Role of the redox protein thioredoxin in cytoprotective mechanism evoked by (-)-deprenyl.

@article{Andoh2005RoleOT,
  title={Role of the redox protein thioredoxin in cytoprotective mechanism evoked by (-)-deprenyl.},
  author={Tsugunobu Andoh and P. Boon Chock and Dennis L. Murphy and Chuang Chin Chiueh},
  journal={Molecular pharmacology},
  year={2005},
  volume={68 5},
  pages={1408-14}
}
Through the inhibition of monoamine oxidase type B (MAO-B), (-)-deprenyl (selegiline) prevents the conversion of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) to the toxic metabolite 1-methyl-4-phenylpyridinium ion (MPP+) and also prevents the neurotoxicity in the dopaminergic neurons in animal models. Cumulative observations suggest that selegiline may also protect against MPP+-induced neurotoxicity, possibly through the induction of pro-survival genes. We have observed that thioredoxin… CONTINUE READING