The propeptide domain of membrane type 1 matrix metalloproteinase is required for binding of tissue inhibitor of metalloproteinases and for activation of pro-gelatinase A.

@article{Cao1998ThePD,
  title={The propeptide domain of membrane type 1 matrix metalloproteinase is required for binding of tissue inhibitor of metalloproteinases and for activation of pro-gelatinase A.},
  author={Jun-kuo Cao and Michelle Drews and Hsi Ming Lee and Cathleen E Conner and Wadie F. Bahou and Stanley H. Zucker},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 52},
  pages={
          34745-52
        }
}
Activation of secreted latent matrix metalloproteinases (MMPs) is accompanied by cleavage of the N-terminal propeptide, thereby liberating the active zinc from binding to the conserved cysteine in the pro-domain. It has been assumed that an analogous mechanism is responsible for the activation of membrane type 1 MMP (MT1-MMP). Using recombinant wild-type MT1-MMP cDNA and mutant cDNAs transfected into COS-1 cells lacking endogenous MT1-MMP, we have examined the function of the propeptide domain… CONTINUE READING
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