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

William Roger English, Gloria Velasco, Jan Olaf Stracke, Vera Knäuper, Gillian Murphy

Research output: Contribution to journalArticlepeer-review

77 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)137-142
Number of pages6
JournalFEBS Letters
Issue number1-2
Publication statusPublished - 23 Feb 2001

Cite this