Interstitial Collagen Catabolism

被引：153

作者：

Fields, Gregg B. ^{[1
]}

机构：

[1] Torrey Pines Inst Mol Studies, Port St Lucie, FL 34987 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2013年 / 288卷 / 13期

基金：

美国国家卫生研究院;

关键词：

HUMAN CATHEPSIN-K; MATRIX-METALLOPROTEINASE ACTIVITIES; NATIVE TYPE-I; NEUTROPHIL COLLAGENASE; SUBSTRATE-SPECIFICITY; GELATINASE-A; FIBROBLAST COLLAGENASE; MOLECULAR-MECHANISM; THERMAL-STABILITY; CATALYTIC DOMAIN;

D O I：

10.1074/jbc.R113.451211

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：

Interstitial collagen mechanical and biological properties are altered by proteases that catalyze the hydrolysis of the collagen triple-helical structure. Collagenolysis is critical in development and homeostasis but also contributes to numerous pathologies. Mammalian collagenolytic enzymes include matrix metalloproteinases, cathepsin K, and neutrophil elastase, and a variety of invertebrates and pathogens possess collagenolytic enzymes. Components of the mechanism of action for the collagenolytic enzyme MMP-1 have been defined experimentally, and insights into other collagenolytic mechanisms have been provided. Ancillary biomolecules may modulate the action of collagenolytic enzymes.

引用

页码：8785 / 8793

页数：9

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