Catalytic activities of membrane‐type 6 matrix metalloproteinase (MMP25)

FEBS Letters

Stracke, Jan Olaf¹  English, William Roger¹  Murphy, Gillian¹  Velasco, Gloria²  Knäuper, Vera¹ 

[1] School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK;Departamento de Bioquı́mica y Biologı́a Molecular, Facultad de Medicina, Universidad de Oviedo, 33006 Oviedo, Spain

关键词: Membrane-type matrix metalloproteinase;    MT6-MMP;    Tissue inhibitor of metalloproteinase;    Extracellular matrix;    Type-IV collagen;    GPI;    glycosylphosphatidylinositol;    ECM;    extracellular matrix;    MMP;    matrix metalloproteinase;    MT-MMP;    membrane-type matrix metalloproteinase;    TIMP;    tissue inhibitor of metalloproteinase;    Mca;    (7-methoxycoumarin-4-yl)acetyl;    Dnp;    2;    4-dinitrophenyl;   

DOI  :  10.1016/S0014-5793(01)02150-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

This study describes the biochemical characterisation of the catalytic domain of membrane-type 6 matrix metalloproteinase (MT6-MMP, MMP25, leukolysin). Its activity towards synthetic peptide substrates, components of the extracellular matrix and inhibitors of MMPs was studied and compared with MT1-MMP, MT4-MMP and stromelysin-1. We have found that MT6-MMP is closer in function to stromelysin-1 than MT1 and MT4-MMP in terms of substrate and inhibitor specificity, being able to cleave type-IV collagen, gelatin, fibronectin and fibrin. However, it differs from stromelysin-1 and MT1-MMP in its inability to cleave laminin-I, and unlike stromelysin-1 cannot activate progelatinase B. Our findings suggest that MT6-MMP could play a role in cellular migration and invasion of the extracellular matrix and basement membranes and its activity may be tightly regulated by all members of the TIMP family.

【 授权许可】

Unknown