Regulation of glycogen synthase kinase 3 in human platelets: a possible role in platelet function?
Barry, F. A., Graham, G. J., Fry, M. J. and Gibbins, J. M. (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
Full text not archived in this repository.
To link to this article DOI: 10.1016/s0014-5793(03)01015-9
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.