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Oxidative Stress Regulation by Reactive Cysteine Persulfides in Inflammation

  • Tomohiro SawaEmail author
Chapter

Abstract

Reactive oxygen species (ROS) such as superoxide anion radical and hydrogen peroxide are ubiquitously generated during metabolisms of aerobic organisms. Excess production of ROS due to imbalance between formation and removal of ROS by the antioxidant system causes oxidative stress-related tissue damage. Therefore reinforcement of antioxidant capacity has been considered as a beneficial approach for treatment and prevention of chronic inflammatory disorders where ROS production is persistently activated. Cysteine persulfide was recently identified regarding its endogenous formation in mammalian cells. Biochemical analyses revealed that cysteine persulfide and its derivatives such as glutathione persulfide act as a strong antioxidant in cells. Better understanding of the antioxidant actions of cysteine persulfides in chronic inflammation-associated diseases is a necessary basis to develop new strategies for disease treatment and prevention by modulating the process of oxidative stress.

Keywords

Reactive oxygen species Oxidative stress Inflammatory mediators Antioxidants Cysteine persulfide Cellular senescence 

References

  1. Ahmed KA, Sawa T, Ihara H et al (2012) Regulation by mitochondrial superoxide and NADPH oxidase of cellular formation of nitrated cyclic GMP: potential implications for ROS signalling. Biochem J 441:719–730CrossRefPubMedGoogle Scholar
  2. Akaike T, Okamoto S, Sawa T et al (2003) 8-Nitroguanosine formation in viral pneumonia and its implication for pathogenesis. Proc Natl Acad Sci U S A 100:685–690CrossRefPubMedPubMedCentralGoogle Scholar
  3. Edwards JO, Pearson RG (1962) The factors determining nucleophilic reactivities. J Am Chem Soc 84:16–24CrossRefGoogle Scholar
  4. Fujii S, Sawa T, Ihara H et al (2010) The critical role of nitric oxide signaling, via protein S-guanylation and nitrated cyclic GMP, in the antioxidant adaptive response. J Biol Chem 285:23970–23984CrossRefPubMedPubMedCentralGoogle Scholar
  5. Halliwell B (2007) Biochemistry of oxidative stress. Biochem Soc Trans 35:1147–1150CrossRefPubMedGoogle Scholar
  6. Hayflick L (1965) The limited in vitro lifetime of human diploid cell strains. Exp Cell Res 37:614–636CrossRefPubMedGoogle Scholar
  7. Holland R, Hawkins AE, Eggler AL et al (2008) Prospective type 1 and type 2 disulfides of Keap1 protein. Chem Res Toxicol 21:2051–2060CrossRefPubMedPubMedCentralGoogle Scholar
  8. Honda K, Yamada N, Yoshida R et al (2015) 8-Mercapto-cyclic GMP mediates hydrogen sulfide-induced stomatal closure in Arabidopsis. Plant Cell Physiol 56:1481–1489CrossRefPubMedGoogle Scholar
  9. Ida T, Sawa T, Ihara H et al (2014) Reactive cysteine persulfides and S-polythiolation regulate oxidative stress and redox signaling. Proc Natl Acad Sci U S A 111:7606–7611CrossRefPubMedPubMedCentralGoogle Scholar
  10. Jurk D, Wilson C, Passos JF et al (2013) Chronic inflammation induces telomere dysfunction and accelerates ageing in mice. Nat Commun 2:4172Google Scholar
  11. Kuilman T, Michaloglou C, Vredeveld LC et al (2008) Oncogene-induced senescence relayed by an interleukin-dependent inflammatory network. Cell 133:1019–1031CrossRefPubMedGoogle Scholar
  12. Miranda KM, Wink DA (2014) Persulfides and the cellular thiol landscape. Proc Natl Acad Sci U S A 111:7505–7506CrossRefPubMedPubMedCentralGoogle Scholar
  13. Niki E (2010) Assessment of antioxidant capacity in vitro and in vivo. Free Radic Biol Med 49:503–515CrossRefPubMedGoogle Scholar
  14. Nishida M, Sawa T, Kitajima N et al (2012) Hydrogen sulfide anion regulates redox signaling via electrophile sulfhydration. Nat Chem Biol 8:714–724CrossRefPubMedPubMedCentralGoogle Scholar
  15. Ono K, Akaike T, Sawa T et al (2014) Redox chemistry and chemical biology of H2S, hydropersulfides, and derived species: implications of their possible biological activity and utility. Free Radic Biol Med 77:82–94CrossRefPubMedGoogle Scholar
  16. Passos JF, Nelson G, Wang C et al (2010) Feedback between p21 and reactive oxygen production is necessary for cell senescence. Mol Syst Biol 6:347CrossRefPubMedPubMedCentralGoogle Scholar
  17. Rahaman MM, Sawa T, Ahtesham AK et al (2014) S-Guanylation proteomics for redox-based mitochondrial signaling. Antioxid Redox Signal 20:295–307CrossRefPubMedPubMedCentralGoogle Scholar
  18. Rodier F, Campisi J (2011) Four faces of cellular senescence. J Cell Biol 192:547–556CrossRefPubMedPubMedCentralGoogle Scholar
  19. Sawa T, Tatemichi M, Akaike T et al (2006) Analysis of urinary 8-nitroguanine, a marker of nitrative nucleic acid damage, by high-performance liquid chromatography-electrochemical detection coupled with immunoaffinity purification: association with cigarette smoking. Free Radic Biol Med 40:711–720CrossRefPubMedGoogle Scholar
  20. Sawa T, Zaki MH, Okamoto T et al (2007) Protein S-guanylation by the biological signal 8-nitroguanosine 3′,5′-cyclic monophosphate. Nat Chem Biol 3:727–735CrossRefPubMedGoogle Scholar
  21. Starkov AA (2008) The role of mitochondria in reactive oxygen species metabolism and signaling. Ann NY Acad Sci 1147:37–52CrossRefPubMedPubMedCentralGoogle Scholar
  22. Sumimoto H (2008) Structure, regulation and evolution of Nox-family NADPH oxidases that produce reactive oxygen species. FEBS J 275:3249–3277CrossRefPubMedGoogle Scholar
  23. Terasaki Y, Akuta T, Terasaki M et al (2006) Guanine nitration in idiopathic pulmonary fibrosis and its implication for carcinogenesis. Am J Respir Crit Care Med 174:665–673CrossRefPubMedGoogle Scholar
  24. Uruno A, Motohashi H (2011) The Keap1-Nrf2 system as an in vivo sensor for electrophiles. Nitric Oxide 25:153–160CrossRefPubMedGoogle Scholar
  25. Wu LL, Chiou CC, Chang PY et al (2004) Urinary 8-OHdG: a marker of oxidative stress to DNA and a risk factor for cancer, atherosclerosis and diabetics. Clin Chim Acta 339:1–9CrossRefPubMedGoogle Scholar
  26. Zaki MH, Fujii S, Okamoto T et al (2009) Cytoprotective function of heme oxygenase 1 induced by a nitrated cyclic nucleotide formed during murine salmonellosis. J Immunol 182:3746–3756CrossRefPubMedGoogle Scholar

Copyright information

© Springer Japan 2016

Authors and Affiliations

  1. 1.Department of Microbiology, Graduate School of Medical SciencesKumamoto UniversityChuo-kuJapan
  2. 2.PRESTOJapan Science and Technology AgencyKawaguchiJapan

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