Sulfiredoxin Translocation into Mitochondria Plays a Crucial Role in Reducing Hyperoxidized Peroxiredoxin III

We further demonstrate that Srx translocates from the cytosol to mitochondria in response to oxidative stress

You Hyun Noh


Scholarcy highlights

  • Peroxiredoxins2 are a family of enzymes that catalyze the reduction of hydrogen peroxide and hydroperox
  • We previously developed a method to monitor the Srx could translocate to the mitochondria in response to H2O2. reduction of sulfinic 2-Cys Prx enzymes by immunoblot analy- To examine this possibility, we investigated the intracellular sis with antibodies that recog- localization of Srx under basal conditions and after oxidative nize both sulfinic and sulfonic forms of these proteins . stress, using subcellular fractionation and confocal
  • Effects of Mitochondria-targeted Srx Overexpression on Rotenone-induced Apoptotic Phenotypes—We looked at the effects of ectopic mitochondrion-targeted Srx expression on steady-state level of sulfinic Prx III in cells treated with rotenone, which inhibits NADH conversion to NAD through respiratory Complex I
  • Various aging and pathological conditions are related to an increase in mitochondrial generation of reactive oxygen species
  • Previous studies have shown that Prx III is vulnerable to inactivation through hyperoxidation of its active site cysteine residues in cells and rodent tissues under oxidative stress
  • Addivation is similar to previous findings that cytosolic DJ-1 or tionally, mitoSrx overexpression results in a decrease in the p66Shc protein translocate to mitochondria following oxidative level of mitochondrial H2O2, which diffuses into stress
  • Overexpression of mitochondrion-targeted Srx efficiently promotes the restoration of Prx III and results in cellular resistance to apoptosis with enhanced elimination of mitochondrial H2O2 and decreased rates of ⌬⌿m collapse

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