Thromb Haemost 2005; 94(06): 1122-1130
DOI: 10.1160/TH05-07-0509
Review Article
Schattauer GmbH

Structure, function and biology of tissue factor pathway inhibitor-2

Hitendra S. Chand
1   Department of Pathology, University of New Mexico Health Sciences Center, Albuquerque, New Mexico, and
,
Donald C. Foster
2   Zymo Genetics, Inc., Seattle, Washington, USA
,
Walter Kisiel
1   Department of Pathology, University of New Mexico Health Sciences Center, Albuquerque, New Mexico, and
› Author Affiliations
Further Information

Publication History

Received 02 July 2005

Accepted after revision 04 October 2005

Publication Date:
07 December 2017 (online)

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Summary

Tissue factor pathway inhibitor-2 (TFPI-2) is a 32 kDa matrix-associated Kunitz-type serine proteinase inhibitor consisting of a short amino-terminal region, three tandem Kunitz-type domains and a positively charged carboxy-terminal tail. Human TFPI-2, previously designated as placental protein 5, inhibits a broad spectrum of serine proteinases almost exclusively through its first Kunitz-type domain, and is thought to play an important role in the regulation of extracellular matrix digestion and re-modeling. In this context, reduced synthesis of TFPI-2 has been related to numerous pathophysiological processes such as inflammation, angiogenesis, atherosclerosis, retinal degeneration and tumor growth/metastasis. In this review, we document current information regarding the expression of TFPI-2 by various tissues, its inhibitory activity and proteinase specificity in-vitro, and discuss possible physiological roles for this inhibitor based on in-vivo studies.

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