Online citations, reference lists, and bibliographies.
← Back to Search

Induction Of Sulfiredoxin Via An Nrf2-dependent Pathway And Hyperoxidation Of Peroxiredoxin III In The Lungs Of Mice Exposed To Hyperoxia.

S. Bae, H. Woo, S. Sung, H. Lee, Se Kyoung Lee, I. S. Kil, S. Rhee
Published 2009 · Biology, Medicine

Save to my Library
Download PDF
Analyze on Scholarcy Visualize in Litmaps
Reduce the time it takes to create your bibliography by a factor of 10 by using the world’s favourite reference manager
Time to take this seriously.
Get Citationsy
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.
This paper references
The mitochondrial generation of hydrogen peroxide. General properties and effect of hyperbaric oxygen.
A. Boveris (1973)
Hyperoxia increases oxygen radical production in rat lungs and lung mitochondria.
B. Freeman (1981)
Regulation of human NAD(P)H:quinone oxidoreductase gene. Role of AP1 binding site contained within human antioxidant response element.
Y. Li (1992)
Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes.
H. Z. Chae (1994)
Lung liquid clearance and Na,K-ATPase during acute hyperoxia and recovery in rats.
W. Olivera (1995)
An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements.
K. Itoh (1997)
Transgenic models for the study of lung antioxidant defense: enhanced manganese-containing superoxide dismutase activity gives partial protection to B6C3 hybrid mice exposed to hyperoxia.
Y. Ho (1998)
Susceptibility of heterozygous MnSOD gene-knockout mice to oxygen toxicity.
M. Tsan (1998)
Targeted disruption of the ubiquitous CNC‐bZIP transcription factor, Nrf‐1, results in anemia and embryonic lethality in mice
J. Chan (1998)
Oxygen toxicity in mouse lung: pathways to cell death.
C. Barazzone (1998)
Chemokine mRNA alterations in newborn and adult mouse lung during acute hyperoxia.
C. D’Angio (1998)
Heme oxygenase-1: molecular mechanisms of gene expression in oxygen-related stress.
S. Ryter (2002)
Regulation of Peroxiredoxin I Activity by Cdc2-mediated Phosphorylation*
T. Chang (2002)
Role of NRF2 in protection against hyperoxic lung injury in mice.
H. Cho (2002)
Proteomics Analysis of Cellular Response to Oxidative Stress
T. Rabilloud (2002)
A Comparative Study on the Hydroperoxide and Thiol Specificity of the Glutathione Peroxidase Family and Selenoprotein P*
G. Takebe (2002)
Inactivation of Human Peroxiredoxin I during Catalysis as the Result of the Oxidation of the Catalytic Site Cysteine to Cysteine-sulfinic Acid*
Kap-Seok Yang (2002)
Structure, mechanism and regulation of peroxiredoxins.
Z. Wood (2003)
ATP-dependent reduction of cysteine–sulphinic acid by S. cerevisiae sulphiredoxin
B. Biteau (2003)
Reversing the Inactivation of Peroxiredoxins Caused by Cysteine Sulfinic Acid Formation
H. A. Woo (2003)
Modulation of Gene Expression by Cancer Chemopreventive Dithiolethiones through the Keap1-Nrf2 Pathway
Mi-Kyoung Kwak (2003)
Reversible Oxidation of the Active Site Cysteine of Peroxiredoxins to Cysteine Sulfinic Acid
Induction of 1-cys peroxiredoxin expression by oxidative stress in lung epithelial cells.
Han-Suk Kim (2003)
Characterization of Mammalian Sulfiredoxin and Its Reactivation of Hyperoxidized Peroxiredoxin through Reduction of Cysteine Sulfinic Acid in the Active Site to Cysteine*
T. Chang (2004)
Reduction of Cysteine Sulfinic Acid by Sulfiredoxin Is Specific to 2-Cys Peroxiredoxins*
H. Woo (2005)
Nrf1 and Nrf2 Regulate Rat Glutamate-Cysteine Ligase Catalytic Subunit Transcription Indirectly via NF-κB and AP-1
Heping Yang (2005)
Transcriptional response of pancreatic beta cells to metabolic stimulation: large scale identification of immediate-early and secondary response genes
Dominique A Glauser (2007)
Cytokines in tolerance to hyperoxia-induced injury in the developing and adult lung.
V. Bhandari (2006)
Nrf2 defends the lung from oxidative stress.
H. Cho (2006)
A novel role for human sulfiredoxin in the reversal of glutathionylation.
V. Findlay (2006)
Hyperoxia stimulates an Nrf2-ARE transcriptional response via ROS-EGFR-PI3K-Akt/ERK MAP kinase signaling in pulmonary epithelial cells.
Srinivas Papaiahgari (2006)
Molecular Mechanism of the Reduction of Cysteine Sulfinic Acid of Peroxiredoxin to Cysteine by Mammalian Sulfiredoxin*
W. Jeong (2006)
Hyperoxia-induced reactive oxygen species formation in pulmonary capillary endothelial cells in situ.
Corinna Brueckl (2006)
Regulation of Peroxiredoxins by Nitric Oxide in Immunostimulated Macrophages*
Alexandre Diet (2007)
Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway.
T. Kensler (2007)
The High Reactivity of Peroxiredoxin 2 with H2O2 Is Not Reflected in Its Reaction with Other Oxidants and Thiol Reagents*
A. Peskin (2007)
Irreversible Oxidation of the Active-site Cysteine of Peroxiredoxin to Cysteine Sulfonic Acid for Enhanced Molecular Chaperone Activity*
J. C. Lim (2008)
Protein cysteine sulfinic acid reductase (sulfiredoxin) as a regulator of cell proliferation and drug response
K. Lei (2008)
Sulfiredoxin is an AP-1 target gene that is required for transformation and shows elevated expression in human skin malignancies
Q. Wei (2008)
HDAC6 is a specific deacetylase of peroxiredoxins and is involved in redox regulation
R. Parmigiani (2008)
Synaptic NMDA receptor activity boosts intrinsic antioxidant defenses
S. Papadia (2008)
Induction of sulfiredoxin expression and reduction of peroxiredoxin hyperoxidation by the neuroprotective Nrf2 activator 3H‐1,2‐dithiole‐3‐thione
Francesc X Soriano (2008)

This paper is referenced by
Nrf2 deficiency decreases NADPH from impaired IDH shuttle and pentose phosphate pathway in retinal pigmented epithelial cells to magnify oxidative stress‐induced mitochondrial dysfunction
M. Cano (2021)
Peroxiredoxins—The Underrated Actors during Virus-Induced Oxidative Stress
I. Karpenko (2021)
The protective effect of Veronica ciliata Fisch. extracts on relieving oxidative stress-induced liver injury via activating AMPK/p62/Nrf2 pathway.
Q. Lu (2021)
The Emerging Role of Sestrin2 in Cell Metabolism, and Cardiovascular and Age-Related Diseases
Wanqing Sun (2020)
Sesn2 attenuates the damage of endothelial progenitor cells induced by angiotensin II through regulating the Keap1/Nrf2 signal pathway
Shiao Ding (2020)
Ablation of Peroxiredoxin V Exacerbates Ischemia/Reperfusion-Induced Kidney Injury in Mice
Jiyoung Park (2020)
Peroxiredoxins and Beyond; Redox Systems Regulating Lung Physiology and Disease.
E. Elko (2019)
Inactivation of the PtdIns(4)P phosphatase Sac1 at the Golgi by H2O2 produced via Ca2+‐dependent Duox in EGF‐stimulated cells
Sujin Park (2019)
Nrf2 in alcoholic liver disease
J. Sun (2018)
Modulators of Redox Metabolism in Head and Neck Cancer.
Xiaofei Chen (2017)
Oxidative stress in malaria and artemisinin combination therapy: Pros and Cons
R. Kavishe (2017)
Explorer Transcriptional regulation of the AP-1 and Nrf 2 target gene sulfiredoxin
Francesc X Soriano (2017)
Deciphering the molecular signaling cascade in rotenone-mediated neuronal death
Y. Yap (2017)
Hydrogen peroxide – production, fate and role in redox signaling of tumor cells
Claudia Lennicke (2015)
Oxidative stress response and Nrf 2 signaling in aging
Hongqiao Zhang (2015)
The antioxidant function of sestrins is mediated by promotion of autophagic degradation of Keap1 and Nrf2 activation and by inhibition of mTORC1.
S. Rhee (2015)
Oxidative stress response and Nrf2 signaling in aging.
H. Zhang (2015)
The aryl hydrocarbon receptor suppresses cigarette-smoke-induced oxidative stress in association with dioxin response element (DRE)-independent regulation of sulfiredoxin 1.
Miles Sarill (2015)
The functional role of peroxiredoxin 3 in reactive oxygen species, apoptosis, and chemoresistance of cancer cells
Lianqin Li (2015)
Les peroxydases à thiol, relais dans la signalisation cellulaire redox associée au peroxyde d’hydrogène : mécanismes moléculaires responsables de la spécificité de l’activation du facteur de transcription Yap1 chez Saccharomyces cerevisiae
Antoine Bersweiler (2015)
Peroxiredoxins as biomarkers of oxidative stress.
Rebecca A. Poynton (2014)
Role of sulfiredoxin in systemic diseases influenced by oxidative stress
Asha Ramesh (2014)
Atmospheric pressure gas plasma-induced colorectal cancer cell death is mediated by Nox2-ASK1 apoptosis pathways and oxidative stress is mitigated by Srx-Nrf2 anti-oxidant system.
M. Ishaq (2014)
Sestrins activate Nrf2 by promoting p62-dependent autophagic degradation of Keap1 and prevent oxidative liver damage.
Soo Han Bae (2013)
Emerging roles of Nrf2 and phase II antioxidant enzymes in neuroprotection
Meijuan Zhang (2013)
Cellular‐signaling pathways unveil the carcinogenic potential of chemicals
G. Hendriks (2013)
Dithiol-based Compounds Maintain Expression of Antioxidant Protein Peroxiredoxin 1 That Counteracts Toxicity of Mutant Huntingtin*
Andrea Pitts (2012)
Peroxiredoxin III and sulfiredoxin together protect mice from pyrazole-induced oxidative liver injury.
Soo Han Bae (2012)
Mitochondrial thiols in antioxidant protection and redox signaling: distinct roles for glutathionylation and other thiol modifications.
M. Murphy (2012)
Inactivation of a peroxiredoxin by hydrogen peroxide is critical for thioredoxin-mediated repair of oxidized proteins and cell survival.
Alison M. Day (2012)
Mitochondrial thiols in the regulation of cell death pathways.
F. Yin (2012)
Role of sulfiredoxin as a regulator of peroxiredoxin function and regulation of its expression.
W. Jeong (2012)
See more
Semantic Scholar Logo Some data provided by SemanticScholar