Oksidatif stres durumunda antioksidan enzimlerin rolü - Süperoksit dismutaz (SOD), katalaz (CAT) ve glutatyon peroksidaz (GPX)

Rahime Aslankoç; Deniz Demirci; Ümmahan İnan; Mahmut Yıldız; Ahmet Öztürk; Mevlüt Çetin; Ecem Şirin Savran; Burak Yılmaz

doi:10.17343/sdutfd.566969

Oksidatif stres durumunda antioksidan enzimlerin rolü - Süperoksit dismutaz (SOD), katalaz (CAT) ve glutatyon peroksidaz (GPX)

Öz

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.

Bu derleme makalesi, SOD, CAT ve GPX antioksidan enzimlerinin oksidatif stresi önlemedeki rolünü açıklamak için yazılmıştır.

Anahtar Kelimeler

Süperoksit dismutaz,Katalaz,Glutatyon peroksidaz,Oksidatif stres

Kaynakça

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: 55e74
5. Percival, M., Antioxidants. Clinical Nutrition Insights 1998; 10:1-4
6. 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.
7. 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.
8. 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.

9. Gutteridge JMC. Biological origin of free radicals, and mechanisms of antioxidant protection, Chem. Biol. Interact. 1994; 91: 133-140.
10. 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.
11. Miao L, Clair DKS. Regulation of superoxide dismutase genes: implications in disease, Free Radic. Bio. Med. 2009;47: 344-356.
12. Young IS, Woodside J V. Antioxidants in health and disease. J Clin Pathol. 2001; 54: 176-186.
13. Al-Omar MA, Beedham C, Alsarra IA. Pathological roles of reactive oxygen species and their defence mechanisms. Saudi Pharm J. 2004;12: 1-18.
14. 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.
15. 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
16. Frankel EN, Neff WE. Formation of malonaldehyde from lipid oxidation products. Biochim Biophys Acta 1983;754(3): 264-270.
17. 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
18. 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.
19. 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
20. Blair IA. DNA adducts with lipid peroxidation products,” Journal of Biological Chemistry 2008;283(23): 15545–15549.
21. 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
22. Sanyal J, Bandyopadhyay SK., Banerjee TK, Mukherjee SC, Chakraborty DP, Ray BC, et al. Plasma levels of lipid peroxides in patients with Parkinson’s disease,”European Review forMedical and Pharmacological Sciences 2009;13( 2): 129–132.
23. 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
24. 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.
25. 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.
26. 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.
27. Lotito SB, Fraga CG. (+)-Catechin prevents human plasma oxidation. Free Radic Biol Med. 1998;24: 435-441
28. Kojo S. Vitamin C: Basic metabolism and its function as an index of oxidative stress. Curr. Med. Chem. 2004; 11: 1041–1064.
29. Landis GN, Tower J. Superoxide dismutase evolution and life span regulation. Mech. Ageing Dev. 2005; 126, 365–379.
30. Sharoni Y, Danilenko M, Dubi N, Ben-Dor A, Levy J. Carotenoids and transcription. Arch. Biochem. Biophys., 2004;430: 89–96.
31. 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.
32. 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.
33. 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.
34. 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.
35. 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.
36. Fattman CL, Schaefer LM, Oury TD. Extracellular superoxide dismutase in biology and medicine. Free Radical Biology & Medicine 2003; 35(3): 236–256.
37. 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.
38. 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.
39. 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.
40. 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
41. 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.
42. Chelikani P, Fita I, Loewen PC. Diversity of structures and properties among catalases. Cell Mol Life Sci. 2004;61: 192–208.
43. Dröge W. Free radicals in the physiological control of cell function. Physiol Rev. 2002;82: 47–95.
44. 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.
45. Khan MA, Tania M, Zhang DZ, Chen HC. Antioxidant enzymes and cancer. Chinese J Cancer Res. 2010;22: 87–92.
46. Góth , Rass P, Páy A. Catalase enzyme mutations and their association with diseases. Mol Diagn. 2004;8: 141–149.
47. 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.
48. 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.
49. 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

Ayrıntılar

Birincil Dil

Türkçe

Konular

Klinik Tıp Bilimleri

Bölüm

Derleme

Yazarlar

Rahime Aslankoç ^*
Türkiye

Deniz Demirci Bu kişi benim

Ümmahan İnan Bu kişi benim

Mahmut Yıldız Bu kişi benim

Ahmet Öztürk Bu kişi benim

Mevlüt Çetin Bu kişi benim

Ecem Şirin Savran Bu kişi benim

Burak Yılmaz Bu kişi benim

Yayımlanma Tarihi

1 Eylül 2019

Gönderilme Tarihi

17 Mayıs 2019

Kabul Tarihi

24 Haziran 2019

Yayımlandığı Sayı

Yıl 2019 Cilt: 26 Sayı: 3

DOI

https://doi.org/10.17343/sdutfd.566969

IZ

https://izlik.org/JA64YX46YB

Kaynak Göster

RIS / Bibtex

APA

Aslankoç, R., Demirci, D., İnan, Ü., Yıldız, M., Öztürk, A., Çetin, M., Savran, E. Ş., & Yılmaz, B. (2019). Oksidatif stres durumunda antioksidan enzimlerin rolü - Süperoksit dismutaz (SOD), katalaz (CAT) ve glutatyon peroksidaz (GPX). Medical Journal of Süleyman Demirel University, 26(3), 362-369. https://doi.org/10.17343/sdutfd.566969

AMA

1.Aslankoç R, Demirci D, İnan Ü, vd. Oksidatif stres durumunda antioksidan enzimlerin rolü - Süperoksit dismutaz (SOD), katalaz (CAT) ve glutatyon peroksidaz (GPX). SDÜ Tıp Fak Derg. 2019;26(3):362-369. doi:10.17343/sdutfd.566969

Chicago

Aslankoç, Rahime, Deniz Demirci, Ümmahan İnan, vd. 2019. “Oksidatif stres durumunda antioksidan enzimlerin rolü - Süperoksit dismutaz (SOD), katalaz (CAT) ve glutatyon peroksidaz (GPX)”. Medical Journal of Süleyman Demirel University 26 (3): 362-69. https://doi.org/10.17343/sdutfd.566969.

EndNote

Aslankoç R, Demirci D, İnan Ü, Yıldız M, Öztürk A, Çetin M, Savran EŞ, Yılmaz B (01 Eylül 2019) Oksidatif stres durumunda antioksidan enzimlerin rolü - Süperoksit dismutaz (SOD), katalaz (CAT) ve glutatyon peroksidaz (GPX). Medical Journal of Süleyman Demirel University 26 3 362–369.

IEEE

[1]R. Aslankoç vd., “Oksidatif stres durumunda antioksidan enzimlerin rolü - Süperoksit dismutaz (SOD), katalaz (CAT) ve glutatyon peroksidaz (GPX)”, SDÜ Tıp Fak Derg, c. 26, sy 3, ss. 362–369, Eyl. 2019, doi: 10.17343/sdutfd.566969.

ISNAD

Aslankoç, Rahime - Demirci, Deniz - İnan, Ümmahan - Yıldız, Mahmut - Öztürk, Ahmet - Çetin, Mevlüt - Savran, Ecem Şirin - Yılmaz, Burak. “Oksidatif stres durumunda antioksidan enzimlerin rolü - Süperoksit dismutaz (SOD), katalaz (CAT) ve glutatyon peroksidaz (GPX)”. Medical Journal of Süleyman Demirel University 26/3 (01 Eylül 2019): 362-369. https://doi.org/10.17343/sdutfd.566969.

JAMA

1.Aslankoç R, Demirci D, İnan Ü, Yıldız M, Öztürk A, Çetin M, Savran EŞ, Yılmaz B. Oksidatif stres durumunda antioksidan enzimlerin rolü - Süperoksit dismutaz (SOD), katalaz (CAT) ve glutatyon peroksidaz (GPX). SDÜ Tıp Fak Derg. 2019;26:362–369.

MLA

Aslankoç, Rahime, vd. “Oksidatif stres durumunda antioksidan enzimlerin rolü - Süperoksit dismutaz (SOD), katalaz (CAT) ve glutatyon peroksidaz (GPX)”. Medical Journal of Süleyman Demirel University, c. 26, sy 3, Eylül 2019, ss. 362-9, doi:10.17343/sdutfd.566969.

Vancouver

1.Rahime Aslankoç, Deniz Demirci, Ümmahan İnan, Mahmut Yıldız, Ahmet Öztürk, Mevlüt Çetin, Ecem Şirin Savran, Burak Yılmaz. Oksidatif stres durumunda antioksidan enzimlerin rolü - Süperoksit dismutaz (SOD), katalaz (CAT) ve glutatyon peroksidaz (GPX). SDÜ Tıp Fak Derg. 01 Eylül 2019;26(3):362-9. doi:10.17343/sdutfd.566969