Inhibition of the activation of multiple serine proteases with a cathepsin C inhibitor requires sustained exposure to prevent pro-enzyme processing.

@article{Mthot2007InhibitionOT,
  title={Inhibition of the activation of multiple serine proteases with a cathepsin C inhibitor requires sustained exposure to prevent pro-enzyme processing.},
  author={Nathalie M{\'e}thot and Joel E. Rubin and Daniel Guay and Christian Beaulieu and Diane Ethier and T. Jagadeeswar Reddy and Denis Riendeau and Maida Percival},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 29},
  pages={20836-46}
}
Cathepsin C is a cysteine protease required for the activation of several pro-inflammatory serine proteases and, as such, is of interest as a therapeutic target. In cathepsin C-deficient mice and humans, the N-terminal processing and activation of neutrophil elastase, cathepsin G, and proteinase-3 is abolished and is accompanied by a reduction of protein levels. Pharmacologically, the consequence of cathepsin C inhibition on the activation of these serine proteases has not been described, due… CONTINUE READING

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