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FEBS Lett. 2002 Dec 4;532(1-2):127-30.

Cellular activation of proMMP-13 by MT1-MMP depends on the C-terminal domain of MMP-13.

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  • 1School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK. vk8@york.ac.uk

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 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 TIMP-2-/- mouse efficiently activated proMMP-13.

PMID:
12459476
[PubMed - indexed for MEDLINE]
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