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

Author

Listed:
  • Hiroaki Ishihara

    (University of California, San Francisco)

  • Andrew J. Connolly

    (University of California, San Francisco
    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
    University of California, San Francisco)

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.

Suggested Citation

  • Hiroaki Ishihara & Andrew J. Connolly & Dewan Zeng & Mark L. Kahn & Yao Wu Zheng & Courtney Timmons & Tracy Tram & Shaun R. Coughlin, 1997. "Protease-activated receptor 3 is a second thrombin receptor in humans," Nature, Nature, vol. 386(6624), pages 502-506, April.
    • Handle: RePEc:nat:nature:v:386:y:1997:i:6624:d:10.1038_386502a0
    DOI: 10.1038/386502a0
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