Rahime ASLANKOÇ, Deniz DEMİRCİ, Ümmahan İNAN, Mahmut YILDIZ, Ahmet ÖZTÜRK, Mevlüt ÇETİN, E. Şirin SAVRAN, Burak YILMAZ

OKSİDATİF STRES DURUMUNDA ANTİOKSİDAN ENZİMLERİN ROLÜ - SÜPEROKSİT DİSMUTAZ (SOD), KATALAZ (CAT) VE GLUTATYON PEROKSİDAZ (GPx)

Vücut enzimatik ve enzimatik olmayan karmaşık bir antioksidan savunma sistemine sahiptir. Antioksidan mekanizmalar vücut dokuları için zararlı etkilere sahip olan serbest radikallere karşı savunma sistemi geliştirirler. Süperoksit dismutaz (SOD), katalaz (CAT) ve glutatyon peroksidaz (GPx) hücrede serbest radikallere karşı temel savunma hattını oluştururlar. Serbest radikaller özellikle mitokondriyal enerji üretim yoluyla sürekli olarak üretilir. Serbest radikallerin hücrede birikmesi oksidatif strese ve hücresel hasara neden olur. Hücre reaktif oksijen türlerinde artışın nörodejeneratif, kardiyovasküler, diyebet ve böbrek hastalıkları gibi bir çok hastalıkların patogenezinde rol oynadığı ifade edilmektedir. SOD, CAT ve GPx’in hücresel hasarı önlemedeki rolü sürekli olarak araştırılmaktadır.

THE ROLE OF ANTIOXIDANT ENZYMES IN OXIDATIVE STRESS - SUPEROXIDE DISMUTASE(SOD), CATALASE (CAT) AND GLUTATHIONE PEROXIDASE (GPx)

The human body has a complex antioxidant defense system that is enzymatic and non-enzymatic. Antioxidant mechanisms develop a defense system against free radicals which have harmful effects on body tissues. Superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPx) occur the basic line of defense against free radicals in the cell. Especially free radicals are produced continuously through production of mitochondrial energy. The accumulation of free radicals in the cell causes oxidative stress and cellular damage. It is stated that increased reactive oxygen species in the cell, play a role in the pathogenesis of many diseases such as neurodegenerative, cardiovascular, diabetic and kidney diseases. The role of SOD, CAT, and GPx in preventing cellular damage is constantly being investigated. This review article was written to explain the role of SOD, CAT and GPx antioxidant enzymes in preventing oxidative stress.

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1. Sies H, Cadenas E. Oxidative stress: damage to intact cells and organs. Philos. Trans. R. Soc. 1985; B311: 617–31
2. Halliwell B. Biochemistry of oxidative stress. Biochemical Society Transactions; 35, part 5.
3. Lopez-Alarcona C, Denicola A. Evaluating the antioxidant capacity of natural products: a review on chemical and cellular-based assays. Anal. Chim. Acta; 2013; 763: 1e10.
4. Pisoschi AM, Pop A. The role of antioxidants in the chemistry of oxidative stress: A review. European Journal of Medicinal Chemistry 2015; 97: 55 74
5. Percival, M., Antioxidants. Clinical Nutrition Insights 1998; 10:1- 4
6. Lobo V, Patil A, Phatak A, Chandra N. Free radicals, antioxidants and functional foods: Impact on human health. Pharmacogn Rev. 2010; 4(8): 118–126.
7. Niki E. Antioxidant defenses in eukaryotic cells. In: Poli G, Albano E, Dianzani MU, editors. Free radicals: From basic science to medicine. Basel, Switzerland: Birkhauser Verlag; 1993. pp. 365–73.
8. Poljsak B, Jamnik P, Raspor P, Pesti M. Oxidation-antioxidation-reduction processes in the cell: impacts of environmental pollution, in: N. Jerome (Ed.), Encyclopedia of Environmental Health, Elsevier, 2011, pp. 300e306.
9. Poljsak B, Suput D, Milisav I. Achieving the balance between ROS and antioxidants: when to use the synthetic antioxidants, Oxid. Med. Cell. Longev 2013;2013: Article ID 956792, 11 pages, http://dx.doi.org/10.1155/2013/956792.
10. Sen S, Chakraborty R, Sridhar C, Reddy YSR, De B. Free radicals, antioxidants, diseases and phytomedicines: Current status and future prospect. Int J Pharm Sci Res 2010; 3(1): 91-100.
11. Gutteridge JMC. Biological origin of free radicals, and mechanisms of antioxidant protection, Chem. Biol. Interact. 1994; 91: 133-140.
12. Kohen R, Nyska A. Oxidation of biological systems: oxidative stress phenomena, antioxidants, redox reactions, and methods for their quantification, Toxicol. Pathol. 2002; 30(6): 620- 650.
13. Miao L, Clair DKS. Regulation of superoxide dismutase genes: implications in disease, Free Radic. Bio. Med. 2009;47: 344- 356.
14. Young IS, Woodside J V. Antioxidants in health and disease. J Clin Pathol. 2001; 54: 176-186.
15. Al-Omar MA, Beedham C, Alsarra IA. Pathological roles of reactive oxygen species and their defence mechanisms. Saudi Pharm J. 2004;12: 1-18.
16. Valko M, Izakovic M, Mazur M, Christopher J, Telser J. Role of oxygen radicals in DNA damage and cancer incidence. Mol. Cell. Biochem. 2004; 266(1-2): 37-56.
17. Ayala A, Munoz MF, Argüelles S. Lipid Peroxidation: Production, Metabolism, and Signaling Mechanisms of Malondialdehyde and 4-Hydroxy-2-Nonenal. Oxidative Medicine and Cellular Longevity 2014; 2014: Article ID 360438, 31 pages
18. Frankel EN, Neff WE. Formation of malonaldehyde from lipid oxidation products. Biochim Biophys Acta 1983;754(3): 264- 270.
19. Esterbauer H, Schaur RJ, Zollner H. Chemistry and Biochemistry of 4-hydroxynonenal,malonaldehyde and related aldehydes. Free Radical Biology and Medicine 1991;11(1): 81–128
20. Wang X, Lei XG, Wang J. Malondialdehyde regulates glucose-stimulated insulin secretion in murine islets via TCF7L2-dependent Wnt signaling pathway. Molecular and Cellular Endocrinology 2014; 382(1): 8–16.
21. Garc´ıa-Ruiz I, de la Torre P, D´ıaz T, Esteban E, Fernandez I, Munoz T, et al. “Sp1 and Sp3 transcription factors mediate malondialdehyde-induced collagen alpha 1(I) gene expression in cultured hepatic stellate cells,” The Journal of Biological Chemistry 2002; 277( 34): 30551–30558
22. Blair IA. DNA adducts with lipid peroxidation products,” Journal of Biological Chemistry 2008;283(23): 15545–15549.
23. Del Rio D, Stewart AJ, Pellegrini N. A review of recent studies on malondialdehyde as toxic molecule and biological marker of oxidative stress. Nutrition, Metabolism & Cardiovascular Diseases 2005; 15: 316-328
24. Sanyal J, Bandyopadhyay SK, Banerjee TK, Mukherjee SC, Chakraborty DP, Ray BC, Rao VR. Plasma levels of lipid peroxides in patients with Parkinson’s disease. European Review forMedical and Pharmacological Sciences 2009;13( 2): 129– 132.
25. Gandhi S, Abramov AY. Mechanism of oxidative stress in neurodegeneration. Oxid. Med. Cell. Longev. 2012 (2012), http://dx. doi.org/10.1155/2012/428010. Article ID 428010, 11 pages.
26. Meagher E, Rader DJ. Antioxidant therapy and atherosclerosis: animal and human studies. Trends Cardiovasc. Med.2001; 11: 162-165.
27. Rodrigo R. Prevention of postoperative atrial fibrillation: novel and safe strategy based on the modulation of the antioxidant system. Front. Physiol. 2012;3: http://dx.doi.org/10.3389/fphys.2012.00093. Article 93.
28. Manea A. NADPH oxidase-derived reactive oxygen species: involvement in vascular physiology and pathology. Cell. Tissue Res. 2010; 342: 325-339.
29. Tandon VR, Sharma S, Mahajan A, Bardi GH. Oxidative stress: a novel strategy in cancer treatment, JK Sci. 2005;7 (1): 1-3.
30. Sequeira S, Rao AV, Rao A. Increased oxidative stress and altered antioxidants status in patients with chronic allergic rhinitis. Adv. Biosci. Biotechnol. 2012;3: 951-956.
31. Mirshafiey A, Mohsenzadegan M. The role of reactive oxygen species in immunopathogenesis of rheumatoid arthritis. Iran. J. Allergy Asthma Immunol. 2008;7: 195-202.
32. Hitchon CA, El-Gabalawy HS. Oxidation in rheumatoid arthritis. Arthritis Res. Ther. 2004; 6: 265-278.
33. Valko M, Leibfritz D, Moncol J, Cronin MTD, Mazur M, Telser J. Free radicals and antioxidants in normal physiological functions and human disease. The International Journal of Biochemistry & Cell Biology 2007; 39: 44–84
34. Ighodaro OM, Akinloye OA. First line defence antioxidants-superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPX): Their fundamental role in the entire antioxidant defence grid. Alexandria Journal of Medicine 2018;54: 287–293.
35. Aslankoc R, Gumral N, Saygın M, Senol M, Ascı H, Cankara FN, Comlekci S. The impact of electric fields on testis physiopathology, sperm parameters and DNA integrity—The role of resveratrol. Andrologia 2018;50:e12971.
36. Postaci I, Coskun O, Senol N, Aslankoc R, Comlekci S. The physiopathological effects of quercetin on oxidative stress in radiation of 4.5 g mobile phone exposed liver tissue of rat. Bratisl Lek Listy. 2018;119(8):481-489.
37. Lotito SB, Fraga CG. (+)-Catechin prevents human plasma oxidation. Free Radic Biol Med. 1998;24: 435-441
38. Kojo S. Vitamin C: Basic metabolism and its function as an index of oxidative stress. Curr. Med. Chem. 2004; 11: 1041–1064.
39. Landis GN, Tower J. Superoxide dismutase evolution and life span regulation. Mech. Ageing Dev. 2005; 126, 365–379.
40. Sharoni Y, Danilenko M, Dubi N, Ben-Dor A, Levy J. Carotenoids and transcription. Arch. Biochem. Biophys., 2004;430: 89–96.
41. Smith AR, Shenvi SV, Widlansky M, Suh JH, Hagen TM. Lipoic acid as a potential therapy for chronic diseases associated with oxidative stress.Curr. Med. Chem. 2004; 11: 1135–1146.
42. Topsakal S, Ozmen O, Aslankoc R, Aydemir DH. Pancreatic damage induced by cigarette smoke: the specific pathological effects of cigarette smoke in the rat model. Toxicol Res (Camb). 2016;5(3): 938-945.
43. Saygin M, Ozmen O, Erol O, Ellidağ HY, Ilhan I, Aslankoc R. The impact of electromagnetic radiation (2.45 GHz, Wi-Fi) on the female reproductive system: The role of vitamin C. Toxicol Ind Health. 2018;34(9): 620-630.
44. 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 Radical Biology & Medicine 2002; 33(3): 337–349.
45. Takada Y, Hachiya M, Park SH, Osawa Y, Ozawa T, Akashi M. Role of Reactive Oxygen Species in Cells Overexpressing Manganese Superoxide Dismutase: Mechanism for Induction of Radioresistance. Molecular Cancer Research 2002;1: 137– 146.
46. Fattman CL, Schaefer LM, Oury TD. Extracellular superoxide dismutase in biology and medicine. Free Radical Biology & Medicine 2003; 35(3): 236–256.
47. Landmesser U, Merten R, Spiekermann S, Buttner K., Drexler H, Hornig B. Vascular extracellular superoxide dismutase activity in patients with coronary artery disease: relation to endothelium-dependent vasodilation. Circulation; 2000;101:2264– 2270.
48. 48. Fukai T, Siegfried MR, Ushio-Fukai M, Griendling KK, Harrison DG. Modulation of extracellular superoxide dismutase expression by angiotensin II and hypertension. Circ. Res.1999; 85: 23–28.
49. Kimura F, Hasegawa G, Obayashi H, Adachi T, Hara H, Ohta M, et al. Serum Extracellular Superoxide Dismutase in Patients With Type 2 Diabetes. Diabetes Care 2003;26:1246–1250.
50. Schneider MP, Sullivan JC, Wach PF , Boesen RI, Yamamoto T, Fukai T, Harrison DG, Pollock DM, Pollock JS. Protective role of extracellular superoxide dismutase in renal ischemia/reperfusion injury. Kidney International 2010; 78: 374–381
51. Radi R, Turrens JF, Chang LY, Bush KM, Crapo JD, Freeman BA. Detection of catalase in rat heart mitochondria. J Biol Chem. 1991;266:22028–22034.
52. Chelikani P, Fita I, Loewen PC. Diversity of structures and properties among catalases. Cell Mol Life Sci. 2004;61: 192–208.
53. Dröge W. Free radicals in the physiological control of cell function. Physiol Rev. 2002;82: 47–95.
54. Zámocky´ M, Koller F. Understanding the structure and function of catalases: clues from molecular evolution and in vitro mutagenesis. Prog Biophys Mol Biol. 1999;72: 19–66.
55. Khan MA, Tania M, Zhang DZ, Chen HC. Antioxidant enzymes and cancer. Chinese J Cancer Res. 2010;22: 87–92.
56. Góth , Rass P, Páy A. Catalase enzyme mutations and their association with diseases. Mol Diagn. 2004;8: 141–149.
57. Cnubben NHP, Rietjens IMCM, Wortelboer H, Van Zanden J, Van Bladeren PJ. The interplay of glutathione-related processes in antioxidant defense. Environmental Toxicology and Pharmacology 2001;10:141-152.
58. Chabory E, Damon C, Lenoir A, Kauselmann G, Kern H, Zevnik B, et al. Epididymis seleno-independent glutathione peroxidase 5 maintains sperm DNA integrity in mice. J Clin Invest. 2009;119(7):2074-2085.
59. Blankenberg S, Rupprecht HJ, Bickel C, Torzewski M, Hafner G, Tiret L, Smieja M, Cambien F, Meyer J, Lackner KJ. Glutathione Peroxidase 1 Activity and Cardiovascular Events in Patients with Coronary Artery Disease. N Engl J Med 2003; 349:1605-1613