Prion protein-deficient neurons reveal lower glutathione reductase activity and increased susceptibility to hydrogen peroxide toxicity.

@article{White1999PrionPN,
  title={Prion protein-deficient neurons reveal lower glutathione reductase activity and increased susceptibility to hydrogen peroxide toxicity.},
  author={Anthony R White and Steven John Collins and Fran Maher and Michael F. Jobling and Leanne R Stewart and James Thyer and Konrad Beyreuther and Colin L. Masters and Roberto Cappai},
  journal={The American journal of pathology},
  year={1999},
  volume={155 5},
  pages={1723-30}
}
The prion protein (PrP) has a central role in the pathogenesis of transmissible spongiform encephalopathies (TSE). Accumulating evidence suggests that normal cellular PrP (PrP(c)) may be involved in copper homeostasis and modulation of copper/zinc superoxide dismutase (Cu/ZnSOD) activity in neurons. Hydrogen peroxide (H(2)O(2)) is a toxic reactive oxygen species generated through normal cellular respiration, and neurons contain two important peroxide detoxifying systems (glutathione pathway and… CONTINUE READING