Human matrix metalloprotease activation by insults of bacterial infection involving proteases and free radicals.

@article{Maeda1998HumanMM,
  title={Human matrix metalloprotease activation by insults of bacterial infection involving proteases and free radicals.},
  author={Hirofumi Maeda and Tatsuya Okamoto and Takaaki Akaike},
  journal={Biological chemistry},
  year={1998},
  volume={379 2},
  pages={193-200}
}
We found that human matrix metalloproteases (MMPs) may be processed from their proenzyme forms (proMMP) to their active forms by two new and unique mechanisms: Firstly, by bacterial proteases such as Pseudomonas elastase and Vibrio cholerae protease, which cleave off the N-terminal autoinhibitory domain (so-called cysteine switch) from proMMPs. The second mechanism depends on free radical generation by activated polymorphonuclear leukocytes (PMNs). In this case, peroxynitrite (ONOO-) or… CONTINUE READING
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