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    Tissue Factor Pathway Inhibitor: Then and Now

    Access Status
    Fulltext not available
    Authors
    Ellery, Paul
    Adams, M.
    Date
    2014
    Type
    Journal Article
    
    Metadata
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    Citation
    Ellery, P. and Adams, M. 2014. Tissue Factor Pathway Inhibitor: Then and Now. Seminars in Thrombosis and Hemostasis. 40 (8): pp. 881-886.
    Source Title
    Seminars in Thrombosis and Hemostasis
    DOI
    10.1055/s-0034-1395153
    ISSN
    0094-6176
    School
    School of Biomedical Sciences
    URI
    http://hdl.handle.net/20.500.11937/6509
    Collection
    • Curtin Research Publications
    Abstract

    Tissue factor pathway inhibitor (TFPI) is the major physiological regulator of tissue factor (TF)-induced blood coagulation. TFPI inhibits the TF-activated factor VII (FVIIa) complex in an activated factor X (FXa)-dependent manner, helping to control thrombin generation and ultimately fibrin formation. The importance of TFPI is demonstrated in models of hemophilia where lower levels of FVIII or FIX are insufficient to overcome its inhibitory effect, resulting in a bleeding phenotype. There are two major isoforms in vivo; TFPI contains three Kunitz-type inhibitory domains (designated K1, K2, and K3), is secreted by endothelial cells and requires protein S to enhance its anticoagulant activity. In contrast, TFPIß contains only the K1 and K2 domains, but it is attached to the endothelial surface via a glycosylphosphatidylinositol anchor. This review will initially provide a brief history of the major discoveries related to TFPI, and then discuss new insights into the physiology of TFPI, including updates on its association with protein S and FV, as well as the current understanding of its association with disease.

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