Specific collagenolysis by gelatinase A, MMP‐2, is determined by the hemopexin domain and not the fibronectin‐like domain

FEBS Letters

Murphy, Gillian¹  Patterson, Margaret L¹  Knäuper, Vera¹  Atkinson, Susan J¹ 

[1] School of Biological Sciences, University of East Anglia, Norwich, NR4 7TJ, UK

关键词: Gelatinase A;    Matrix metalloproteinase-2;    Hemopexin;    Fibronectin-like domain;    Collagenolysis;    TIMP;    tissue inhibitor of metalloproteinases;    MMP;    matrix metalloproteinase;    ΔGBR MMP-2;    proΔ191-364 MMP-2;    N-terminal MMP-2;    proΔ418-631 MMP-2;    Mca;    methoxycoumarin;    Nva;    norvaline;    Dpa;    diaminopropionyl;    APMA;    p-aminophenylmercuric acetate;   

DOI  :  10.1016/S0014-5793(01)02723-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In view of the essential role of the hemopexin domain of the traditional interstitial collagenases, MMP-1, -8, -13 and MT1-MMP (MMP-14), in determining specific collagen cleavage we have studied the function of this domain in MMP-2, relative to that of the fibronectin-like domain that promotes gelatinolysis. Although the fibronectin-like domain promotes avid binding to collagen, our data demonstrate that the catalytic and hemopexin domains of MMP-2 are sufficient to effect the critical step in cleavage of rat type I collagen into 3/4 and 1/4 fragments. The mechanism of MMP-2 cleavage of collagen proceeds in two phases, the first resembling that of the interstitial collagenases, followed by gelatinolysis, promoted by the fibronectin-like domain.

【 授权许可】

Unknown