with an acid-insoluble substrate. The latter fraction had a higher affinity for UDP-glucose and accounted for between 5 and 21% of total activity depending on hormonal conditions. Phosphorylase overexpression mimicked the effect of glucagon. It is concluded that phosphorylase activation or overexpression causes dissociation of glycogen synthase from proteoglycogen causing inhibition of initiation of glycogen synthesis. © 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Publication metadata

Author(s): Tavridou A, Agius L

Publication type: Article

Publication status: Published

Journal: FEBS Letters

Year: 2003

Volume: 551

Issue: 1-3

Pages: 87-91

ISSN (print): 0014-5793

ISSN (electronic):

Publisher: Elsevier


DOI: 10.1016/S0014-5793(03)00902-5

PubMed id: 12965209


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