Evaluation of some newer matrix metalloproteinases

Murphy, Gillian, Knäuper, Vera ORCID: https://orcid.org/0000-0002-3965-9924, Cowell, Susan, Stanton, Heather, Butler, Georgina, Freije, Jose, Pendas, Alberto M., Lopez-Otin, Carlos and Hembrey, Rosalind 1999. Evaluation of some newer matrix metalloproteinases. Annals of the New York Academy of Sciences 878 (1) , pp. 25-39. 10.1111/j.1749-6632.1999.tb07672.x

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Abstract

Recombinant protein expression techniques have been utilized to facilitate the biochemical and cell biological characterization of human matrix metalloproteinases (MMPs). The importance of the membrane type 1 MMP (MMP 14) in the regulation of pericellular proteolysis, either directly or through the activation of MMP-2, MMP-9, and MMP-13 has been identified. Studies on an in vitro chondrocyte-like cell and an in vivo cartilage repair model indicated that such MT1 MMP-regulated activation cascades are physiologically feasible. MMP19 shows a limited sequence identity with other MMPs and may represent a novel subclass. However, analysis of the recombinant protein identified a number of biochemical properties typical of the MMP family. Proteolysis of the extracellular matrix (ECM) is a key component of the inflammatory response, acting as a key effector in the modulation of the cell-cell and cell-ECM interactions underlying both disease and repair activities. The role of matrix metalloproteinases (MMPs) in matrix turnover has long been under scrutiny, and it has become evident that there is a bewildering array of these enzymes with apparently overlapping substrate specificities and expression patterns. A number of the MMPs that have been identified more recently have been biochemically and biologically characterized in our laboratories in order to relate their function to that of the more established members of the MMP family.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Dentistry
Publisher:	Wiley
ISSN:	1749-6632
Last Modified:	08 Nov 2023 16:30
URI:	https://orca.cardiff.ac.uk/id/eprint/161588

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