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dc.contributor.authorEllery, Paul
dc.contributor.authorAdams, M.
dc.date.accessioned2017-01-30T10:53:34Z
dc.date.available2017-01-30T10:53:34Z
dc.date.created2015-10-29T04:10:08Z
dc.date.issued2014
dc.identifier.citationEllery, P. and Adams, M. 2014. Tissue Factor Pathway Inhibitor: Then and Now. Seminars in Thrombosis and Hemostasis. 40 (8): pp. 881-886.
dc.identifier.urihttp://hdl.handle.net/20.500.11937/6509
dc.identifier.doi10.1055/s-0034-1395153
dc.description.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.

dc.publisherThieme Medical Publishers, Inc.
dc.titleTissue Factor Pathway Inhibitor: Then and Now
dc.typeJournal Article
dcterms.source.volume40
dcterms.source.number8
dcterms.source.startPage881
dcterms.source.endPage886
dcterms.source.issn0094-6176
dcterms.source.titleSeminars in Thrombosis and Hemostasis
curtin.departmentSchool of Biomedical Sciences
curtin.accessStatusFulltext not available


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