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Vitronectin (VTN), a member of the chymosin family, is abundant in serum, extracellular matrix and bone. It is a secreted protein that exists as a single chain or as a sandwich, double chain formed by disulfide bonds. VTN consists of three domains: an N-terminal somatomodulin B domain, a central domain with homology to heme, and a C-terminal domain. VTN promotes cell adhesion and spreading, inhibits membrane disruption of terminal cellular complement pathways, and binds to various serine protease inhibitors.