Crossref journal-article
Wiley
FEBS Letters (311)
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.

Bibliography

Blake, R. A., Schieven, G. L., & Watson, S. P. (1994). Collagen stimulates tyrosine phosphorylation of phospholipase C‐γ2 but not phospholipase C‐γ1 in human platelets. FEBS Letters, 353(2), 212–216. Portico.

Dates
Type When
Created 23 years, 1 month ago (July 25, 2002, 5:12 a.m.)
Deposited 1 year, 11 months ago (Sept. 16, 2023, 9:45 a.m.)
Indexed 1 year, 3 months ago (May 6, 2024, 5:25 p.m.)
Issued 30 years, 10 months ago (Oct. 17, 1994)
Published 30 years, 10 months ago (Oct. 17, 1994)
Published Online 23 years, 10 months ago (Oct. 19, 2001)
Published Print 30 years, 10 months ago (Oct. 17, 1994)
Funders 0

None

@article{Blake_1994, title={Collagen stimulates tyrosine phosphorylation of phospholipase C‐γ2 but not phospholipase C‐γ1 in human platelets}, volume={353}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/0014-5793(94)01037-4}, DOI={10.1016/0014-5793(94)01037-4}, number={2}, journal={FEBS Letters}, publisher={Wiley}, author={Blake, Robert A. and Schieven, Gary L. and Watson, Steve P.}, year={1994}, month=oct, pages={212–216} }