Osteopontin is a 34kDa extracellular matrix protein with a cell binding domain. It was originally identified as a major component of the non-collagenous organic bone matrix, however, it has subsequently been demonstrated in a wide range of normal adult tissue and body fluids. It is a multifunctional protein involved in bone mineralization, cell adhesion, cell migration, chronic inflammatory disease and transformation. Proteolytic cleavage by thrombin and matrix metalloproteinases close to the integrin-binding Arg-Gly-Asp sequence modulates the function of OPN and its integrin binding properties. Thrombin-cleaved fragments of Osteopontin are overexpressed in malignant glial tumors and provide a molecular niche with survival advantage and provide a novel substrate for plasmin and cathepsin D.
44 kDa bone phosphoprotein; BNSP; Bone sialoprotein 1; calcium oxalate crystal growth inhibitor protein; early T-lymphocyte activation 1; early T-lymphocyte activation 1 protein; minopontin; Nephropontin; OPN; Osteopontin; osteopontin-like protein; osteopontin/immunoglobulin alpha 1 heavy chain constant region fusion protein; PSEC0156; Secreted Phosphoprotein 1; secreted phosphoprotein 1 (osteopontin, bone sialoprotein I, early T-lymphocyte activation 1); secreted phosphoprotein 1 variant 6; SPP-1; SPP1/CALPHA1 fusion; Urinary stone protein; Uropontin
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