Protease-activated receptor 3 is a second thrombin receptor in humans

Hiroaki Ishihara, Andrew J. Connolly, Dewan Zeng, Mark L. Kahn, Yao Wu Zheng, Courtney Timmons, Tracy Tram and Shaun R. Coughlin
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Hiroaki Ishihara: University of California, San Francisco
Andrew J. Connolly: University of California, San Francisco
Dewan Zeng: University of California, San Francisco
Mark L. Kahn: University of California, San Francisco
Yao Wu Zheng: University of California, San Francisco
Courtney Timmons: University of California, San Francisco
Tracy Tram: University of California, San Francisco
Shaun R. Coughlin: University of California, San Francisco

Nature, 1997, vol. 386, issue 6624, 502-506

Abstract: Abstract Thrombin is a coagulation protease that activates platelets, leukocytes, endothelial and mesenchymal cells at sites of vascular injury, acting partly through an unusual proteolytically activated G-protein-coupled receptor1–3. Knockout of the gene encoding this receptor provided definitive evidence for a second thrombin receptor in mouse platelets and for tissue-specific roles for different thrombin receptors4. We now report the cloning and characterization of a new human thrombin receptor, designated protease-activated receptor 3 (PAR3). PAR3 can mediate throm-bin-triggered phosphoinositide hydrolysis and is expressed in a variety of tissues, including human bone marrow and mouse megakaryocytes, making it a candidate for the sought-after second platelet thrombin receptor. PAR3 provides a new tool for understanding thrombin signalling and a possible target for therapeutics designed selectively to block thrombotic, inflammatory and proliferative responses to thrombin.

Date: 1997
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DOI: 10.1038/386502a0

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