Degradation of vitronectin by matrix metalloproteinases-1, -2, -3, -7 and -9.
The susceptibility of vitronectin (Vn) purified from human plasma to digestion by matrix metalloproteinases (MMPs) was examined. MMP-2, -3, -7 and -9 except for MMP-1 degraded Vn into multiple fragments. MMP-7 showed the highest activity to the substrate among these MMPs, digesting 8-, 30- and 44-fold more preferentially than MMP-2, -3, and -9, respectively. These data suggest that MMP-2, -3, -7 and -9 may be responsible for the pathological degradation and/or normal turnover of Vn.
Imai
K
K
Department of Molecular Immunology and Pathology, Cancer Research Institute, Kanazawa University, Ishikawa, Japan.
Shikata
H
H
Okada
Y
Y
D001798:Blood Proteins / Q000302:isolation & purification / Q000378:metabolism*; D006023:Glycoproteins / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008666:Metalloendopeptidases / Q000378:metabolism*; D019096:Vitronectin
D001798:Blood Proteins; D006023:Glycoproteins; D019096:Vitronectin; D008666:Metalloendopeptidases