PMID: 8944416Jan 1, 1996Paper

Serine/threonine dephosphorylation may be involved in tyrosine phosphorylation: a new mode of signal transduction in platelets

Seminars in Thrombosis and Hemostasis
V ArtçanuthurryS Lévy-Toledano

Abstract

Platelet signal transduction involves not only reversible phosphorylation of proteins on both tyrosine and serine/threonine residues, but also mechanisms of cross-talk to coordinate different pathways. We have, therefore, investigated the effect of okadaic acid, a potent inhibitor of serine/threonine protein phosphatases type 1 and type 2A (PP1 and PP2A), to better understand the interplay that must exist between serine/threonine and tyrosine phosphorylations during platelet activation. Okadaic acid drastically inhibits thrombin-induced platelet aggregation, secretion, and thromboxane synthesis. The inhibition is accompanied by a marked increase in the phosphorylation of at least 5 proteins (230, 210, 74, 57, and 50 to 52 kDa). However, protein kinase C activity is not modified because thrombin-and phorbol-12-myristate-13-acetate-induced phosphorylation of pleckstrin is still occurring, although slightly decreased. Inhibition of platelet function and extent of the phosphorylation of the 5 substrates in the presence of okadaic acid are concentration and time dependent, suggesting a relation between the accumulation of one or more phosphoproteins and the inhibitory effect of okadaic acid. Okadaic acid inhibits thrombin-induced ty...Continue Reading

Citations

Jan 7, 2000·The Journal of Immunology : Official Journal of the American Association of Immunologists·E Rollet-LabelleP H Naccache
Dec 15, 2020·Biochimica Et Biophysica Acta. Molecular Cell Research·Alessandra V S FariaGwenny M Fuhler

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