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PMID: 10415718 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Evaluation of some newer matrix metalloproteinases.

Annals of the New York Academy of Sciences ·Vol. 878 ·1999-06-30 ·Pages 25-39

Murphy G, Knäuper V, Cowell S, Hembry R, Stanton H, Butler G, Freije J, Pendás AM, López-Otín C

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.

MeSH Terms
Animals Enzyme Activation Extracellular Matrix/physiology Humans Matrix Metalloproteinases, Secreted Metalloendopeptidases/genetics,metabolism Models, Biological Recombinant Proteins/metabolism Tissue Inhibitor of Metalloproteinases/pharmacology,physiology
Chemicals
Recombinant Proteins Tissue Inhibitor of Metalloproteinases Matrix Metalloproteinases, Secreted Metalloendopeptidases matrix metalloproteinase 19
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Murphy G
School of Biological Sciences, University of East Anglia, Norwich, UK. g.murphy@uea.ac.uk
Knäuper V
Cowell S
Hembry R
Stanton H
Butler G
Freije J
Pendás A M
López-Otín C
Article Info
Journal
Annals of the New York Academy of Sciences
Abbr.
Ann N Y Acad Sci
ISSN
0077-8923
Published
1999-06-30
Pages
25-39
Language
English
Region
United States
NLM ID
7506858
Subset
IM
Grants
Wellcome Trust · United Kingdom
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