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Protein C inhibitor (PCI) is a member of the serine protease inhibitor (serpin) family. PCI was initially found to be an inhibitor of activated protein C, and later shown to be a potent inhibitor of blood coagulation and fibrinolysis such as that mediated by urokinase type-plasminogen activator. Therefore, the protein came to be known as plasminogen activator inhibitor-3. It also inhibits proteases involved in fertilization. PCI is broadly conserved, and is found in human, rhesus monkey, cow, rabbit, rat, mouse and chicken. The human PCI gene is located on chromosome 14q32.1 in a cluster of genes encoding related serpins. Sp1- and AP2-binding sites in the 5′-flanking region act as promoter and enhancer, respectively, for its expression in the liver. PCI mRNA is expressed in many organs in primates, but only in the reproductive organs in rodents. Recent studies using transgenic mice expressing the human gene have suggested that PCI is also involved in regulation of lung remodeling, tissue regeneration, vascular permeability, proteolysis in the kidney and tumor cell invasion. A protease inhibitor-independent activity of PCI, the prevention of anti-angiogenesis and metastasis of tumor cells, has also been observed. Thus, PCI is a unique multi-functional serpin playing diverse roles in the thrombosis and hemostasis in multiple organs and tissues of a variety of species.