Activation of protein-tyrosine kinase Syk in human platelets stimulated with lysophosphatidic acid or sphingosine 1-phosphate

Biochemical and Biophysical Research Communications
L YangS Kume

Abstract

It has been reported that not only lysophosphatidic acid (LPA) but also its sphingolipid counterpart, sphingosine 1-phosphate (Sph-1-P), induce platelet functional responses. We report here Syk activation in human platelets stimulated with these lysophospholipids. LPA rapidly induced platelet protein-tyrosine phosphorylation, including that of Syk, and Syk activation, assessed by immunoprecipitation kinase assay. Sph-1-P, although rather weaker, mimicked LPA in inducing these tyrosine kinase-related events. Pretreatment of platelets with staurosporine, a potent protein kinase inhibitor, diminished LPA-induced Syk phosphorylation and activation, but not intracellular Ca2+ mobilization. These results demonstrate that, in platelets, the bioactive lysophospholipids induce Syk activation, which, however, may not be related to Ca2+ mobilization.

Citations

Jul 6, 2000·The Biochemical Journal·S Pyne, N J Pyne
Jun 24, 2008·Endothelium : Journal of Endothelial Cell Research·Vidya Limaye
Dec 31, 1997·FEBS Letters·Y YatomiY Igarashi
Nov 22, 2001·Circulation Research·T LevadeR Salvayre
Aug 1, 2006·Pathophysiology of Haemostasis and Thrombosis·Suzanne J A Korporaal, Jan-Willem N Akkerman
May 9, 2000·The Journal of Immunology : Official Journal of the American Association of Immunologists·E E PrieschlT Baumruker

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