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FEBS Lett. 2003 Oct 9;553(1-2):173-8.

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

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School of Animal and Microbial Sciences, The University of Reading, Whiteknights, PO Box 228 RG6 6AJ, Reading, UK.


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.

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