Overexpression of both catalytically active and -inactive cathepsin D by cancer cells enhances apoptosis-dependent chemo-sensitivity

@article{Beaujouin2006OverexpressionOB,
  title={Overexpression of both catalytically active and -inactive cathepsin D by cancer cells enhances apoptosis-dependent chemo-sensitivity},
  author={M{\'e}lanie Beaujouin and Stephen Baghdiguian and Murielle Glondu-Lassis and Guy J. Berchem and Emmanuelle Liaudet-Coopman},
  journal={Oncogene},
  year={2006},
  volume={25},
  pages={1967-1973}
}
The aspartic protease cathepsin D (cath-D) is a key mediator of induced-apoptosis and its proteolytic activity has been generally involved in this event. During apoptosis, cath-D is translocated to the cytosol. Because cath-D is one of the lysosomal enzymes that requires a more acidic pH to be proteolytically active relative to the cysteine lysosomal enzymes such as cath-B and -L, it is therefore open to question whether cytosolic cath-D might be able to cleave substrate(s) implicated in the… CONTINUE READING