Mechanisms for pro matrix metalloproteinase activation
GILLIAN MURPHY,
HEATHER STANTON,
SUSAN COWELL, GEORGINA BUTLER,
VERA KNÄUPER,
SUSAN ATKINSON,
JELENA GAVRILOVIC,
Corresponding Author
GILLIAN MURPHY
School of Biological Sciences, University of East Anglia, Norwich, UK
School of Biological Sciences, University of East Anglia, Norwich, UK.Search for more papers by this authorHEATHER STANTON
School of Biological Sciences, University of East Anglia, Norwich, UK
Search for more papers by this authorGEORGINA BUTLER
School of Biological Sciences, University of East Anglia, Norwich, UK
Search for more papers by this authorVERA KNÄUPER
School of Biological Sciences, University of East Anglia, Norwich, UK
Search for more papers by this authorSUSAN ATKINSON
School of Biological Sciences, University of East Anglia, Norwich, UK
Search for more papers by this authorJELENA GAVRILOVIC
School of Biological Sciences, University of East Anglia, Norwich, UK
Search for more papers by this authorGILLIAN MURPHY,
HEATHER STANTON,
SUSAN COWELL, GEORGINA BUTLER,
VERA KNÄUPER,
SUSAN ATKINSON,
JELENA GAVRILOVIC,
Corresponding Author
GILLIAN MURPHY
School of Biological Sciences, University of East Anglia, Norwich, UK
School of Biological Sciences, University of East Anglia, Norwich, UK.Search for more papers by this authorHEATHER STANTON
School of Biological Sciences, University of East Anglia, Norwich, UK
Search for more papers by this authorGEORGINA BUTLER
School of Biological Sciences, University of East Anglia, Norwich, UK
Search for more papers by this authorVERA KNÄUPER
School of Biological Sciences, University of East Anglia, Norwich, UK
Search for more papers by this authorSUSAN ATKINSON
School of Biological Sciences, University of East Anglia, Norwich, UK
Search for more papers by this authorJELENA GAVRILOVIC
School of Biological Sciences, University of East Anglia, Norwich, UK
Search for more papers by this authorAbstract
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.
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