Degradation of vitronectin by matrix metalloproteinases‐1, ‐2, ‐3, ‐7 and ‐9
Open Access
- 7 August 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 369 (2-3) , 249-251
- https://doi.org/10.1016/0014-5793(95)00752-u
Abstract
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.Keywords
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