Modification of permeability transition pore arginine(s) by phenylglyoxal derivatives in isolated mitochondria and mammalian cells. Structure-function relationship of arginine ligands.

@article{Johans2005ModificationOP,
  title={Modification of permeability transition pore arginine(s) by phenylglyoxal derivatives in isolated mitochondria and mammalian cells. Structure-function relationship of arginine ligands.},
  author={Milena Johans and Eva Milanesi and Marina Christina Mikaela Franck and Christoffer Johans and Julius Liobikas and Maria Panagiotaki and Lucedio Greci and Giovanni Principato and Paavo K. J. Kinnunen and Paolo Bernardi and Paola Costantini and Ove Eriksson},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 13},
  pages={12130-6}
}
Methylglyoxal and synthetic glyoxal derivatives react covalently with arginine residue(s) on the mitochondrial permeability transition pore (PTP). In this study, we have investigated how the binding of a panel of synthetic phenylglyoxal derivatives influences the opening and closing of the PTP. Using both isolated mitochondria and mammalian cells, we demonstrate that the resulting arginine-phenylglyoxal adduct can lead to either suppression or induction of permeability transition, depending on… CONTINUE READING
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