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Updated: Aug 30, 2026

Preparation of Washed Human Platelets for Quantitative Metabolic Flux Studies
Published on: January 10, 2025
Regulation of glycogen synthase kinase 3 in human platelets: a possible role in platelet function?
Fiona A Barry1, Gwenda J Graham, Michael J Fry
1School of Animal and Microbial Sciences, The University of Reading, Whiteknights, PO Box 228 RG6 6AJ, Reading, UK.
Abstract:
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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