[HTML][HTML] The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation …
H Will, SJ Atkinson, GS Butler, B Smith… - Journal of Biological …, 1996 - ASBMB
It has been proposed that the cell-mediated activation of progelatinase A requires binding of
the C-terminal domain of the proenzyme to a membrane-associated complex of the
membrane type matrix metalloproteinase MT1-MMP and TIMP-2. Subsequent sequential
proteolysis of the propeptide by MT1-MMP and gelatinase A is thought to generate the active
form of gelatinase A. We have prepared the proform of the catalytic domain of the MT1-MMP
and demonstrated that this may be activated in vitro by trypsin proteolysis to yield a …
the C-terminal domain of the proenzyme to a membrane-associated complex of the
membrane type matrix metalloproteinase MT1-MMP and TIMP-2. Subsequent sequential
proteolysis of the propeptide by MT1-MMP and gelatinase A is thought to generate the active
form of gelatinase A. We have prepared the proform of the catalytic domain of the MT1-MMP
and demonstrated that this may be activated in vitro by trypsin proteolysis to yield a …