Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0242706 (hyperoxia)
 5,219 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The cysteine residue at the active site of peroxiredoxin (Prx) I, Prx II, or Prx III is reversibly hyperoxidized to cysteine sulfinic acid, with concomitant loss of peroxidase activity, during normal catalysis. Sulfiredoxin (Srx) is the enzyme responsible for reversing this hyperoxidation. We now show that the expression of Srx at both the mRNA and protein levels is increased markedly in the lungs of mice exposed to hyperoxia. This hyperoxia-induced expression of Srx was not evident in mice deficient in the transcription factor Nrf2, indicating an essential role for an Nrf2 signaling pathway in this effect. Hyperoxia also elicited the accumulation of the sulfinic form of the mitochondrial enzyme Prx III, but not that of the cytosolic enzymes Prx I or Prx II, in lung tissue. This selective hyperoxidation of Prx III is likely due either to mitochondria being the major site of the hyperoxia-induced production of reactive oxygen species or to the translocation of Srx from the cytosol into mitochondria being rate limiting for the reduction of sulfinic Prx III. Hyperoxia induced the degradation of Prx III in Nrf2-deficient mice but not in wild-type animals, suggesting that, in the absence of a sufficient amount of Srx, sulfinic Prx III is converted to a form that is susceptible to proteolysis.
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PMID:Induction of sulfiredoxin via an Nrf2-dependent pathway and hyperoxidation of peroxiredoxin III in the lungs of mice exposed to hyperoxia. 1908 7

The mechanisms underlying organisms respond to and protect from hyperoxia remain elusive. We establish a system for cultivating the yeast Saccharomyces cerevisiae cells in liquid medium under 100% O(2) and revealed that SRX1, encoding sulfiredoxin, is significantly induced by 100% O(2) dependently on transcription factors Yap1 and Skn7. Sulfiredoxin has a role in restoring the abundant peroxiredoxin, Tsa1. Tsa1 was indispensable for protection from 100% O(2) in the presence of antimycin A, an inhibitor of complex III in the mitochondrial respiratory chain, collectively emphasizing the significance of sulfiredoxin, peroxiredoxin, and mitochondrial respiratory chain to respond to and to protect from 100% O(2).
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PMID:Significance of sulfiredoxin/peroxiredoxin and mitochondrial respiratory chain in response to and protection from 100% O(2) in Saccharomyces cerevisiae. 2329 33