Oxidative Stress and Antioxidant Defense

World Allergy Organization Journal

Omer Kalayci¹  Serpil Erzurum²  Cansin Sackesen¹  Umit Murat Sahiner¹  Esra Birben¹ 

[1] Pediatric Allergy and Asthma Unit, Hacettepe University School of Medicine, Ankara, Turkey;Department of Pathobiology, Lerner Research Institute, and the Respiratory Institute, Cleveland Clinic, Cleveland, OH

关键词: redox;    reactive oxygen species;    oxidative stress;    oxidant;    antioxidant;   

Others  :  1137715
DOI  :  10.1097/WOX.0b013e3182439613

【 摘 要 】

Reactive oxygen species (ROS) are produced by living organisms as a result of normal cellular metabolism and environmental factors, such as air pollutants or cigarette smoke. ROS are highly reactive molecules and can damage cell structures such as carbohydrates, nucleic acids, lipids, and proteins and alter their functions. The shift in the balance between oxidants and antioxidants in favor of oxidants is termed "oxidative stress." Regulation of reducing and oxidizing (redox) state is critical for cell viability, activation, proliferation, and organ function. Aerobic organisms have integrated antioxidant systems, which include enzymatic and non-enzymatic antioxidants that are usually effective in blocking harmful effects of ROS. However, in pathological conditions, the antioxidant systems can be overwhelmed. Oxidative stress contributes to many pathological conditions and diseases, including cancer, neurological disorders, atherosclerosis, hypertension, ischemia/perfusion, diabetes, acute respiratory distress syndrome, idiopathic pulmonary fibrosis, chronic obstructive pulmonary disease, and asthma. In this review, we summarize the cellular oxidant and antioxidant systems and discuss the cellular effects and mechanisms of the oxidative stress.

【 授权许可】

   
2012 World Allergy Organization; licensee BioMed Central Ltd.

【 图 表 】

Figure 1.

Figure 2.

【 参考文献 】

• [1]Valko M, Rhodes CJ, Moncol J, Izakovic M, Mazur M: Free radicals, metals and antioxidants in oxidative stress-induced cancer. Chem Biol Interact 2006, 160:1-40.
• [2]Halliwell B, Gutteridge JMC: Free Radicals in Biology and Medicine. 3rd edition. New York: Oxford University Press; 1999.
• [3]Marnett LJ: Lipid peroxidation--DNA damage by malondialdehyde. Mutat Res 1999, 424:83-95.
• [4]Siems WG, Grune T, Esterbauer H: 4-Hydroxynonenal formation during ischemia and reperfusion of rat small-intestine. Life Sci 1995, 57:785-789.
• [5]Stadtman ER: Role of oxidant species in aging. Curr Med Chem 2004, 11:1105-1112.
• [6]Wang MY, Dhingra K, Hittelman WN, Liehr JG, deAndrade M, Li DH: Lipid peroxidation-induced putative malondialdehyde-DNA adducts in human breast tissues. Cancer Epidemiol Biomarkers Prev 1996, 5:705-710.
• [7]Jenner P: Oxidative stress in Parkinson's disease. Ann Neurol 2003, 53:S26-S36.
• [8]Lyras L, Cairns NJ, Jenner A, Jenner P, Halliwell B: An assessment of oxidative damage to proteins, lipids, and DNA in brain from patients with Alzheimer's disease. J Neurochem 1997, 68:2061-2069.
• [9]Sayre LM, Smith MA, Perry G: Chemistry and biochemistry of oxidative stress in neurodegenerative disease. Curr Med Chem 2001, 8:721-738.
• [10]Toshniwal PK, Zarling EJ: Evidence for increased lipid peroxidation in multiple sclerosis. Neurochem Res 1992, 17:205-207.
• [11]Dhalla NS, Temsah RM, Netticadan T: Role of oxidative stress in cardiovascular diseases. J Hypertens 2000, 18:655-673.
• [12]Kasparova S, Brezova V, Valko M, Horecky J, Mlynarik V, et al.: Study of the oxidative stress in a rat model of chronic brain hypoperfusion. Neurochem Int 2005, 46:601-611.
• [13]Kerr S, Brosnan MJ, McIntyre M, Reid JL, Dominiczak AF, Hamilton CA: Superoxide anion production is increased in a model of genetic hypertension: role of the endothelium. Hypertension 1999, 33:1353-1358.
• [14]Kukreja RC, Hess ML: The oxygen free-radical system: from equations through membrane-protein interactions to cardiovascular injury and protection. Cardiovasc Res 1992, 26:641-655.
• [15]Asami S, Manabe H, Miyake J, Tsurudome Y, Hirano T, et al.: Cigarette smoking induces an increase in oxidative DNA damage, 8-hydroxydeoxyguanosine, in a central site of the human lung. Carci-nogenesis 1997, 18:1763-1766.
• [16]Andreadis AA, Hazen SL, Comhair SA, Erzurum SC: Oxidative and nitrosative events in asthma. Free Radic Biol Med 2003, 35:213-225.
• [17]Comhair SA, Ricci KS, Arroliga M, Lara AR, Dweik RA, et al.: Correlation of systemic superoxide dismutase deficiency to airflow obstruction in asthma. Am J Respir Crit Care Med 2005, 172:306-313.
• [18]Comhair SA, Xu W, Ghosh S, Thunnissen FB, Almasan A, et al.: Superoxide dismutase inactivation in pathophysiology of asthmatic airway remodeling and reactivity. Am J Pathol 2005, 166:663-674.
• [19]Dut R, Dizdar EA, Birben E, Sackesen C, Soyer OU, Besler T, Kalayci O: Oxidative stress and its determinants in the airways of children with asthma. Allergy 2008, 63:1605-1609.
• [20]Ercan H, Birben E, Dizdar EA, Keskin O, Karaaslan C, et al.: Oxidative stress and genetic and epidemiologic determinants of oxidant injury in childhood asthma. J Allergy Clin Immunol 2006, 118:1097-1104.
• [21]Fitzpatrick AM, Teague WG, Holguin F, Yeh M, Brown LA: Severe Asthma Research Program. Airway glutathione homeostasis is altered in children with severe asthma: evidence for oxidant stress. J Allergy Clin Immunol 2009, 123:146-152.
• [22]Miller DM, Buettner GR, Aust SD: Transition metals as catalysts of "autoxidation" reactions. Free Radic Biol Med 1990, 8:95-108.
• [23]Dupuy C, Virion A, Ohayon R, Kaniewski J, Dème D, Pommier J: Mechanism of hydrogen peroxide formation catalyzed by NADPH oxidase in thyroid plasma membrane. J Biol Chem 1991, 266:3739-3743.
• [24]Granger DN: Role of xanthine oxidase and granulocytes in ischemia-reperfusion injury. Am J Physiol 1988, 255:H1269-H1275.
• [25]Fenton HJH: Oxidation of tartaric acid in the presence of iron. J Chem Soc 1984, 65:899-910.
• [26]Haber F, Weiss JJ: The catalytic decomposition of hydrogen peroxide by iron salts. Proc R Soc Lond Ser A 1934, 147:332-351.
• [27]Liochev SI, Fridovich I: The Haber-Weiss cycle--70 years later: an alternative view. Redox Rep 2002, 7:55-57.
• [28]Klebanoff SJ: Myeloperoxidase: friend and foe. J Leukoc Biol 2005, 77:598-625.
• [29]Whiteman M, Jenner A, Halliwell B: Hypochlorous acid-induced base modifications in isolated calf thymus DNA. Chem Res Toxicol 1997, 10:1240-1246.
• [30]Kulcharyk PA, Heinecke JW: Hypochlorous acid produced by the myeloperoxidase system of human phagocytes induces covalent cross-links between DNA and protein. Biochemistry 2001, 40:3648-3656.
• [31]Brennan ML, Wu W, Fu X, Shen Z, Song W, et al.: A tale of two controversies: defining both the role of peroxidases in nitrotyrosine formation in vivo using eosinophil peroxidase and myeloperoxidase-deficient mice, and the nature of peroxidase-generated reactive nitrogen species. J Biol Chem 2002, 277:17415-17427.
• [32]Denzler KL, Borchers MT, Crosby JR, Cieslewicz G, Hines EM, et al.: Extensive eosinophil degranulation and peroxidase-mediated oxidation of airway proteins do not occur in a mouse ovalbumin-challenge model of pulmonary inflammation. J Immunol 2001, 167:1672-1682.
• [33]van Dalen CJ, Winterbourn CC, Senthilmohan R, Kettle AJ: Nitrite as a substrate and inhibitor of myeloperoxidase. Implications for nitration and hypochlorous acid production at sites of inflammation. J Biol Chem 2000, 275:11638-11644.
• [34]Wood LG, Fitzgerald DA, Gibson PG, Cooper DM, Garg ML: Lipid peroxidation as determined by plasma isoprostanes is related to disease severity in mild asthma. Lipids 2000, 35:967-974.
• [35]Montuschi P, Corradi M, Ciabattoni G, Nightingale J, Kharitonov SA, Barnes PJ: Increased 8-isoprostane, a marker of oxidative stress, in exhaled condensate of asthma patients. Am J Respir Crit Care Med 1999, 160:216-220.
• [36]Church DF, Pryor WA: Free-radical chemistry of cigarette smoke and its toxicological implications. Environ Health Perspect 1985, 64:111-126.
• [37]Hiltermann JT, Lapperre TS, van Bree L, Steerenberg PA, Brahim JJ, et al.: Ozone-induced inflammation assessed in sputum and bronchial lavage fluid from asthmatics: a new noninvasive tool in epidemiologic studies on air pollution and asthma. Free Radic Biol Med 1999, 27:1448-1454.
• [38]Nightingale JA, Rogers DF, Barnes PJ: Effect of inhaled ozone on exhaled nitric oxide, pulmonary function, and induced sputum in normal and asthmatic subjects. Thorax 1999, 54:1061-1069.
• [39]Cho AK, Sioutas C, Miguel AH, Kumagai Y, Schmitz DA, et al.: Redox activity of airborne particulate matter at different sites in the Los Angeles Basin. Environ Res 2005, 99:40-47.
• [40]Comhair SA, Thomassen MJ, Erzurum SC: Differential induction of extracellular glutathione peroxidase and nitric oxide synthase 2 in airways of healthy individuals exposed to 100% O(2) or cigarette smoke. Am J Respir Cell Mol Biol 2000, 23:350-354.
• [41]Matthay MA, Geiser T, Matalon S, Ischiropoulos H: Oxidant-mediated lung injury in the acute respiratory distress syndrome. Crit Care Med 1999, 27:2028-2030.
• [42]Biaglow JE, Mitchell JB, Held K: The importance of peroxide and superoxide in the X-ray response. Int J Radiat Oncol Biol Phys 1992, 22:665-669.
• [43]Chiu SM, Xue LY, Friedman LR, Oleinick NL: Copper ion-mediated sensitization of nuclear matrix attachment sites to ionizing radiation. Biochemistry 1993, 32:6214-6219.
• [44]Narayanan PK, Goodwin EH, Lehnert BE: Alpha particles initiate biological production of superoxide anions and hydrogen peroxide in human cells. Cancer Res 1997, 57:3963-3971.
• [45]Tuttle SW, Varnes ME, Mitchell JB, Biaglow JE: Sensitivity to chemical oxidants and radiation in CHO cell lines deficient in oxidative pentose cycle activity. Int J Radiat Oncol Biol Phys 1992, 22:671-675.
• [46]Guo G, Yan-Sanders Y, Lyn-Cook BD, Wang T, Tamae D, et al.: Manganese superoxide dismutase-mediated gene expression in radiation-induced adaptive responses. Mol Cell Biol 2003, 23:2362-2378.
• [47]Azzam EI, de Toledo SM, Spitz DR, Little JB: Oxidative metabolism modulates signal transduction and micronucleus formation in bystander cells from a-particle irradiated normal human fibroblasts. Cancer Res 2002, 62:5436-5442.
• [48]Leach JK, Van Tuyle G, Lin PS, Schmidt-Ullrich R, Mikkelsen RB: Ionizing radiation-induced, mitochondria-dependent generation of reactive oxygen/nitrogen. Cancer Res 2001, 61:3894-3901.
• [49]Dent P, Yacoub A, Fisher PB, Hagan MP, Grant S: MAPK pathways in radiation responses. Oncogene 2003, 22:5885-5896.
• [50]Wei SJ, Botero A, Hirota K, Bradbury CM, Markovina S, et al.: Thioredoxin nuclear translocation and interaction with redox factor-1 activates the AP-1 transcription factor in response to ionizing radiation. Cancer Res 2000, 60:6688-6695.
• [51]Cadet J, Douki T, Gasparutto D, Ravanat JL: Oxidative damage to DNA: formation, measurement and biochemical features. Mutat Res 2003, 531:5-23.
• [52]Yokoya A, Cunniffe SM, O'Neill P: Effect of hydration on the induction of strand breaks and base lesions in plasmid DNA films by gamma-radiation. J Am Chem Soc 2002, 124:8859-8866.
• [53]Janssen YM, Van Houten B, Borm PJ, Mossman BT: Cell and tissue responses to oxidative damage. Lab Invest 1993, 69:261-274.
• [54]Iwanaga M, Mori K, Iida T, Urata Y, Matsuo T, et al.: Nuclear factor kappa B dependent induction of gamma glutamylcysteine synthetase by ionizing radiation in T98G human glioblastoma cells. Free Radic Biol Med 1998, 24:1256-1268.
• [55]Stohs SJ, Bagchi D: Oxidative mechanisms in the toxicity of metal ions. Free Radic Biol Med 1995, 18:321-336.
• [56]Leonard SS, Harris GK, Shi X: Metal-induced oxidative stress and signal transduction. Free Radic Biol Med 2004, 37:1921-1942.
• [57]Shi H, Shi X, Liu KJ: Oxidative mechanism of arsenic toxicity and carcinogenesis. Mol Cell Biochem 2004, 255:67-78.
• [58]Pi J, Horiguchi S, Sun Y, Nikaido M, Shimojo N, Hayashi T: A potential mechanism for the impairment of nitric oxide formation caused by prolonged oral exposure to arsenate in rabbits. Free Radic Biol Med 2003, 35:102-113.
• [59]Rin K, Kawaguchi K, Yamanaka K, Tezuka M, Oku N, Okada S: DNA-strand breaks induced by dimethylarsinic acid, a metabolite of inorganic arsenics, are strongly enhanced by superoxide anion radicals. Biol Pharm Bull 1995, 18:45-58.
• [60]Waalkes MP, Liu J, Ward JM, Diwan LA: Mechanisms underlying arsenic carcinogenesis: hypersensitivity of mice exposed to inorganic arsenic during gestation. Toxicology 2004, 198:31-38.
• [61]Schiller CM, Fowler BA, Woods JS: Effects of arsenic on pyruvate dehydrogenase activation. Environ Health Perspect 1977, 19:205-207.
• [62]Monterio HP, Bechara EJH, Abdalla DSP: Free radicals involvement in neurological porphyrias and lead poisoning. Mol Cell Biochem 1991, 103:73-83.
• [63]Tripathi RM, Raghunath R, Mahapatra S: Blood lead and its effect on Cd, Cu, Zn, Fe and hemoglobin levels of children. Sci Total Environ 2001, 277:161-168.
• [64]Nehru B, Dua R: The effect of dietary selenium on lead neurotoxicity. J Environ Pathol Toxicol Oncol 1997, 16:47-50.
• [65]Reid TM, Feig DI, Loeb LA: Mutagenesis by metal-induced oxygen radicals. Environ Health Perspect 1994, 102(suppl 3):57-61.
• [66]Kinnula VL, Crapo JD: Superoxide dismutases in the lung and human lung diseases. Am J Respir Crit Care Med 2003, 167:1600-1619.
• [67]Kinnula VL: Production and degradation of oxygen metabolites during inflammatory states in the human lung. Curr Drug Targets In3amm Allergy 2005, 4:465-470.
• [68]Zelko IN, Mariani TJ, Folz RJ: Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression. Free Radic Biol Med 2002, 33:337-349.
• [69]Kirkman HN, Rolfo M, Ferraris AM, Gaetani GF: Mechanisms of protection of catalase by NADPH. Kinetics and stoichiometry. J Biol Chem 1999, 274:13908-13914.
• [70]Flohé L: Glutathione peroxidase. Basic Life Sci 1988, 49:663-668.
• [71]Arthur JR: The glutathione peroxidases. Cell Mol Life Sci 2000, 57:1825-1835.
• [72]Chu FF, Doroshow JH, Esworthy RS: Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI. J Biol Chem 1993, 268:2571-2576.
• [73]Comhair SA, Bhathena PR, Farver C, Thunnissen FB, Erzurum SC: Extracellular glutathione peroxidase induction in asthmatic lungs: evidence for redox regulation of expression in human airway epithelial cells. FASEB J 2001, 15:70-78.
• [74]Gromer S, Urig S, Becker K: The thioredoxin system--from science to clinic. Med Res Rev 2004, 24:40-89.
• [75]Kinnula VL, Lehtonen S, Kaarteenaho-Wiik R, Lakari E, Pääkkö P, et al.: Cell specific expression of peroxiredoxins in human lung and pulmonary sarcoidosis. Thorax 2002, 57:157-164.
• [76]Dubuisson M, Vander Stricht D, Clippe A, Etienne F, Nauser T, et al.: Human peroxiredoxin 5 is a peroxynitrite reductase. FEBS Lett 2004, 571:161-165.
• [77]Holmgren A: Antioxidant function of thioredoxin and glutaredoxin systems. Antioxid Redox Signal 2000, 2:811-820.
• [78]Dickinson DA, Forman HJ: Glutathione in defense and signaling: lessons from a small thiol. Ann N Y Acad Sci 2002, 973:488-504.
• [79]Sies H: Glutathione and its role in cellular functions. Free Radic Biol Med 1999, 27:916-921.
• [80]Ladner JE, Parsons JF, Rife CL, Gilliland GL, Armstrong RN: Parallel evolutionary pathways for glutathione transferases: structure and mechanism of the mitochondrial class kappa enzyme rGSTK1-1. Biochemistry 2004, 43:52-61.
• [81]Robinson A, Huttley GA, Booth HS, Board PG: Modelling and bioinformatics studies of the human kappa class glutathione transferase predict a novel third transferase family with homology to prokaryotic 2-hydroxychromene-2-carboxylate isomerases. Biochem J 2004, 379:541-552.
• [82]Jakobsson P-J, Morgenstern R, Mancini J, Ford-Hutchinson A, Persson B: Common structural features of MAPEG--a widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism. Protein Sci 1999, 8:689-692.
• [83]Hayes JD, Pulford DJ: The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit Rev Biochem Mol Biol 1995, 30:445-600.
• [84]Armstrong RN: Structure, catalytic mechanism, and evolution of the glutathione transferases. Chem Res Toxicol 1997, 10:2-18.
• [85]Hayes JD, McLellan LI: Glutathione and glutathione-dependent enzymes represent a co-ordinately regulated defence against oxidative stress. Free Radic Res 1999, 31:273-300.
• [86]Sheehan D, Meade G, Foley VM, Dowd CA: Structure, function and evolution of glutathione transferases: implications for classification of nonmammalian members of an ancient enzyme superfamily. Biochem J 2001, 360:1-16.
• [87]Cho S-G, Lee YH, Park H-S, Ryoo K, Kang KW, et al.: Glutathione S-transferase Mu modulates the stress activated signals by suppressing apoptosis signal-regulating kinase 1. J Biol Chem 2001, 276:12749-12755.
• [88]Dorion S, Lambert H, Landry J: Activation of the p38 signaling pathway by heat shock involves the dissociation of glutathione S-transferase Mu from Ask1. J Biol Chem 2002, 277:30792-30797.
• [89]Adler V, Yin Z, Fuchs SY, Benezra M, Rosario L, et al.: Regulation of JNK signalling by GSTp. EMBO J 1999, 18:1321-1334.
• [90]Manevich Y, Feinstein SI, Fisher AB: Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pGST. Proc Natl Acad Sci USA 2004, 101:3780-3785.
• [91]Bunker VW: Free radicals, antioxidants and ageing. Med Lab Sci 1992, 49:299-312.
• [92]Mezzetti A, Lapenna D, Romano F, Costantini F, Pierdomenico SD, et al.: Systemic oxidative stress and its relationship with age and illness. J Am Geriatr Soc 1996, 44:823-827.
• [93]White E, Shannon JS, Patterson RE: Relationship between vitamin and calcium supplement use and colon cancer. Cancer Epidemiol Bio-markers Prev 1997, 6:769-774.
• [94]Masella R, Di Benedetto R, Vari R, Filesi C, Giovannini C: Novel mechanisms of natural antioxidant compounds in biological systems: involvement of glutathione and glutathione-related enzymes. J Nutr Biochem 2005, 16:577-586.
• [95]Curello S, Ceconi C, Bigoli C, Ferrari R, Albertini A, Guarnieri C: Changes in the cardiac glutathione status after ischemia and reperfusion. Experientia 1985, 41:42-43.
• [96]El-Agamey A, Lowe GM, McGarvey DJ, Mortensen A, Phillip DM, Truscott TG: Carotenoid radical chemistry and antioxidant/pro-oxidant properties. Arch Biochem Biophys 2004, 430:37-48.
• [97]Rice-Evans CA, Sampson J, Bramley PM, Holloway DE: Why do we expect carotenoids to be antioxidants in vivo? Free Radic Res 1997, 26:381-398.
• [98]Niles RM: Signaling pathways in retinoid chemoprevention and treatment of cancer. Mutat Res 2004, 555:81-96.
• [99]Donato LJ, Noy N: Suppression of mammary carcinoma growth by retinoic acid: proapoptotic genes are targets for retinoic acid receptor and cellular retinoic acid-binding protein II signaling. Cancer Res 2005, 65:8193-8199.
• [100]Niizuma H, Nakamura Y, Ozaki T, Nakanishi H, Ohira M, et al.: Bcl-2 is a key regulator for the retinoic acid-induced apoptotic cell death in neuroblastoma. Oncogene 2006, 25:5046-5055.
• [101]Dalton TP, Shertzer HG, Puga A: Regulation of gene expression by reactive oxygen. Ann Rev Pharmacol Toxicol 1999, 39:67-101.
• [102]Scandalios JG: Genomic responses to oxidative stress. In Encyclopedia of Molecular Cell Biology and Molecular Medicine. Volume 5. 2nd edition. Edited by Meyers RA. Weinheim, Germany: Wiley-VCH; 2004::489-512.
• [103]Ghosh R, Mitchell DL: Effect of oxidative DNA damage in promoter elements on transcription factor binding. Nucleic Acids Res 1999, 27:3213-3218.
• [104]Marietta C, Gulam H, Brooks PJ: A single 8, 50-cyclo-20-deoxyadeno-sine lesion in a TATA box prevents binding of the TATA binding protein and strongly reduces transcription in vivo. DNA Repair (Amst) 2002, 1:967-975.
• [105]Jackson AL, Chen R, Loeb LA: Induction of microsatellite instability by oxidative DNA damage. Proc Natl Acad Sci USA 1998, 95:12468-12473.
• [106]Caldecott KW: Protein-protein interactions during mammalian DNA single-strand break repair. Biochem Soc Trans 2003, 31:247-251.
• [107]Cooke MS, Evans MD, Dizdaroglu M, Lunec J: Oxidative DNA damage: mechanisms, mutation, and disease. FASEB J 2003, 17:1195-1214.
• [108]Jones PL, Wolffe AP: Relationships between chromatin organization and DNA methylation in determining gene expression. Semin Cancer Biol 1999, 9:339-347.
• [109]Girotti AW: Mechanisms of lipid peroxidation. J Free Radic Biol Med 1985, 1:87-95.
• [110]Siu GM, Draper HH: Metabolism of malonaldehyde in vivo and in vitro. Lipids 1982, 17:349-355.
• [111]Esterbauer H, Koller E, Slee RG, Koster JF: Possible involvement of the lipid-peroxidation product 4-hydroxynonenal in the formation of fluorescent chromolipids. Biochem J 1986, 239:405-409.
• [112]Hagihara M, Nishigaki I, Maseki M, Yagi K: Age-dependent changes in lipid peroxide levels in the lipoprotein fractions of human serum. J Gerontol 1984, 39:269-272.
• [113]Keller JN, Mark RJ, Bruce AJ, Blanc E, Rothstein JD, et al.: 4-Hydroxynonenal, an aldehydic product of membrane lipid peroxidation, impairs glutamate transport and mitochondrial function in synaptosomes. Neuroscience 1997, 806:85-96.
• [114]Uchida K, Shiraishi M, Naito Y, Torii Y, Nakamura Y, Osawa T: Activation of stress signaling pathways by the end product of lipid peroxidation. 4-hydroxy-2-nonenal is a potential inducer of intracellular peroxide production. J Biol Chem 1999, 274:2234-2242.
• [115]Suc I, Meilhac O, Lajoie-Mazenc I, Vandaele J, Jurgens G, Salvayre R, Negre-Salvayre A: Activation of EGF receptor by oxidized LDL. FASEB J 1998, 12:665-671.
• [116]Tsukagoshi H, Kawata T, Shimizu Y, Ishizuka T, Dobashi K, Mori M: 4-Hydroxy-2-nonenal enhances fibronectin production by IMR-90 human lung fibroblasts partly via activation of epidermal growth factor receptor-linked extracellular signal-regulated kinase p44/42 pathway. Toxicol Appl Pharmacol 2002, 184:127-135.
• [117]Montuschi P, Collins JV, Ciabattoni G, Lazzeri N, Corradi M, Kharitonov SA, Barnes PJ: Exhaled 8-isoprostane as an in vivo bio-marker of lung oxidative stress in patients with COPD and healthy smokers. Am J Respir Crit Care Med 2000, 162:1175-1177.
• [118]Morrison D, Rahman I, Lannan S, MacNee W: Epithelial permeability, inflammation, and oxidant stress in the air spaces of smokers. Am J Respir Crit Care Med 1999, 159:473-479.
• [119]Nowak D, Kasielski M, Antczak A, Pietras T, Bialasiewicz P: Increased content of thiobarbituric acid-reactive substances and hydrogen peroxide in the expired breath condensate of patients with stable chronic obstructive pulmonary disease: no significant effect of cigarette smoking. Respir Med 1999, 93:389-396.
• [120]Kelly FJ, Mudway IS: Protein oxidation at the air-lung interface. Amino Acids 2003, 25:375-396.
• [121]Dean RT, Roberts CR, Jessup W: Fragmentation of extracellular and intracellular polypeptides by free radicals. Prog Clin Biol Res 1985, 180:341-350.
• [122]Keck RG: The use of t-butyl hydroperoxide as a probe for methionine oxidation in proteins. Anal Biochem 1996, 236:56-62.
• [123]Davies KJ: Protein damage and degradation by oxygen radicals. I. General aspects. J Biol Chem 1987, 262:9895-9901.
• [124]Stadtman ER: Metal ion-catalyzed oxidation of proteins: biochemical mechanism and biological consequences. Free Radic Biol Med 1990, 9:315-325.
• [125]Fucci L, Oliver CN, Coon MJ, Stadtman ER: Inactivation of key metabolic enzymes by mixed-function oxidation reactions: possible implication in protein turnover and ageing. Proc Natl Acad Sci USA 1983, 80:1521-1525.
• [126]Stadtman ER, Moskovitz J, Levine RL: Oxidation of methionine residues of proteins: biological consequences. Antioxid Redox Signal 2003, 5:577-582.
• [127]Stadtman ER, Levine RL: Free radical-mediated oxidation of free amino acids and amino acid residues in proteins. Amino Acids 2003, 25:207-218.
• [128]Stadtman ER: Protein oxidation in aging and age-related diseases. Ann N Y Acad Sci 2001, 928:22-38.
• [129]Shacter E: Quantification and significance of protein oxidation in biological samples. Drug Metab Rev 2000, 32:307-326.
• [130]Poli G, Leonarduzzi G, Biasi F, Chiarpotto E: Oxidative stress and cell signalling. Curr Med Chem 2004, 11:1163-1182.
• [131]Neufeld G, Cohen T, Gengrinovitch S, Poltorak Z: Vascular endothelial growth factor (VEGF) and its receptors. FASEB J 1999, 13:9-22.
• [132]Sundaresan M, Yu ZX, Ferrans VJ, Sulciner DJ, Gutkind JS, et al.: Regulation of reactive-oxygen species generation in fibroblasts by Rac1. Biochem J 1996, 318:379-382.
• [133]Sun T, Oberley LW: Redox regulation of transcriptional activators. Free Radic Biol Med 1996, 21:335-348.
• [134]Klatt P, Molina EP, De Lacoba MG, Padilla CA, Martinez-Galesteo E, Barcena JA, Lamas S: Redox regulation of c-Jun DNA binding by reversible S-glutathiolation. FASEB J 1999, 13:1481-1490.
• [135]Reynaert NL, Ckless K, Guala AS, Wouters EF, van der Vliet A, Janssen-Heininger YM: In situ detection of S-glutathionylated proteins following glutaredoxin-1 catalyzed cysteine derivatization. Biochim Biophys Acta 2006, 1760:380-387.
• [136]Reynaert NL, Wouters EF, Janssen-Heininger YM: Modulation of glu-taredoxin-1 expression in a mouse model of allergic airway disease. Am J Respir Cell Mol Biol 2007, 36:147-151.
• [137]Filomeni G, Rotilio G, Ciriolo MR: Cell signalling and the glutathione redox system. Biochem Pharmacol 2002, 64:1057-1064.
• [138]Pande V, Ramos MJ: Molecular recognition of 15-deoxydelta (12, 14)-prostaglandin J(2) by nuclear factor-kappa B and other cellular proteins. Bioorg Med Chem Lett 2005, 15:4057-4063.
• [139]Perkins ND: Integrating cell-signalling pathways with NF-kappaB and IKK function. Nat Rev Mol Cell Biol 2007, 8:49-62.
• [140]Gilmore TD: Introduction to NF-kappaB: players, pathways, perspectives. Oncogene 2006, 25:6680-6684.
• [141]Hirota K, Murata M, Sachi Y, Nakamura H, Takeuchi J, Mori K, Yodoi J: Distinct roles of thioredoxin in the cytoplasm and in the nucleus. A two-step mechanism of redox regulation of transcription factor NF-kappaB. J Biol Chem 1999, 274:27891-27897.
• [142]Ward PA: Role of complement, chemokines and regulatory cytokines in acute lung injury. Ann N Y Acad Sci 1996, 796:104-112.
• [143]Akira S, Kishimoto A: NF-IL6 and NF-kB in cytokine gene regulation. Adv Immunol 1997, 65:1-46.
• [144]Meyer M, Schreck R, Baeuerle PA: H2O2 and antioxidants have opposite effects on activation of NF-kappa B and AP-1 in intact cells: AP-1 as secondary antioxidant-responsive factor. EMBO J 1993, 12:2005-2015.
• [145]Abate C, Patel L, Rausher FJ, Curran T: Redox regulation of fos and jun DNA-binding activity in vitro. Science 1990, 249:1157-1161.
• [146]Galter D, Mihm S, Droge W: Distinct effects of glutathione disulphide on the nuclear transcription factors kB and the activator protein-1. Eur J Biochem 1994, 221:639-648.
• [147]Hirota K, Matsui M, Iwata S, Nishiyama A, Mori K, Yodoi J: AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1. Proc Natl Acad Sci USA 1997, 94:3633-3638.