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

English, William Roger ORCID: https://orcid.org/0000-0003-3024-2441, Velasco, Gloria, Stracke, Jan Olaf, Knäuper, Vera and Murphy, Gillian (2001) Catalytic activities of membrane-type 6 matrix metalloproteinase (MMP25). FEBS Letters, 491 (1-2). pp. 137-142. ISSN 1873-3468

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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.

Item Type:	Article
Faculty \ School:	Faculty of Medicine and Health Sciences > Norwich Medical School Faculty of Science > School of Biological Sciences
UEA Research Groups:	Faculty of Medicine and Health Sciences > Research Centres > Metabolic Health
Depositing User:	LivePure Connector
Date Deposited:	15 Nov 2018 10:30
Last Modified:	19 Oct 2023 01:05
URI:	https://ueaeprints.uea.ac.uk/id/eprint/68899
DOI:	10.1016/S0014-5793(01)02150-0

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