NO restores HIF-1alpha hydroxylation during hypoxia: role of reactive oxygen species.

@article{Callapina2005NORH,
  title={NO restores HIF-1alpha hydroxylation during hypoxia: role of reactive oxygen species.},
  author={Melvin Callapina and Jie Zhou and Tobias Schmid and Roman K{\"o}hl and Bernhard Br{\"u}ne},
  journal={Free radical biology & medicine},
  year={2005},
  volume={39 7},
  pages={925-36}
}
The activity of hypoxia-inducible factor 1 (HIF-1) is primarily determined by stability regulation of its alpha subunit, which is stabilized under hypoxia but degraded during normoxia. Hydroxylation of HIF-1alpha by prolyl hydroxylases (PHDs) recruits the von Hippel-Lindau (pVHL) E3 ubiquitin ligase complex to initiate proteolytic destruction of the alpha subunit. Hypoxic stabilization of HIF-1alpha has been reported to be antagonized by nitric oxide (NO). By using a HIF-1alpha-pVHL binding… CONTINUE READING

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