Vitronectin is a multi-functional 75 kDa glycoprotein that is found in the circulation where it contributes to hemostasis by regulating blood coagulation and fibrinolysis ; it forms a major component of the extracellular matrix where it plays major roles in cell adhesion, pericellular proteolysis, angiogenesis, tissue invasion and metastasis.
Vitronectin binds to a number of ligands including integrin receptors, heparin, plasminogen, plasminogen activator inhibitor-1 (PAI-1), thrombin–anti-thrombin (TAT) complexes, glycosaminoglycans, collagen, complement, and the urokinase plasminogen activator receptor (uPAR) and IGF-II . VN is also involved in the immune defence system through its interaction with the terminal complex of complement.
The insulin-like growth factor (IGF) system plays an important role in a number of disease states, such as cancer and psoriasis, through its ability to modulate cell proliferation, attachment, and migration. Both the IGF-II:VN and IGF-I:IGFBP-5:VN complexes stimulate not only enhanced cell migration, but also enhanced cell protein synthesis in skin keratinocytes.
Bibliography
Vitronectin from Wikipedia, the free encyclopedia
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