Activation of human neutrophil procollagenase by stromelysin 2

被引：64

作者：

Knauper, V ^{[1
]}

Murphy, G ^{[1
]}

Tschesche, H ^{[1
]}

机构：

[1] UNIV BIELEFELD, DEPT BIOCHEM, W-4800 BIELEFELD, GERMANY

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1996年 / 235卷 / 1-2期

基金：

英国惠康基金;

关键词：

activation; neutrophil collagenase; stromelysin; 2; matrix metalloproteinases;

D O I：

10.1111/j.1432-1033.1996.00187.x

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：

Neutrophil procollagenase (MMP-8) was efficiently activated by incubation with active stromelysin 2 (MMP-10). A single-step activation mechanism involving the cleavage of the Gly78-Phe79 peptide bond at the end of the propeptide domain was observed. Determination of the collagenolytic activity revealed the generation of active neutrophil collagenase displaying high specific activity. When compared with the specific activity following mercurial activation, which generates active collagenase by autoproteolytic cleavage of either Phe79-Met80 or Met80-Leu81 peptide bonds [Blaser, J., Knauper, V., Osthues, A., Reinke, H. & Tschesche, H. (1991) fur: J. Biochem. 202, 1223-1230], the specific activity of the stromelysin-2-activated enzyme was considerably higher. Thus, human neutrophil procollagenase was 'superactivated' by stromelysin 2, as was recently shown for the stromelysin-1-activated enzyme [Knauper, V., Wilhelm, S. M., Seperack, P. K., De Clerck,Y. A., Langley, K. E., Osthues, A. & Tschesche, H. (1993 a) Biochem. J. 295, 581-586].

引用

页码：187 / 191

页数：5

共 51 条

[21] THE MATRIX-DEGRADING METALLOPROTEINASES [J].