【 摘 要 】
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.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
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RO201912020300188ZK.pdf | 521KB | download |