Evaluation of some newer matrix metalloproteinases

被引：83

作者：

Murphy, G ^{[1
]}

Knäuper, V

Cowell, S

Hembry, R

Stanton, H

Butler, G

Freije, J

Pendás, AM

López-Otín, C

机构：

[1] Univ E Anglia, Sch Biol Sci, Norwich NR4 7TJ, Norfolk, England

[2] Strangeways Res Lab, Cambridge CB1 4RN, England

[3] Univ Oviedo, Fac Med, Dept Bioquim & Biol Mol, Oviedo, Spain

来源：

INHIBITION OF MATRIX METALLOPROTEINASES: THERAPEUTIC APPLICATIONS | 1999年 / 878卷

基金：

英国惠康基金;

关键词：

D O I：

10.1111/j.1749-6632.1999.tb07672.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：

Recombinant protein expression techniques have been utilized to facilitate the biochemical and cell biological characterization of human matrix metalloproteinases (MMPs). The importance of the membrane type 1 MMP (MMP 14) in the regulation of pericellular proteolysis, either directly or through the activation of MMP-2, MMP-9, and MMP-13 has been identified. Studies on an in vitro chondrocyte-like cell and an in vivo cartilage repair model indicated that such MT1 MMP-regulated activation cascades are physiologically feasible. MMP19 shows a limited sequence identity with other MMPs and may represent a novel subclass. However, analysis of the recombinant protein identified a number of biochemical properties typical of the MMP family.

引用

页码：25 / 39

页数：15

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