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

Knauper, Vera ORCID: https://orcid.org/0000-0002-3965-9924, Bailey, Louise, Worley, Joanna R., Soloway, Paul, Patterson, Margaret L. and Murphy, Gillian 2002. Cellular activation of proMMP-13 by MT1-MMP depends on the C-terminal domain of MMP-13. FEBS Letters 532 (1-2) , pp. 127-130. 10.1016/S0014-5793(02)03654-2

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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.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Dentistry
Subjects:	Q Science > Q Science (General)
Uncontrolled Keywords:	Activation; Procollagenase-3; Membrane type matrix metalloproteinase 1; TIMP-2 null mouse; Progelatinase A; Tissue inhibitor of metalloproteinase-2.
Publisher:	Elsevier
ISSN:	0014-5793
Last Modified:	27 Oct 2022 10:13
URI:	https://orca.cardiff.ac.uk/id/eprint/69336

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