| Literature DB >> 14550568 |
Fiona A Barry1, Gwenda J Graham, Michael J Fry, Jonathan M Gibbins.
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.Entities:
Mesh:
Substances:
Year: 2003 PMID: 14550568 DOI: 10.1016/s0014-5793(03)01015-9
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124