Mechanisms for pro matrix metalloproteinase activation

Murphy, Gillian, Stanton, Heather, Cowell, Susan, Butler, Georgina, Knauper, Vera ORCID: https://orcid.org/0000-0002-3965-9924, Susan, Atkinson and Gavrilovic, Jelena 1999. Mechanisms for pro matrix metalloproteinase activation. APMIS 107 (1-6) , pp. 38-44. 10.1111/j.1699-0463.1999.tb01524.x

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Abstract

The activation of pro matrix metalloproteinases (MMPs) by sequential proteolysis of the propeptide blocking the active site cleft is regarded as one of the key levels of regulation of these proteinases. Potential physiological mechanisms including cell-associated plasmin generation by urokinase-like plasminogen activator, or the action of cell surface MT1-MMPs appear to be involved in the initiation of cascades of pro MMP activation. Gelatinase A, collagenase 3 and gelatinase B may be activated by MT-MMP based mechanisms, as evidenced by both biochemical and cell based studies. Hence the regulation of MT-MMPs themselves becomes critical to the determination of MMP activity. This includes activation, assembly at the cell surfaces as TIMP-2 complexes and subsequent inactivation by proteolysis or TIMP inhibition.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Dentistry
Publisher:	Wiley
ISSN:	0903-4641
Last Modified:	15 Sep 2023 11:00
URI:	https://orca.cardiff.ac.uk/id/eprint/161627

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