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Regulation of glycogen synthase kinase 3 in human platelets: a possible role in platelet function?

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Barry, F. A., Graham, G. J., Fry, M. J. and Gibbins, J. M. ORCID: https://orcid.org/0000-0002-0372-5352 (2003) Regulation of glycogen synthase kinase 3 in human platelets: a possible role in platelet function? FEBS Letters, 553 (1-2). pp. 173-178. ISSN 0014-5793

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To link to this item DOI: 10.1016/s0014-5793(03)01015-9

Abstract/Summary

In this study we show that both glycogen synthase kinase 3 (GSK3) isoforms, GSK3alpha and GSK3beta, are present in human platelets and are phosphorylated on Ser(21) and Ser(9), respectively, in platelets stimulated with collagen, convulxin and thrombin. Phosphorylation of GSK3alpha/beta was dependent on phosphoinositide 3-kinase (PI3K) activity and independent of platelet aggregation, and correlated with a decrease in GSK3 activity that was preserved by pre-incubating platelets with PI3K inhibitor LY294002. Three structurally distinct GSK3 inhibitors, lithium, SB415286 and TDZD-8, were found to inhibit platelet aggregation. This implicates GSK3 as a potential regulator of platelet function. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Item Type:Article
Refereed:Yes
Divisions:Life Sciences > School of Biological Sciences
Interdisciplinary centres and themes > Institute for Cardiovascular and Metabolic Research (ICMR)
ID Code:10665
Uncontrolled Keywords:platelet, platelet activation, platelet aggregation, glycogen synthase, kinase 3, phosphoinositide 3-kinase, protein kinase B, RECEPTOR GAMMA-CHAIN, GLYCOPROTEIN-VI, COLLAGEN RECEPTOR, INTEGRIN, ALPHA(2)BETA(1), TYROSINE PHOSPHORYLATION, ALZHEIMERS-DISEASE, INTACT-CELLS, INHIBITORS, ACTIVATION, 3-KINASE
Publisher:Elsevier
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