Role of critical thiol groups on the matrix surface of the adenine nucleotide translocase in the mechanism of the mitochondrial permeability transition pore.

@article{McStay2002RoleOC,
  title={Role of critical thiol groups on the matrix surface of the adenine nucleotide translocase in the mechanism of the mitochondrial permeability transition pore.},
  author={Gavin P. McStay and Samantha J. Clarke and Andrew Philip Halestrap},
  journal={The Biochemical journal},
  year={2002},
  volume={367 Pt 2},
  pages={541-8}
}
Opening of the mitochondrial permeability transition pore (MPTP) is sensitized to [Ca(2+)] by oxidative stress (diamide) and phenylarsine oxide (PAO). We have proposed that both agents cross-link two thiol groups on the adenine nucleotide translocase (ANT) involved in ADP and cyclophilin-D (CyP-D) binding. Here, we demonstrate that blocking Cys(160) with 80 microM eosin 5-maleimide (EMA) or 500 microM N-ethylmaleimide (NEM) greatly decreased ADP inhibition of the MPTP. The ability of diamide… CONTINUE READING
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