Collagen stimulates tyrosine phosphorylation of phospholipase C‐γ2 but not phospholipase C‐γ1 in human platelets

Abstract

Collagen is an important primary stimulus of platelets during the process of hemostasis. As with many other platelet stimuli, collagen signal transduction involves the hydrolysis of inositol phospholipids; however, the mechanism which underlies this event is not well understood. Neither the collagen receptor nor the isoform of phospholipase C that is activated have been identified. We report that collagen-activation of platelets induces tyrosine phosphorylation of phospholipase C-γ2 but not phospholipase C-γ1. We also show that the platelet low affinity Fc receptor (FcγRII), which mediates activation of platelets by immune complexes, and wheat germ agglutinin, which binds non-specifically to glycoprotein, stimulate phospholipase C-γ2 tyrosine phosphorylation. In contrast, we could not detect phospholipase C-γ2 tyrosine phosphorylation in platelets stimulated by either thrombin or a stable thromboxane A₂ analogue, U46619.