Vitronectin
Title: Vitronectin
Additional Names: Serum spreading factor; S-protein
Literature References: Multifunctional adhesive glycoprotein found in serum and in various tissues. Has binding sites for integrins, collagen, heparin, complement components, and perforin, q.q.v. Thought to play a regulatory role in hemostasis, wound healing, tissue remodeling and cancer. Synthesized by hepatocytes as a single chain polypeptide, mol wt ~78 kDa. Binds readily to proteoglycans of the extracellular matrix and is deposited in normal loose connective tissues, in dermal elastin fibers, and in the vascular wall. Also synthesized by platelets, macrophages and megakaryocytes. Released by activated platelets in different multimeric forms. Promotes cellular attachment, spreading and migration of a wide variety of cell types and serves as a matrix-associated regulator of blood coagulation. Identification: R. Holmes, J. Cell Biol. 32, 297 (1967). Isoln and comparison with fibronectin, q.v.: D. Barnes et al., J. Supramol. Struct. 14, 47 (1980). Purification and tissue distribution: E. G. Hayman et al., Proc. Natl. Acad. Sci. USA 80, 4003 (1983). Amino acid sequence: S. Suzuki et al., EMBO J. 4, 2519 (1985). Identity with S-protein: K. T. Preissner et al., Biochem. Biophys. Res. Commun. 134, 951 (1986); B. R. Tomasini, D. F. Mosher, Blood 68, 737 (1986). Review of structure and biological function in hemostasis: K. T. Preissner, Annu. Rev. Cell Biol. 7, 275-310 (1991); K. T. Preissner, D. Jenne, Thromb. Haemostasis 66, 123-132; 189-194 (1991). Review of vitronectin receptors and role in cell growth and differentiation: B. Felding-Habermann, D. A. Cheresh, Curr. Opin. Cell Biol. 5, 864-868 (1993).

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