Modulation of the mitochondrial permeability transition pore by pyridine nucleotides and dithiol oxidation at two separate sites.

@article{Costantini1996ModulationOT,
  title={Modulation of the mitochondrial permeability transition pore by pyridine nucleotides and dithiol oxidation at two separate sites.},
  author={Paola Costantini and Boris V Chernyak and Valeria Petronilli and Paolo Bernardi},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 12},
  pages={6746-51}
}
After accumulation of a Ca2+ load, the addition of uncoupler to respiring rat liver mitochondria is followed by opening of the permeability transition pore (MTP), a voltage-dependent channel sensitive to cyclosporin A. The channel's voltage threshold is profoundly affected under conditions of oxidative stress, with a shift to more negative values that may cause MTP opening at physiological membrane potentials. In this paper we further clarify the mechanisms by which oxidative agents affect the… CONTINUE READING
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