Functional interaction of endothelial nitric oxide synthase with a voltage-dependent anion channel.

@article{Sun2002FunctionalIO,
  title={Functional interaction of endothelial nitric oxide synthase with a voltage-dependent anion channel.},
  author={Jianxin Sun and James K. Liao},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2002},
  volume={99 20},
  pages={13108-13}
}
Endothelium-derived nitric oxide (NO) is an important regulator of vascular function. NO is produced by endothelial NO synthase (eNOS) whose function is modulated, in part, by specific protein interactions. By coimmunoprecipitation experiments followed by MS analyses, we identified a human voltage-dependent anion/cation channel or porin as a binding partner of eNOS. The interaction between porin and eNOS was demonstrated by coimmunoprecipitation studies in nontransfected human endothelial cells… CONTINUE READING
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Porin enhances eNOS activity in vitro and within cells

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