Journal
FEBS LETTERS
Volume 532, Issue 1-2, Pages 127-130Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(02)03654-2
Keywords
activation; procollagenase-3; membrane type matrix metalloproteinase 1; TIMP-2 null mouse; progelatinase A; tissue inhibitor of metalloproteinase-2
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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 Delta(249-451) 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 Gly(35)-Ile(36) was dependent on MT1-MMP activity, as conversion to the active enzyme (Tyr(85) 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 T1MP-2-/- mouse efficiently activated proMMP-13. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
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