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

English, William Roger, 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. 10.1016/S0014-5793(01)02150-0

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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
Date Type:	Publication
Status:	Published
Schools:	Dentistry
Publisher:	Wiley
ISSN:	1873-3468
Date of Acceptance:	19 January 2001
Last Modified:	14 Sep 2023 13:00
URI:	https://orca.cardiff.ac.uk/id/eprint/161594

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