Singlet oxygen species and systemic lupus erythematosus: a brief review

References

• Dirks, R. C.; Faiman, M. D. Free Radical Formation and Lipid Peroxidation in Rat and Mouse Cerebral Cortex Slices Exposed to High Oxygen Pressure. Brain Res. 1982, 248(1982), 355–360.
   PubMedGoogle Scholar
• Harabin, A. L.; Braisted, J. C.; Flynn, E. T. Response of Antioxidant Enzymes to Intermittent and Continuous Hyperbaric Oxygen. J. Appl. Physiol. 1990, 69(1), 328–335. DOI: 10.1152/jappl.1990.69.1.328.
   PubMed Web of Science ®Google Scholar
• Beckman, J. S.; Koppenol, W. H. Nitric Oxide, Superoxide, and Peroxynitrite: The Good, the Bad, and Ugly. Am. J. Physiol. 1996, 271, C1424–C1437. DOI: 10.1152/ajpcell.1996.271.5.C1424.
   PubMed Web of Science ®Google Scholar
• Agarwal, P.; Ahsan, H.; Ahmad, R. Studies of Human Hemoglobin Modified with Peroxynitrite: A Cytotoxic Metabolite Generated in Numerous Disorders. Int. J. Health Sciences. 2018, 12(6), 30–35.
   Google Scholar
• Ahmad, R.; Alam, K.; Ali, R. Antigen Binding Characteristics of Antibodies against Hydroxyl Radical Modified Thymidine Monophosphate. Immunol. Lett. 2000, 71, 111–115. DOI: 10.1016/S0165-2478(99)00177-7.
   PubMed Web of Science ®Google Scholar
• Miller, D. M.; Buettner, G. R.; Aust, S. D. Transition Metals as Catalysts of “Autoxidation” Reactions. Free Radic Biol Med. 1990, 8(1), 95–108.
   PubMed Web of Science ®Google Scholar
• Valko, M.; Morris, H.; Cronin, M. T. Metals, Toxicity and Oxidative Stress. Curr. Med. Chem. 2005, 12(10), 1161–1208.
   PubMed Web of Science ®Google Scholar
• Puppo, A.; Halliwell, B. Formation of Hydroxyl Radicals from Hydrogen Peroxide in the Presence of Iron. Is Hemoglobin a Biological Fenton Reagent. Biochem J. 1988, 249, 185–190. DOI: 10.1042/bj2490185.
   PubMed Web of Science ®Google Scholar
• Ogilby, P. R.;. Singlet Oxygen: There Is Indeed Something New under the Sun. Chem. Soc. Rev. 2010, 39(8), 3181–3209. DOI: 10.1039/b926014p.
   PubMed Web of Science ®Google Scholar
• Rasheed, Z.; Ahmad, R.; Ali, R. Structure and Immunological Function of Oxidized Albumin in Lung Cancer Patients: Its Potential Role as a Biomarker of Elevated Oxidative Stress. Brit. J. Biomed. Sci. 2009, 66(2), 67–73. DOI: 10.1080/09674845.2009.11730247.
   PubMed Web of Science ®Google Scholar
• Passos, J. F.; Von Zglinicki, T. Oxygen Free Radicals in Cell Senescence: Are They Signal Transducers? Free Radic. Res. 2006, 40, 1277–1283. DOI: 10.1080/10715760600917151.
   PubMed Web of Science ®Google Scholar
• Lu, T.; Finkel, T. Free Radicals and Senescence. Exp. Cell Res. 2008, 314(9), 1918–1922. DOI: 10.1016/j.yexcr.2008.01.011.
   PubMed Web of Science ®Google Scholar
• Percival M. Antioxidants. Clinical Nutrition Insights. Copyright © 1996 Advanced Nutrition Publications, Inc., Revised 1998, pp 1–4.
   Google Scholar
• Tiwari, A. K.;. Imbalance in Antioxidant Defense and Human Diseases: Multiple Approach of Natural Antioxidants Therapy. Current Science. 2001, 81(9), 212–218.
   Web of Science ®Google Scholar
• Alberti, M. N.; Orfanopoulos, M. Unraveling the Mechanism of the Singlet Oxygen Ene Reaction: Recent Computational and Experimental Approaches. Chem. Eur. J. 2010, 16(31), 9414–9421. DOI: 10.1002/chem.201000752.
   PubMed Web of Science ®Google Scholar
• Schweitzer, C.; Schmidt, R. Physical Mechanisms of Generation and Deactivation of Singlet Oxygen. Chem. Rev. 2003, 103(5), 1685–1757. DOI: 10.1021/cr010371d.
   PubMed Web of Science ®Google Scholar
• Clennan, E. L.; Pace, A. Advances in Singlet Oxygen Chemistry. Tetrahedron. 2005, 61(28), 6665–6691. DOI: 10.1016/j.tet.2005.04.017.
   Web of Science ®Google Scholar
• Sies, H.;. Biochemistry of Oxidative Stress. Angew. Chem. Int. Ed. Eng. 1986, 25, 1058–1071. DOI: 10.1002/(ISSN)1521-3773.
   Web of Science ®Google Scholar
• Krinsky, N. I.;. Singlet Oxygen in Biological Systems. Trends Biochem. Sci. 1977, 2, 35–38.
   Web of Science ®Google Scholar
• Foote CS. Photosensitized oxygenations and the role of singlet oxygen. Acc. Chem. Res., 1968, 1(4), 104–110.
   Google Scholar
• Joshi, P. C.;. Comparison Of The DNA-damaging Property Of Photosensitized Riboflavin Via Singlet Oxygen (‘0,) And Superoxide Radical Mechanisms. Toxicol. Lett. 1985, 26, 211–217. DOI: 10.1016/0378-4274(85)90169-9.
   PubMed Web of Science ®Google Scholar
• Ito, T.;. Cellular and Subcellular Mechanisms of PDT Action. Photochem. Photobiol. 1978, 28, 493–508.
   PubMed Web of Science ®Google Scholar
• Epe, B.; Hegler, J.; Wild, D. Singlet Oxygen as the Ultimately Reactive Species in Salmonella Typhimurium DNA Damage Induced by Methylene Blue/Visible Light. Carcinogenesis. 1989, 10, 2019–2024. DOI: 10.1093/carcin/10.11.2019.
   PubMed Web of Science ®Google Scholar
• Wasserman HH, Scheffer JR. Singlet oxygen reactions from photoperoxides. J Am Chem Soc. 1967, 89(12), 3073–3075.
   Google Scholar
• Halliwell, B.;. Free Radicals, Antioxidants, and Human Disease: Curiosity, Cause, or Consequence? . Lancet. 1994, 344, 721–724.
   PubMed Web of Science ®Google Scholar
• Halliwell B, Gutteridge JM. Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem J. 1984, 219(1), 1–14. doi: 10.1042/bj2190001.
   Google Scholar
• Krinsky NI. Singlet oxygen in biological systems. Trend Biochem Sci, 1977, 2(2), 35–38.
   Google Scholar
• Kearns, D. R.;. Physical and Chemical Properties of Singlet Molecular Oxygen. Chem. Rev. 1971, 71, 395–427. DOI: 10.1021/cr60272a004.
   Web of Science ®Google Scholar
• Kuimova, M. K.; Yahioglu, G.; Ogilby, P. R. Singlet Oxygen in a Cell: Spatiallydependent Lifetimes and Quenching Rate Constants. J. AmChem. Soc. 2009, 131, 332–340. DOI: 10.1021/ja807484b.
   Google Scholar
• Frimer, A. A.;. Singlet Oxygen Volume I, Physical-Chemical Aspects; CRC press: Boca Raton, Fl, 1985; pp 4–7.
   Google Scholar
• Kussmaul, L.; Hirst, J. The Mechanism of Superoxide Productionby NADH: Ubiquinone Oxidoreductase (Complex I) from Bovine Heart Mitochondria. Proc. Natl. Acad. Sci. USA. 2006, 103, 7607–7612. DOI: 10.1073/pnas.0510977103.
   PubMed Web of Science ®Google Scholar
• Mulliken, R. S.;. Interpretation of the Atmospheric Oxygen Bands; Electronic Levels of the Oxygen Molecule. Nature. 1928, 122, 505. DOI: 10.1038/122505a0.
   Google Scholar
• Foldes, T.; Cermak, P.; Macko, M.; Veis, P.; Macko, P. Cavity Ring-Down Spectroscopy of Singlet Oxygen Generated in Microwave Plasma. Chem. Phys. Lett. 2009, 467(4–6), 233–236. DOI: 10.1016/j.cplett.2008.11.040.
   Web of Science ®Google Scholar
• Gupta, A.; Wani, A.; Joshi, A.; Ahsan, H.; Ahmad, R. Characterization of Human Serum Albumin G Modified with Singlet Oxygen. Ind. J. Clin. Biochem. 2014, 29(1), 63–68. DOI: 10.1007/s12291-013-0333-0.
   PubMedGoogle Scholar
• Khan, F.; Khan, F.; Siddiqui, A. A.; Ali, R. Plasmid DNA Acquires Immunogenicity on Exposure to Singlet Oxygen. Biochemistry (Mosc). 2006, 71(8), 871–878.
   PubMed Web of Science ®Google Scholar
• Khan, F.; Khan, F.; Ali, R. Immunogenicity of DNA Modified by Singlet Oxygen: Implications in Systemic Lupus Erythematosus and Cancer. Biotechnol. Appl. Biochem. Feb 2007, 46(Pt 2), 97–103. DOI: 10.1042/BA20060113.
   PubMedGoogle Scholar
• Rasheed, Z.; Ahmad, R.; Sheikh, N.; Ali, R. Role of Reactive Oxygen Species Damaged Human Serum Albumin in the Etiopathogenesis of Systemic Lupus Erythematosus. Autoimmunity. 2007, 40(7), 512–520. DOI: 10.1080/08916930701574331.
   PubMed Web of Science ®Google Scholar
• Khan, S.; Alam, R.; Moinuddin, A. A. Oxygen Free Radical Modified DNA: Implications in the Etiopathogenesis of Systemic Lupus Erythematosus. Indian J. Clin. Biochem. 2009, 24(2), 123–130. DOI: 10.1007/s12291-009-0023-0.
   PubMedGoogle Scholar