| Literature DB >> 10415718 |
G Murphy1, V Knäuper, S Cowell, R Hembry, H Stanton, G Butler, J Freije, A M Pendás, C López-Otín.
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.Entities:
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Year: 1999 PMID： 10415718 DOI： 10.1111/j.1749-6632.1999.tb07672.x
Source DB: PubMed Journal: Ann N Y Acad Sci ISSN： 0077-8923 Impact factor: 5.691