[HTML][HTML] The TIMP2 membrane type 1 metalloproteinase “receptor” regulates the concentration and efficient activation of progelatinase A: a kinetic study
GS Butler, MJ Butler, SJ Atkinson, H Will… - Journal of Biological …, 1998 - ASBMB
We have used C-terminal domain mutants to further define the role of interactions of
progelatinase A and membrane type 1 matrix metalloproteinase (MT1 MMP) in the binding
of TIMP2 and in the cell-associated activation of progelatinase A. Soluble constructs of MT1
MMP were used to demonstrate that binding with TIMP2 occurs primarily through N-terminal
domain interactions, leaving the C-terminal domain free for interactions with progelatinase
A. The rate of autolytic activation of progelatinase A initiated by MT1 MMP cleavage could be …
progelatinase A and membrane type 1 matrix metalloproteinase (MT1 MMP) in the binding
of TIMP2 and in the cell-associated activation of progelatinase A. Soluble constructs of MT1
MMP were used to demonstrate that binding with TIMP2 occurs primarily through N-terminal
domain interactions, leaving the C-terminal domain free for interactions with progelatinase
A. The rate of autolytic activation of progelatinase A initiated by MT1 MMP cleavage could be …