DEGRADATION OF VITRONECTIN BY MATRIX METALLOPROTEINASE-1, METALLOPROTEINASE-2, METALLOPROTEINASE-3, METALLOPROTEINASE-7 AND METALLOPROTEINASE-9

被引:56
作者
IMAI, K
SHIKATA, H
OKADA, Y
机构
[1] KANAZAWA UNIV, CANC RES INST, DEPT MOLEC IMMUNOL & PATHOL, KANAZAWA, ISHIKAWA 920, JAPAN
[2] MEIKAI UNIV, SCH DENT, DEPT ORAL PATHOL, SAKADO, SAITAMA 35002, JAPAN
来源
FEBS LETTERS | 1995年 / 369卷 / 2-3期
关键词
VITRONECTIN; MATRIX METALLOPROTEINASE; DEGRADATION; KINETICS;
D O I
10.1016/0014-5793(95)00752-U
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:249 / 251
页数:3
相关论文
共 21 条
  • [21] YATOHGO T, 1988, CELL STRUCT FUNCT, V13, P281, DOI 10.1247/csf.13.281