Alpha(v)beta(3) integrin engagement enhances cell invasiveness in human multiple myeloma.

摘要: BACKGROUND AND OBJECTIVES: In multiple myeloma (MM), the mechanisms used by plasma cells to invade locally and metastasize are thought be similar those developed solid tumors include cell proliferation secretion of extracellular matrix (ECM) degrading enzymes following adhesion ECM proteins. We studied these in fresh bone marrow patients with MM after proteins vitronectin (VN) fibronectin (FN). DESIGN METHODS: The ability adhere VN FN consequent formation focal plaques on surface, their composition phosphorylation several signal transduction proteins, metalloproteinase-2 (MMP-2) -9 (MMP-9) urokinase-type plasminogen activator (uPA) were studied. RESULTS: Plasma adhered immobilized FN. Adhesion was fully prevented neutralizing anti-avb3 integrin antibody. Integrin engagement caused aggregation plaques, which contained b3 subunit, some cytoskeletal tyrosine kinases, Grb-2 adapter protein, mitogen-activated protein (MAP) kinase. Free stimulated production release uPA, increased activated forms MMP-2 MMP-9 an avb3 integrin-dependent manner. INTERPRETATION CONCLUSIONS: This interact via suggests a novel mechanism for invasion spreading, since this interaction allows them substratum enhances protease secretion.