Glutathione adducts induced by ischemia and deletion of glutaredoxin-1 stabilize HIF-1α and improve limb revascularization.

@article{Watanabe2016GlutathioneAI,
  title={Glutathione adducts induced by ischemia and deletion of glutaredoxin-1 stabilize HIF-1α and improve limb revascularization.},
  author={Yosuke Watanabe and Colin E Murdoch and Soichi Sano and Yasuo Ido and Markus M Bachschmid and Richard Alan Cohen and Reiko Matsui},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2016},
  volume={113 21},
  pages={6011-6}
}
Reactive oxygen species (ROS) are increased in ischemic tissues and necessary for revascularization; however, the mechanism remains unclear. Exposure of cysteine residues to ROS in the presence of glutathione (GSH) generates GSH-protein adducts that are specifically reversed by the cytosolic thioltransferase, glutaredoxin-1 (Glrx). Here, we show that a key angiogenic transcriptional factor hypoxia-inducible factor (HIF)-1α is stabilized by GSH adducts, and the genetic deletion of Glrx improves… CONTINUE READING
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In mouse muscle C2C12 cells , HIF-1α protein levels are increased by increasing GSH adducts with cell - permeable oxidized GSH ( GSSG - ethyl ester ) or 2-acetylamino-3-[4-(2-acetylamino-2-carboxyethylsulfanyl thiocarbonylamino ) phenylthiocarbamoylsulfanyl ] propionic acid ( 2-AAPA ) , an inhibitor of glutathione reductase .
In mouse muscle C2C12 cells , HIF-1α protein levels are increased by increasing GSH adducts with cell - permeable oxidized GSH ( GSSG - ethyl ester ) or 2-acetylamino-3-[4-(2-acetylamino-2-carboxyethylsulfanyl thiocarbonylamino ) phenylthiocarbamoylsulfanyl ] propionic acid ( 2-AAPA ) , an inhibitor of glutathione reductase .
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