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FEBS Lett. 2001 Feb 23;491(1-2):137-42.

Catalytic activities of membrane-type 6 matrix metalloproteinase (MMP25).

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1
School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK. w.english@uea.ac.uk

Abstract

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.

PMID:
11226436
DOI:
10.1016/s0014-5793(01)02150-0
[Indexed for MEDLINE]
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