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- Title
Cellular activation of proMMP-13 by MT1-MMP depends on the C-terminal domain of MMP-13
- Authors
Knäuper, Vera; Bailey, Louise; Worley, Joanna R.; Soloway, Paul; Patterson, Margaret L.; Murphy, Gillian
- Abstract
Procollagenase-3 (proMMP-13) can be activated by soluble or cell associated membrane type matrix metalloproteinase 1 (MT1-MMP). In this study we show that the cell based activation of proMMP-13 by MT1-MMP was dependent on the C-terminal domain, as Δ249–451 proMMP-13, which lacks the haemopexin domain, and a chimaera from N-terminal MMP-13 and C-terminal MMP-19 (proMMP-13/19) were not processed by MT1-MMP expressing cells. Only the initial cleavage at Gly35–Ile36 was dependent on MT1-MMP activity, as conversion to the active enzyme (Tyr85 N-terminus) required a functional MMP-13 active site. Unlike proMMP-2 activation, this process was independent of tissue inhibitor of metalloproteinase-2 (TIMP-2) as MT1-MMP expressing cells from the TIMP-2−/− mouse efficiently activated proMMP-13.
- Subjects
METALLOPROTEINASES; ENZYMES
- Publication
FEBS Letters, 2002, Vol 532, Issue 1/2, p127
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/S0014-5793(02)03654-2