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Ann N Y Acad Sci. 1999 Jun 30;878:25-39.

Evaluation of some newer matrix metalloproteinases.

Author information

1
School of Biological Sciences, University of East Anglia, Norwich, UK. g.murphy@uea.ac.uk

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.

[Indexed for MEDLINE]

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