THE C-TERMINAL DOMAIN OF 72-KDA GELATINASE-A IS NOT REQUIRED FOR CATALYSIS, BUT IS ESSENTIAL FOR MEMBRANE ACTIVATION AND MODULATES INTERACTIONS WITH TISSUE INHIBITORS OF METALLOPROTEINASES

被引：265

作者：

MURPHY, G ^{[1
]}

WILLENBROCK, F ^{[1
]}

WARD, RV ^{[1
]}

COCKETT, MI ^{[1
]}

EATON, D ^{[1
]}

DOCHERTY, AJP ^{[1
]}

机构：

[1] CELLTECH LTD, SLOUGH SL1 4EN, ENGLAND

来源：

BIOCHEMICAL JOURNAL | 1992年 / 283卷

关键词：

D O I：

10.1042/bj2830637

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：

Recombinant 72 kDa gelatinase A and a truncated form lacking the C-terminal domain were shown to be activated by organomercurials and to possess similar activities towards a number of substrates. The truncated proenzyme differed from the full-length gelatinase in that it could not be activated by a membrane activator and did not bind tissue inhibitor of metalloproteinase (TIMP)-2. Kinetic studies also showed that the inhibition of the activated truncated enzyme, by both TIMP-1 and TIMP-2, was considerably decreased compared with the full-length enzyme. We conclude that the C-terminal domain plays an important role in the regulation of gelatinase A by a potential physiological activator and inhibitors.

引用

页码：637 / 641

页数：5

共 36 条

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