K. Imai et al., DEGRADATION OF VITRONECTIN BY MATRIX METALLOPROTEINASE-1, METALLOPROTEINASE-2, METALLOPROTEINASE-3, METALLOPROTEINASE-7 AND METALLOPROTEINASE-9, FEBS letters, 369(2-3), 1995, pp. 249-251
The susceptibility of vitronectin (Vn) purified from human plasma to d
igestion 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, digesti
ng 8-, 30-and 44-fold more preferentially than MMP-2, -3 and -9, respe
ctively. These data suggest that MMP-2, -3, -7 and -9 may be responsib
le for the pathological degradation and/or normal turnover of Vn.