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Mechanisms for pro matrix metalloproteinase activation
Author(s) -
MURPHY GILLIAN,
STANTON HEATHER,
COWELL SUSAN,
BUTLER GEORGINA,
KNÄUPER VERA,
ATKINSON SUSAN,
GAVRILOVIC JELENA
Publication year - 1999
Publication title -
apmis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0903-4641
DOI - 10.1111/j.1699-0463.1999.tb01524.x
Subject(s) - matrix metalloproteinase , plasmin , proteolysis , gelatinase a , gelatinase , chemistry , plasminogen activator , microbiology and biotechnology , metalloproteinase , urokinase , cell , activator (genetics) , collagenase , interstitial collagenase , enzyme activator , biochemistry , enzyme , biology , receptor , endocrinology , genetics
The activation of pro matrix metalloproteinases (MMPs) by sequential proteolysis of the propeptide blocking the active site cleft is regarded as one of the key levels of regulation of these proteinases. Potential physiological mechanisms including cell‐associated plasmin generation by urokinase‐like plasminogen activator, or the action of cell surface MT1‐MMPs appear to be involved in the initiation of cascades of pro MMP activation. Gelatinase A, collagenase 3 and gelatinase B may be activated by MT‐MMP based mechanisms, as evidenced by both biochemical and cell based studies. Hence the regulation of MT‐MMPs themselves becomes critical to the determination of MMP activity. This includes activation, assembly at the cell surfaces as TIMP‐2 complexes and subsequent inactivation by proteolysis or TIMP inhibition.