Free Radicals: Properties, Sources, Targets, and Their Implication in Various Diseases

Indian Journal of Clinical Biochemistry

Volumn 30, Issue 1, 2015, Pages 11-26

  Phaniendra, Alugoju ^a   Jestadi, Dinesh Babu ^a   Periyasamy, Latha ^a  

^a PONDICHERRY UNIVERSITY   (India)

Author keywords

Free radicals; Oxidative stress; Reactive nitrogen species (RNS); Reactive oxygen species (ROS)

Indexed keywords

DNA; FREE RADICAL; HYDROGEN PEROXIDE; HYDROXYL RADICAL; HYPOCHLOROUS ACID; LIPID; NITRIC OXIDE; NITROGEN DERIVATIVE; OZONE; PEROXY RADICAL; PEROXYNITRITE; PROTEIN; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; RNA; SINGLET OXYGEN; SUPEROXIDE;

ALZHEIMER DISEASE; ASTHMA; ATHEROSCLEROSIS; BLADDER CANCER; BREAST CANCER; CARDIOVASCULAR DISEASE; CATARACT; COLORECTAL CANCER; DEGENERATIVE DISEASE; DIABETES MELLITUS; ENDOPLASMIC RETICULUM; FENTON REACTION; HUMAN; HYPERTENSION; LUNG CANCER; MITOCHONDRION; MULTIPLE SCLEROSIS; OXIDATIVE STRESS; OXYGEN CONSUMPTION; PARKINSON DISEASE; PEROXISOME; PHYSICAL DISEASE; PROSTATE CANCER; REVIEW; RHEUMATOID ARTHRITIS;

NICOTIANA TABACUM;

EID: 84961291449     PISSN: 09701915     EISSN: 09740422     Source Type: Journal    
DOI: 10.1007/s12291-014-0446-0     Document Type: Review

References (209)

1. Gomberg M. An Incidence of Trivalent Carbon Trimethylphenyl. J Am Chem Soc. 1900;22:757–71.
2. Gerschman R, Gilbert DL, Nye SW, Dwyer P, Fenn WO. Oxygen poisoning and x-irradiation-A mechanism in common. Science. 1954;119:623–6.
3. Commoner B, Townsend J, Pake GE. Free radicals in biological materials. Nature. 1954;174(4432):689–91.
4. McCord JM, Fridovich I. Superoxide dismutase an enzymatic function for erythrocuprein (chemocuprein). J Biol Chem. 1969;244(22):6049–55.
5. Loschen G, Flohe L, chance B. Respiratory chain linked H O production in pigeon heart mitochondria. FEBS Lett. 1971;18(2):261–4.
6. Nohl H, Hegner D. Do mitochondria produce oxygen radicals in vivo? Eur J Biochem. 1978;82:563–7.
7. Mittal CK, Murad F. Activation of guanylate cyclase by superoxide-dismutase and hydroxyl radical-Physiological regulator of guanosine 3′,5′-monophosphate formation. Proc Natl Acad Sci USA. 1977;74(10):4360–4.
8. Halliwell B, Gutteridge JMC. Free radicals in biology and medicine. 2nd ed. Oxford: Clarendon Press; 1989.
9. Mukherji SM, Singh SP. Reaction mechanism in organic chemistry. Madras: Macmillan IndiaPress; 1986.
10. Pham-Huy LA, Hua He, Pham-Huy C. Free Radicals, Antioxidants in Disease and Health. Int J Biomed Sci. 2008;4(2):89–96.
11. Valko M, Leibfritz D, Moncola J, Cronin MT, Mazura M, Telser J. Review Free radicals and antioxidants in normal physiological functions and human disease. Int J Biochem Cell Biol. 2007;39(1):44–84.
12. Nordberg J, Arner EJ. Reactive oxygen species, antioxidants, and the mammalian Thioredoxin system. Free Radical Biol Med. 2001;31(11):1287–312.
13. Yla-Herttuala S. Oxidized LDL and atherogenesis. Ann N Y Acad Sci. 1999;874:134–7.
14. Stadtman ER, Levine RL. Protein oxidation. Ann N Y Acad Sci. 2000;899:191–208.
15. Marnett LJ. Oxyradicals and DNA damage. Carcinogenesis. 2000;21(3):361–70.
16. Kohen R, Nyska A. Invited review Oxidation of Biological Systems: Oxidative Stress Phenomena, Antioxidants, Redox Reactions, and Methods for Their Quantification. Toxicol Pathol. 2002;30(6):620–50.
17. Halliwell B. Free Radicals and other reactive species in disease. Nature Encyclopedia of life sciences. 2001. p. 1–7.
18. Genestra M. Oxyl radicals, redox-sensitive signalling cascades and antioxidants. Review Cell Signal. 2007;19(9):1807–19.
19. Mugoni V, Santoro MM. Manipulating redox signaling to block tumor angiogenesis, research directions in tumor angiogenesis, Dr. Jianyuan Chai (Ed.), ISBN: 978-953-51-0963-1, InTech, 2013. doi: 10.5772/54593.
20. Michelson AM, McCord JM, Fridovich I. Superoxide and Superoxide Dismutases. London: Academic Press; 1977. p. 320.
21. Kuppusamy P, Zweier JL. Characterization of free radical generation by xanthine oxidase. Evidence for hydroxyl radical generation. J Biol Chem. 1989;264(17):9880–4.
22. Kontos HA, Wei EP, Ellis EF, Jenkins LW, Povlishock JT, Rowe GT, et al. Appearance of superoxide anion radical in cerebral extracellular space during increased prostaglandin synthesis in cats. Circ Res. 1985;57(1):142–51.
23. McIntyre M, Bohr DF, Dominiczak AF. Endothelial function in hypertension. Hypertension. 1999;34:539–45.
24. Bielski BHJ, Cabelli DE. Superoxide and hydroxyl radical chemistry in aqueous solution. Active Oxygen in Chemistry. 1996;66–104.
25. Bielski BHJ, Cabelli BH, Arudi RL, Ross AB. Reactivity of RO2/O2. Radicals in aqueous solution. J Phys Chem Ref Data. 1985;14:1041–100.
26. Bedwell S, Dean RT, Jessup W. The action of defined oxygen centred free radicals on human low density lipoprotein. Biochem J. 1989;262(3):707–12.
27. Halliwell B. Oxidants and human disease: some new concepts. FASEB J. 1987;1(5):358–64.
28. Fenton HJH. Oxidation of tartaric acid in the presence of iron. J Chem Soc Trans. 1894;65:899–910.
29. Haber F, Weiss J. The catalytic decomposition of hydrogen peroxide by iron salts. Proc R Soc London (A). 1934;147:332–51.
30. 2˙: the forgotten radical. DNA Cell Biol. 2002;21:251–7.
31. Cerruti PA. Pro-oxidant states and tumor activation. Science. 1985;227:375–81.
32. Halliwell B, Clement MV, Long LH. Hydrogen peroxide in the human body. FEBS Lett. 2000;486(1):10–3.
33. Mates JM, Perez-Gomez C, Nunez de Castro I. Antioxidant enzymes and human diseases. Clin Biochem. 1999;32(8):595–603.
34. Chae HZ, Kang SW, Rhee SG. Isoforms of mammalian peroxiredoxin that reduce peroxides in presence of thioredoxin. Methods Enzymol. 1999;300:219–26.
35. Hojo Y, Okado A, kawazoe S, Mizutani T. In vivo singlet-oxygen generation in blood of chromium(VI)-treated mice an electron spin resonance spin-trapping study. Biol Trace Elem Res. 2000;76(1):85–93.
36. Agnez-Lima LF, Melo JT, Silva AE, Oliveira AH, Timoteo AR, Lima-Bessa KM, et al. Review DNA damage by singlet oxygen and cellular protective mechanisms. Mutat Res. 2012;751(1):1–14.
37. Hampton MB, Kettle AJ, Winterbourn CC. Inside the neutrophil phagosome: oxidants, myeloperoxidase, and bacterial killing. Blood. 1998;92(9):3007–17.
38. Kanovasky JR. Singlet oxygen production by biological systems. Chem Biol Interact. 1989;70(1–2):1–28.
39. Chan HWS. Singlet oxygen analogs in biological systems: coupled oxygenation of 1,3-dienes by soybean lipoxidase. J Am Chem Soc. 1971;93(9):2357–8.
40. Hayaishi O, Nozaki M. Nature and mechanisms of oxygenases. Science. 1969;164:389–96.
41. Kanofsky JR. Singlet oxygen production by lactoperoxidase. J Biol Chem. 1983;258(10):5991–3.
42. Sies H, Menck CF. Singlet oxygen induced DNA damage. Mutat Res. 1992;275:367–75.
43. Lerner RA, Eschenmoser A. Ozone in biology. Proc Natl Acad Sci USA. 2003;100(6):3013–5.
44. Goldstein BD, Lodi C, Collinson C, Balchum OJ. Ozone and lipid peroxidation. Arch Environ Heath. 1969;18:631–5.
45. Freeman BA, Mudd JB. Reaction of ozone with sulfhydryls of human erythrocytes. Arch Biochem Biophys. 1981;208(1):212–20.
46. Mudd JB, Leavitt R, Ongun A, McManus TT. Reaction of ozone with amino acids and proteins. Atmos Environ. 1969;3:669–81.
47. Mustafa MG. Biochemical Basis of Ozone Toxicity. Free Radical Biol Med. 1990;9:245–65.
48. Fetner RH. Ozone induced chromosome breakage in human cell culture. Nature. 1962;194:793–4.
49. Winterbourn CC, Kettle AJ. Biomarkers of myeloperoxidase-derived hypochlorous acid. Free Radic Biol Med. 2000;29(5):403–9.
50. Albrich JM, McCarthy CA, Hurst JK. Biological reactivity of hypochlorous acid: implications for microbicidal mechanisms of leukocyte myeloperoxidase. Proc Natl Acad Sci USA. 1981;78(1):210–4.
51. Winterbourn CC. Comparative reactivities of various biological compounds with myeloperoxidase-hydrogen peroxide-chloride, and similarity of the oxidant to hypochlorite. Biochim Biophys Acta. 1985;840(2):204–10.
52. Prutz WA. Hypochlorous acid interactions with thiols, nucleotides, DNA, and other biological substrates. Arch Biochem Biophys. 1996;332(1):110–20.
53. Andrew PJ, Mayer B. Enzymatic function of nitric oxide synthases. Cardiovasc Res. 1999;43(3):521–31.
54. Chiueh CC. Neuroprotective properties of nitric oxide. Ann N Y Acad Sci. 1999;890:301–11.
55. Ignarro LJ, Buga GM, Wood KS, Byrns RE, Chandhuri G. Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide. Proc Natl Acad Sci USA. 1987;84:9265–9.
56. Wink DA, Mitchell JB. Chemical biology of nitric oxide: insights into regulatory, cytotoxic, and cytoprotective mechanisms of nitric oxide. Free Radic Biol Med. 1998;25(4–5):434–56.
57. Stamler JS. Redox signaling: nitrosylation and related target interactions of nitric oxide. Cell. 1994;78(6):931–6.
58. Koshland DE Jr. The molecule of the year. Science. 1992;258(5090):1861.
59. Beckman JS, Koppenol WH. Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly. Am J Physiol. 1996;271:C1424–37.
60. Douki H, Cadet J. Peroxynitrite mediated oxidation of purine bases of nucleosides and isolated DNA. Free Rad Res. 1996;24(5):369–80.
61. Ischiropoulos H, Al-Mehdi AB. Peroxynitrite mediated oxidative protein modifications. FEBS Lett. 1995;364(3):279–82.
62. Czapski G, Goldstein S. The role of the reactions of NO with superoxide and oxygen in biological systems: a kinetic approach. Free Radic Biol Med. 1995;19(6):785–94.
63. Finkel T, Holbrook NJ. Oxidants, oxidative stress and the biology of ageing. Nature. 2000;408:239–47.
64. Starkov AA. The role of mitochondria in reactive oxygen species metabolism and signaling. Ann NY Acad Sci. 2008;1147:37–52.
65. Giorgio M, Migliaccio E, Orsini F, Paolucci D, Moroni M, Contursi C, et al. Electron transfer between cytochrome c and p66Shc generates reactive oxygen species that trigger mitochondrial apoptosis. Cell. 2005;122(2):221–33.
66. De Duve C, Bauduhuin P. peroxisomes (microbodies and related particles). Physiol Rev. 1966;46:323–57.
67. Schrader M, Fahimi HD. Review Peroxisomes and oxidative stress. Biochim Biophys Acta. 2006;1763(12):1755–66.
68. Cheeseman KH, Slater TF. An introduction to free radical biochemistry. Br Med Bull. 1993;49(3):481–93.
69. Gross E, Sevier CS, Heldman N, Vitu E, Bentzur M, Kaiser CA, et al. Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p. Proc Nat Acad Sci USA. 2006;103(2):299–304.
70. Droge W. Review Free radicals in the physiological control of cell function. Physiol Rev. 2002;82(1):47–95.
71. Halliwell B, Gutteridge JM. Free radicals in biology and medicine, vol. Third edition. Midsomer Norton: Oxford University Press; 1999.
72. Dizdaroglu M, Jaruga P, Birincioglu M, Rodriguez H. Free radical-induced damage to DNA: mechanisms and measurement. Free Radical Biol Med. 2002;32(11):1102–15.
73. Barja G. The flux of free radical attack through mitochondrial DNA is related to aging rate. Aging (Milano). 2000;12(5):342–55.
74. Hiraku Y, Kawanishi S, Ichinose T, Murata M. The role of iNOS-mediated DNA damage in infection- and asbestos-induced carcinogenesis. Ann NY Acad Sci. 2010;1203:15–22.
75. Yermilov V, Rubio J, Ohshima H. Formation of 8-nitroguanine in DNA treated with peroxynitrite in vitro and its rapid removal from DNA by depurination. FEBS Lett. 1995;376(3):207–10.
76. Loeb LA, Preston BD. Mutagenesis by apurinic/apyrimidinic sites. Annu Rev Genet. 1986;20:201–30.
77. Hofer T, Badouard C, Bajak E, Ravanat JL, Mattsson A, Cotgreave IA. Hydrogen peroxide causes greater oxidation in cellular RNA than in DNA. Biol Chem. 2005;386(4):333–7.
78. Abe T, Tohgi H, Isobe C, Murata T, Sato C. Remarkable increase in the concentration of 8-hydroxyguanosine in cerebrospinal fluid from patients with Alzheimer’s disease. J Neurosci Res. 2002;70(3):447–50.
79. Kikuchi A, Takeda A, Onodera H, Kimpara T, Hisanaga K, Sato N, et al. Systemic increase of oxidative nucleic acid damage in Parkinson’s disease and multiple system atrophy. Neurobiol Dis. 2002;9(2):244–8.
80. Martinet W, de Meyer GR, Herman AG, Kockx MM. Reactive oxygen species induce RNA damage in human atherosclerosis. Eur J Clin Invest. 2004;34(5):323–7.
81. Broedbaek K, Poulsen HE, Weimann A, Kom GD, Schwedhelm E, Nielsen P, et al. Urinary excretion of biomarkers of oxidatively damaged DNA and RNA in hereditary hemochromatosis. Free Radical Biol Med. 2009;47(8):1230–3.
82. Tateyama M, Takeda A, Onodera Y, Matsuzaki M, Hasegawa T, Nunomura A, et al. Oxidative stress and predominant Abeta 42 (43) deposition in myopathies with rimmed vacuoles. Acta Neuropathol. 2003;105(6):581–5.
83. Siems WG, Grune T, Esterbauer H. 4-Hydroxynonenal formation during ischemia and reperfusion of rat small-intestine. Life Sci. 1995;57(8):785–9.
84. Bast A. Oxidative stress and calcium homeostasis. In: Halliwell B, Aruoma OI, editors. DNA and free radicals. London: Ellis Horwood; 1993. p. 95–108.
85. Marnett LJ. Lipid peroxidation—DNA damage by malondialdehyde. Mutat Res. 1999;424(1–2):83–95.
86. Aruoma OI. Free radicals, oxidative stress, and antioxidants in human health and disease. J Am Oil chem Soc. 1998;75(2):199–212.
87. Dean RT, Fu S, Stocker R, Davies MJ. Biochemistry and pathology of radical-mediated protein oxidation. Biochem J. 1997;324:1–18.
88. Butterfield DA, Koppal T, Howard B, Subramaniam R, Hall N, Hensley K, et al. Structural and functional changes in proteins induced by free radical-mediated oxidative stress and protective action of the antioxidants N-tert-butyl-alpha-phenylnitrone and vitamin E. Ann N Y Acad Sci. 1998;854:448–62.
89. Brodie E, Reed DJ. Cellular recovery of glyceraldehyde-3-phosphate dehydrogenase activity and thiol status after exposure to hydroperoxide. Arch Biochem Biophys. 1990;276(1):210–2.
90. Pryor WA, Jin X, Squadrito GL. One- and two-electron oxidations of methionine by peroxynitrite. Proc Natl Acad Sci USA. 1994;91(23):11173–7.
91. Berlett BS, Stadtman E. Protein oxidation in aging, disease, and oxidative stress. J Bio Chem. 1997;272(33):20313–6.
92. Kikugawa K, Kato T, Okamoto Y. Damage of amino acids and proteins induced by nitrogen dioxide, a free radical toxin, in air. Free Rad Biol Med. 1994;16(3):373–82.
93. Uchida K, Kawakishi S. 2-oxohistidine as a novel biological marker for oxidatively modified proteins. FEBS Lett. 1993;332(3):208–10.
94. Garrison WM. Reaction mechanisms in radiolysis of peptides, polypeptides, and proteins. Chem Rev. 1987;8792:381–98.
95. Chevion M, Berenshtein E, Stadtman ER. Human studies related to protein oxidation: protein carbonyl content as a marker of damage. Free Radic Res. 2000;33:S99–108.
96. Smith CD, Carney JM, Starke-Reed PE, Oliver CN, Stadtman ER, Floyd RA, et al. Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease. Proc Natl Acad Sci USA. 1991;88(23):10540–3.
97. Floor E, Wetzel MG. Increased protein oxidation in human substantia nigra pars compacta in comparison with basal ganglia and prefrontal cortex measured with an improved dinitrophenylhydrazine assay. J Neurochem. 1998;7091:268–75.
98. Murphy ME, Kehrer JP. Oxidation state of tissue thiol groups and content of protein carbonyl groups in chickens with inherited muscular dystrophy. Biochem J. 1989;260(2):359–64.
99. Garland D, Russell P, Zigler JS. Oxidative modification of lens proteins. Basic Life Sci. 1988;49:347–53.
100. Chapman ML, Rubin BR, Gracy RW. Increased carbonyl content of proteins in synovial fluid from patients with rhematoid arthritis. J Rheumatol. 1989;16(1):15–8.
101. Jones RH, Hothersall JS. The effect of diabetes and dietary ascorbate supplementation on the oxidative modification of rat lens beta L crystallin. Biochem Med Metab Biol. 1993;50(2):197–209.
102. Oliver CN, Ahn BW, Moerman EJ, Goldstein S, Stadtman ER. Age-related changes in oxidized proteins. J Biol Chem. 1987;262(12):5488–91.
103. Gavin JR, Alberti KGMM, Davidson MB, DeFronzo RA, Drash A, Gabbe SG, et al. Report of the expert committee on the diagnosis and classification of diabetes mellitus. Diabetes Care. 1997;20:1183–97.
104. Oberley LW. Free radicals and diabetes. Free Radic Biol Med. 1988;5(2):113–24.
105. Bashan N, Kovsan J, Kachko I, Ovadia H, Rudich A. Positive and negative regulation of insulin signaling by reactive oxygen and nitrogen species. Physiol Rev. 2009;89(1):27–71.
106. Ahmed RG. The physiological and biochemical Effects of diabetes on the balance between oxidative stress and Antioxidant defense system. Med J Islam World Acad Sci. 2005;15(1):31–42.
107. Kwong LK, Sohal RS. Substrate and site specificity of hydrogen peroxide generation in mouse mitochondria. Arch Biochem Biophys. 1998;350(1):118–26.
108. Bajaj S, Khan A. Antioxidants and diabetes. Indian J Endocrinol Metab. 2012;2:S267–71.
109. Pollack M, Leeuwenburgh C. Molecular mechanisms of oxidative stress in aging: free radicals, aging, antioxidants and disease. Elsevier Science B.V. Handbook of Oxidants and Antioxidants in Exercise. 1999;881–923.
110. Rivas-Arancibia S, Guevara-Guzmán R, López-Vidal Y, Rodríguez-Martínez E, Zanardo-Gomes M, Angoa-Pérez M, et al. Oxidative stress caused by ozone exposure induces loss of brain repair in the hippocampus of adult rats. Toxicol Sci. 2010;113(1):187–97.
111. Santiago-López JA, Bautista-Martínez CI, Reyes-Hernandez M, Aguilar-Martínez S, Rivas- Arancibia S. Oxidative stress, progressive damage in the substantia nigra and plasma dopamine oxidation, in rats chronically exposed to ozone. Toxicol Lett. 2010;197(3):193–200.
112. Pan XD, Zhu YG, Lin N, Zhang J, Ye QY, Huang HP, Chen XC. Microglial phagocytosis induced by fibrillar β-amyloid is attenuated by oligomeric β-amyloid: implications for Alzheimer’s disease. Mol Neurodegener. 2011;6(45):1–17.
113. Sevcsik E, Trexler AJ, Dunn JM, Rhoades E. Allostery in a disordered protein: oxidative modifications to α-synuclein act distally to regulate membrane binding. J Am Chem Soc. 2011;133(18):7152–8.
114. Zhao W, Varghese M, Yemul S, Pan Y, Cheng A, Marano P, et al. Peroxisome proliferator activator receptor gamma coactivator-1alpha (PGC-1α) improves motor performance and survival in a mouse model of amyotrophic lateral sclerosis. Mol Neurodegener. 2011;6(1):1–8.
115. Witherick J, Wilkins A, Scolding N, Kemp K. Mechanisms of oxidative damage in multiple sclerosis and a cell therapy approach to treatment. Autoimmune Dis. 2010;1–11.
116. Fisher LJ, Gage FH. Radical directions in Parkinson’s disease. Nat Med. 1995;1(3):201–3.
117. Olivieri S, Conti A, Iannaccone S, Cannistraci CV, Campanella A, Barbariga M, et al. Ceruloplasmin oxidation, a feature of Parkinson’s disease CSF, inhibits ferroxidase activity and promotes cellular iron retention. J Neurosci. 2011;31:18568–77.
118. Butterfield DA, Perluigi M, Sultana R. Oxidative stress in Alzheimer’s disease brain: new insights from redox proteomics. Eur J Pharmacol. 2006;545(1):39–50.
119. Chang Y, Kong Q, Shan X, Tian G, Ilieva H, Cleveland DW, et al. Messenger RNA oxidation occurs early in disease pathogenesis and promotes motor neuron degeneration in ALS. PLoS ONE. 2008;3(8):1–19.
120. Uttara B, Singh AV, Zamboni P, Mahajan RT. Oxidative stress and neurodegenerative diseases. A Review of upstream and downstream antioxidant therapeutic options. Curr Neuropharmacol. 2009;7(1):65–74.
121. Gonsette RE. Neurodegeneration in multiple sclerosis: the role of oxidative stress and excitotoxicity. J Neurol Sci. 2008;274(1–2):48–53.
122. Mitosek-Szewczyk K, Gordon-Krajcer W, Walendzik P, Stelmasiak Z. Free radical peroxidation products in cerebrospinal fluid and serum of patients with multiple sclerosis after glucocorticoid therapy. Folia Neuropathol. 2010;48(2):116–22.
123. Goldstein BD, Witz G. Free radicals and carcinogenesis. Free Radic Res Commum. 1990;11(1–3):3–10.
124. Dreher D, Junod AF. Role of oxygen free radicals in cancer development. Eur J Cancer. 1996;32A(1):30–8.
125. Acuna UM, Wittwer J, Ayers S, Pearce CJ, Oberlies NH, De Blanco EJ. Effects of (5Z)-7-Oxozeaenol on the Oxidative pathway of cancer cells. Anticancer Res. 2012;32(7):2665–71.
126. Cairns RA, Harris I, McCracken S, Mak TW. Cancer cell metabolism. Cold Spring Harb Symp Quant Biol. 2011;76:299–311.
127. Valko M, Leibfritz D, Moncol J, Cronin MT, Mazur M, Telser J. Free radicals and antioxidants in normal hitological functions and human disease. Int J Biochem Cell Biol. 2007;39(1):44–84.
128. Valko M, Izakovic M, Mazur M, Rhodes CJ, Telser J. Role of oxygen radicals in DNA damage and cancer incidence. Mol Cell Biochem. 2004;266(1–2):37–56.
129. Jemal A, Bray F, Center MM, Ferlay J, Ward E, Forman D. Global cancer statistics. CA Cancer J Clin. 2011;61(2):69–90.
130. Blau S, Rubinstein A, Bass P, Singaram C, Kohen R. Differences in the reducing power along the rat GI tract: lower antioxidant capacity of the colon. Mol Cell Biochem. 1999;194(1–2):185–91.
131. Foksinski M, Rozalski R, Guz J, Ruszkowska B, Sztukowska P, Piwowarski M, et al. Urinary excretion of DNA repair products correlates with metabolic rates as well as with maximum life spans of different mammalian species. Free Radic Biol Med. 2004;37(9):1449–54.
132. Haklar G, Sayin-Ozveri E, Yuksel M, Aktan AO, Yalcin AS. Different kinds of reactive oxygen and nitrogen species were detected in colon and breast tumors. Cancer Lett. 2001;165(2):219–24.
133. Guz J, Foksinski M, Siomek A, Gackowski D, Rozalski R, Dziaman T, et al. The relationship between 8-oxo-7,8-dihydro-2-deoxyguanosine level and extent of cytosine methylation in leukocytes DNA of healthy subjects and in patients with colon adenomas and carcinomas. Mutat Res. 2008;640(1–2):170–3.
134. Rainis T, Maor I, Lanir A, Shnizer S, Lavy A. Enhanced oxidative stress and leucocyte activation in neoplastic tissues of the colon. Dig Dis Sci. 2007;52(2):526–30.
135. Suzuki K, Ito Y, Wakai K, Kawado M, Hashimoto S, Toyoshima H, et al. Serum oxidized low-density lipoprotein levels and risk of colorectal cancer: a case-control study nested in the Japan Collaborative Cohort Study. Cancer Epidemiol Biomark Prev. 2004;13(11):1781–7.
136. Murrell TG. Epidemiological and biochemical support for a theory on the cause and prevention of breast cancer. Med Hypotheses. 1991;36(4):389–96.
137. Brown NS, Jones A, Fujiyama C, Harris AL, Bicknell R. Thymidine phosphorylase induces carcinoma cell oxidative stress and promotes secretion of angiogenic factors. Cancer Res. 2000;60(22):6298–302.
138. Sipe HJ Jr, Jordan SJ, Hanna PM, Mason RP. The metabolism of 17 beta-estradiol by lactoperoxidase: a possible source of oxidative stress in breast cancer. Carcinogenesis. 1994;15(11):2637–43.
139. Arnold RS, He J, Remo A, Ritsick D, Yin-Goen Q, Lambeth JD, et al. Nox1 expression determines cellular reactive oxygen and modulates c-fos-induced growth factor, interleukin-8, and Cav-1. Am J Pathol. 2007;171(6):2021–32.
140. Lim SD, Sun C, Lambeth JD, Marshall F, Amin M, Chung L, et al. Increased Nox1 and hydrogen peroxide in prostate cancer. Prostate. 2005;62(2):200–7.
141. Brar SS, Corbin Z, Kennedy TP, Hemendinger R, Thornton L, Bommarius B, et al. NOX5 NAD(P)H oxidase regulates growth and apoptosis in DU 145 prostate cancer cells. Am J Physiol Cell Physiol. 2003;285(2):C353–69.
142. Kumar B, Koul S, Khandrika L, Measchan RB, Koul HK. Oxidative stress is inherent in prostate cancer cells and is required for aggressive phenotype. Cancer Res. 2008;68:1777–85.
143. Veeramani S, Yuan TC, Lin FF, Lin MF. Mitochondrial redox signaling by p66Shc in involved in regulating androgenic growth stimulation of human prostate cancer cell. Oncogene. 2008;27(37):5057–68.
144. WHO World cancer Report 2008. In: Boyle P, Levin B, editors. Lung cancer, 12. Chapter 5.10.
145. Azad N, Rojanasakul Y, Vallyathan V. Inflammation and lung cancer: roles of reactive oxygen/nitrogen species. J Toxicol Environ Health. 2008;11(1):1–15.
146. Jemal A, Bray F, Center MM, Ferlay J, Ward E, Forman D. Global cancer statistics. CA Cancer J Clin. 2011;61(2):69–90.
147. Hoagland LF 4th, Campa MJ, Gottlin EB, Herndon 2nd JE, Patz Jr EF. Haptoglobin and posttranslational glycan-modified derivatives as serum biomarkers for the diagnosis of nonsmall cell lung cancer. Cancer. 2007;110(10):2260–2268.
148. Pastora MD, Nogala A, Molina-Pineloa S, Meléndeza R, Salinasa A, González De la Penaa M, et al. Identification of proteomic signatures associated with lung cancer and COPD. J Proteomics. 2013;89:227–37.
149. Jemal A, Siegel R, Ward E, Murray T, Xu J, Thun MJ. Cancer statistics. CA Cancer J Clin. 2007;57:43–6.
150. Wynder EL, Goldsmith R. The epidemiology of bladder cancer: a second look. Cancer. 1977;40:1246–68.
151. Opanuraks J, Boonla C, Saelim C, Kittikowit W, Sumpatanukul P, Honglertsakula C, et al. Elevated urinary total sialic acid and increased oxidative stress in patients with bladder cancer. Asian Biomedicine. 2010;4(5):703–10.
152. Opanuraks J, Boonla C, Saelim C, Kittikowit W, Sumpatanukul P, Honglertsakula C, Tosukhowong P. Elevated urinary total sialic acid and increased oxidative stress in patients with bladder cancer. Asian Biomedicine. 2010;4(5):703–10.
153. Soini Y, Haapasaari KM, Vaarala MH, Turpeenniemi-Hujanen T, Karja V, Karihtala P. 8-hydroxydeguanosine and nitrotyrosine are prognostic factors in urinary bladder carcinoma. Int J Clin Exp Pathol. 2011;4(3):267–75.
154. Eijan AM, Piccardo I, Riveros MD, Sandes EO, Porcella H, Jasnis MA, et al. Nitric oxide in patients with transitional bladder cancer. J Surg Oncol. 2002;81:203–8.
155. Gecit I, Aslan M, Gunes M, Pirincci N, Esen R, Demir H, et al. Serum prolidase activity, oxidative stress, and nitric oxide levels in patients with bladder cancer. J Cancer Res Clin Oncol. 2012;138(5):739–43.
156. Ellidag HY, Eren E, Aydın O, Akgol E, Yalcınkaya S, Sezer C, et al. Ischemia Modified Albumin Levels and Oxidative Stress in Patients with Bladder Cancer. Asian Pacific J Cancer Prev. 2013;14(5):2759–63.
157. Yılmaz IA, Akçay T, Çakatay U, Telci A, Ataus S, Yalcin V. Relation between bladder cancer and protein oxidation. ˙. Int Urol Nephrol. 2003;35(3):345–50.
158. DeMarchi E, B Faldassari, Bononi A, Wieckowski MR, Pinton P. Oxidative Stress in Cardiovascular Diseases and Obesity: Role of p66Shc and Protein Kinase C Oxidative Medicine and Cellular Longevity. 2013;1-11. Review.
159. Yin Y, Pastrana JL, Li X, Huang X, Mallilankaraman K, Choi ET, et al. Inflammasomes: sensors of metabolic stresses for vascular inflammation. Front Biosci. 2013;18:638–49.
160. Ross R. Atherosclerosis—an inflammatory disease. N Engl J Med. 1999;340(2):115–26.
161. Papaharalambus CA, Griendling KK. Basic mechanisms of oxidative stress and reactive oxygen species in cardiovascular injury. Trends Cardiovasc Med. 2007;17(2):48–54.
162. Rajagopalan S, Meng XP, Ramasamy S, Harrison DG, Galis ZS. Reactive oxygen species produced by macrophage-derived foam cells regulate the activity of vascular matrix metalloproteinases in vitro. Implications for atherosclerotic plaque stability. J Clin Invest. 1996;98(11):2572–9.
163. Barnoya J, Glantz SA. Cardiovascular effects of secondhand smoke: nearly as large as smoking. Circulation. 2005;111(20):2684–98.
164. Yang Z, Ming XF. Recent advances in understanding endothelial dysfunction in atherosclerosis. Clin Med Res. 2006;4(1):53–65.
165. Botto N, Rizza A, Colombo MG, Mazzone AM, Manfredi S, Masetti S, et al. Evidence for DNA damage in patients with coronary artery disease. Mutat Res. 2001;493(1–2):23–30.
166. Ding Z, Liu S, Wang X, Khaidakov M, Dai Y, Mehta JL. Oxidant stress in mitochondrial DNA damage, autophagy and inflammation in atherosclerosis. Sci Rep. 2013;3:1–6.
167. Mercer JR, Cheng KK, Figg N, Gorenne I, Mahmoudi M, Griffin J, et al. DNA damage links mitochondrial dysfunction to atherosclerosis and the metabolic syndrome novelty and significance. Circ Res. 2010;107:1021–31.
168. A global brief on hypertension. World health day 2013. WHO.
169. Zalba G, Jose GS, Moreno MU, Fortuno MA, Fortuno A, Beaumont FJ, et al. Oxidative stress in arterial hypertension role of NAD(P)H oxidase. Hypertension. 2001;38(6):1395–9.
170. Dzau VJ. Tissue angiotensin and pathobiology of vascular disease: a unifying hypothesis. Hypertension. 2001;37:1047–52.
171. Touyz RM. Reactive oxygen species, vascular oxidative stress, and redox signaling in hypertension: what is the clinical significance? Hypertension. 2004;44(3):248–52.
172. Touyz RM. Reactive oxygen species and angiotensin II signaling in vascular cells: implications in cardiovascular disease. Braz J Med Biol Res. 2004;37(8):1263–73.
173. Hashim Z, Zarina S. Osmotic stress induced oxidative damage: Possible mechanism of cataract formation in diabetes. J Diabetes Complicat. 2012;26(4):275–9.
174. Thylefors B, Negrel AD, Pararajasegaram R, Dadzie KY. Global data on blindness. Bull World Health Organ. 1995;73(1):115–21.
175. Nagai N, Fukuhata T, Ito Y. Effect of magnesium deficiency on intracellular ATP Levels in human lens epithelial cells. Biol Pharm Bull. 2007;30(1):6–10.
176. Beebe DC, Holekamp NM, Shui YB. Oxidative damage and the prevention of age-related cataracts. Ophthalmic Res. 2010;44(3):155–65.
177. Berthoud VM, Beyer EC. Forum review article oxidative stress, lens gap junctions, and cataracts. Antioxid Redox Signal. 2009;11(2):339–53.
178. Bhuyan KC, Bhuyan DK, Podos SM. Lipid peroxidation in cataract of the human. Life Sci. 1986;38(16):1463–71.
179. Gupta SK, Trivedi D, Srivastava S, Joshi S, Halder N, Verma SD. Lycopene attenuates oxidative stress induced experimental cataract development: an in vitro and in vivo study. Nutrition. 2003;19(9):794–9.
180. Boettner EH, Walter JR. Transmission of the ocular media. GPO Invest Ophthalmol Vis Sci. 1962;1:776–83.
181. Krishna CM, Uppuluri S, Riesz P, Zigler JS Jr, Balasubramian D. A study of the photodynamic efficiencies of some eye lens constituents. Photochem Photobiol. 1991;54(1):51–8.
182. Dilsiz N, Olcucu A, Atas M. Determination of calcium, sodium, potassium and magnesium concentrations in human senile cataractous lenses. Cell Biochem Funct. 2000;18(4):259–62.
183. David LL, Azuma M, Shearer TR. Cataract and the acceleration of calpain-induced beta-crystallin insolubilization occurring during normal maturation of rat lens. Invest Ophthalmol Vis Sci. 1994;35(3):785–93.
184. Spector A, Garner WH. Hydrogen peroxide and human cataract. Exp Eye Res. 1981;33(6):673–81.
185. Hapeta B, Koczy B, Fitowska A, Dobrakowski M, Kasperczyk A, Ostałowska A, et al. Metabolism and protein transformations in synovial membrane of a knee joint in the course of rheumatoid arthritis and degenerative arthritis. Pol Orthop Traumatol. 2012;77:53–8.
186. Stamp LK, Khalilova I, Tarr JM, Senthilmohan R, Turner R, Haigh RC, et al. Myeloperoxidase and oxidative stress in rheumatoid arthritis. Rheumatology (Oxford). 2012;51(10):1796–803.
187. Desai PB, Manjunath S, Kadi S, Chetana K, Vanishree J. Oxidative stress and enzymatic antioxidant status in rheumatoid arthritis: a case control study. Eur Rev Med Pharmacol Sci. 2010;14(11):959–67.
188. Grover HS, Gaba N, Gupta A, Marya CM. Rheumatoid arthritis: a review and dental care considerations. Nepal Med Coll J. 2011;13(2):74–6.
189. De Pablo P, Dietrich T, McAlindon TE. Association of periodontal disease and tooth loss with rheumatoid arthritis in the US population. J Rheumatol. 2008;35(1):70–6.
190. Vasanthi P, Nalini G, Rajasekhar G. Status of oxidative stress in rheumatoid arthritis. Int J Rheum Dis. 2009;12(1):29–33.
191. Hitchon CA, El-Gabalawy HS. Review Oxidation in rheumatoid arthritis. Arthritis Res Ther. 2004;6(6):265–78.
192. Grootveld M, Henderson EB, Farell A, Blake DR, Parkes HG, Haycock P. Oxidative damage to hyaluronate and glucose in synovial fluid during exercise of the inflamed rheumatoid joint. Detection of abnormal lowmolecular-mass metabolites by proton-n.m.r. spectroscopy. Biochem J. 1991;273:459–67.
193. Rowley D, Gutteridge JM, Blake D, Farr M, Halliwell B. Lipid peroxidation in rheumatoid arthritis: thiobarbituric acid-reactive material and catalytic iron salts in synovial fluid from rheumatoid patients. Clin Sci (London). 1984;66(6):691–5.
194. Dai L, Lamb DJ, Leake DS. Evidence for oxidized low density lipoprotein in synovial fluid from rheumatoid arthritis patients. Free Radic Res. 2000;32(6):479–86.
195. Dalle-Donne I, Rossi R, Giustarini D, Milzani A, Colombo R. Protein carbonyl groups as biomarkers of oxidative stress. Clin Chim Acta. 2003;329(1–2):23–38.
196. Dai L, Lamb DJ, Leake DS, Kus ML, Jones HW, Morris CJ, et al. Evidence for oxidised low density lipoprotein in synovial fluid from rheumatoid arthritis patients. Free Radic Res. 2000;32(6):479–86.
197. Costenbader KH, Karlson EW. Cigarette smoking and autoimmune disease: what can we learn from epidemiology? Lupus. 2006;15(11):737–45.
198. Kottova M, Pourova J, Voprsalova M. Oxidative stress and its role in respiratory diseases. Ceska Slov Farm. 2007;56(5):215–9.
199. Masoli M, Fabian D, Holt S, Beasley R. The global burden of asthma: Executive summary of the GINA Dissemination Committee report. Allergy. 2004;59(5):469–78.
200. Chung KF. Role of inflammation in the hyper reactivity of the airways in asthma. Thorax. 1986;41:657–62.
201. Barnes PJ. Reactive oxygen species and airway inflammation. Free Radic Biol Med. 1990;9(3):235–43.
202. Xiao M, Zhu T, Wang T, Wen FQ. Hydrogen-rich saline reduces airway remodeling via inactivation of NF-κB in a murine model of asthma. Eur Rev Med Pharmacol Sci. 2013;17(8):1033–43.
203. Tohyama Y, Kanazawa H, Fujiwara F, Hirata K, Fujimoto S, Yoshikawa J. Role of nitric oxide on airway microvascular permeability in patients with asthma. Osaka City Med J. 2005;51(1):1–9.
204. Rahman I, Biswas SK, Kode A. Oxidant and antioxidant balance in the airways and airway diseases. Eur J Pharmacol. 2006;533(1–3):222–39.
205. Terada LS. Specificity in reactive oxidant signaling: Think globally, act locally. J Cell Biol. 2006;174(5):615–23.
206. Fujisawa T. Role of oxygen radicals on bronchial asthma. Curr Drug Targets Inflamm Allergy. 2005;4(4):505–9.
207. Ozaras R, Tahan V, Turkmen S, Talay F, Besirli K, Aydin S, et al. Changes in malondialdehyde levels in bronchoalveolar fluid and serum by the treatment of asthma with inhaled steroid and beta2-agonist. Respirology. 2000;5(3):289–92.
208. Ahmad A, Shameem M, Husain Q. Relation of oxidant-antioxidant imbalance with disease progression in patients with asthma. Ann Thorac Med. 2012;7(4):226–32.
209. Pobed’onna HP. Antioxidant protection, metabolites of nitrogen oxide on the forming of oxidative stress in patients with bronchial asthma. Lik Sprava. 2005;(5–6):36–40.