Summary

Tissue factor pathway inhibitor-2 (TFPI-2) is a 32 kDa matrix-associatedKunitz-type serine proteinase inhibitor consisting of ashort amino-terminal region,three tandem Kunitz-type domainsand a positively charged carboxy-terminal tail. Human TFPI-2,previously designated as placental protein 5, inhibits a broadspectrum of serine proteinases almost exclusively through itsfirst Kunitz-type domain, and is thought to play an importantrole in the regulation of extracellular matrix digestion and remodeling. In this context, reduced synthesis of TFPI-2 has beenrelated to numerous pathophysiological processes such as inflammation,angiogenesis, atherosclerosis, retinal degenerationand tumor growth/metastasis. In this review, we document currentinformation regarding the expression of TFPI-2 by varioustissues, its inhibitory activity and proteinase specificity in-vitro,and discuss possible physiological roles for this inhibitor basedon in-vivo studies