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Evaluation of Some Newer Matrix Metalloproteinases
Author(s) -
MURPHY GILLIAN,
KNÄUPER VERA,
COWELL SUSAN,
HEMBRY ROSALIND,
STANTON HEATHER,
BUTLER GEORGINA,
FREIJE JOSÉ,
PENDÁS ALBERTO M.,
LÓPEZOTÍN CARLOS
Publication year - 1999
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1999.tb07672.x
Subject(s) - matrix metalloproteinase , matrix (chemical analysis) , computational biology , chemistry , medicine , biology , chromatography
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.