Evaluation of some newer matrix metalloproteinases.
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.
School of Biological Sciences, University of East Anglia, Norwich, UK. g.murphy@uea.ac.uk
G
G
Murphy
V
V
Knäuper
S
S
Cowell
R
R
Hembry
H
H
Stanton
G
G
Butler
J
J
Freije
A M
AM
Pendás
C
C
López-Otín
D000818:Animals; D004789:Enzyme Activation; D005109:Extracellular Matrix / Q000502:physiology*; D006801:Humans; D053505:Matrix Metalloproteinases, Secreted; D008666:Metalloendopeptidases / Q000235:genetics / Q000378:metabolism*; D008954:Models, Biological; D011994:Recombinant Proteins / Q000378:metabolism; D019714:Tissue Inhibitor of Metalloproteinases / Q000494:pharmacology / Q000502:physiology*
D011994:Recombinant Proteins; D019714:Tissue Inhibitor of Metalloproteinases; D053505:Matrix Metalloproteinases, Secreted; D008666:Metalloendopeptidases; C108362:matrix metalloproteinase 19