α-Synuclein-induced mitochondrial dysfunction in isolated preparation and intact cells: implications in the pathogenesis of Parkinson's disease.

@article{Bir2014SynucleininducedMD,
  title={α-Synuclein-induced mitochondrial dysfunction in isolated preparation and intact cells: implications in the pathogenesis of Parkinson's disease.},
  author={Aritri Bir and Oishimaya Sen and Shruti Anand and Vineet Kumar Khemka and Priyanjalee Banerjee and Roberto Cappai and Arghyadip Sahoo and Sasanka Chakrabarti},
  journal={Journal of neurochemistry},
  year={2014},
  volume={131 6},
  pages={868-77}
}
This study has shown that purified recombinant human α-synuclein (20 μM) causes membrane depolarization and loss of phosphorylation capacity of isolated purified rat brain mitochondria by activating permeability transition pore complex. In intact SHSY5Y (human neuroblastoma cell line) cells, lactacystin (5 μM), a proteasomal inhibitor, causes an accumulation of α-synuclein with concomitant mitochondrial dysfunction and cell death. The effects of lactacystin on intact SHSY5Y cells are, however… CONTINUE READING
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