Preview

Журнал им. Н.В. Склифосовского «Неотложная медицинская помощь»

Расширенный поиск

СУПЕРОКСИДДИСМУТАЗА В СОСТАВЕ АНТИОКСИДАНТНОЙ ТЕРАПИИ: СОСТОЯНИЕ ВОПРОСА И ПЕРСПЕКТИВЫ (ОБЗОР ЛИТЕРАТУРЫ)

Аннотация

Оксидативный стресс, развивающийся при многих заболеваниях, является нарушением баланса между прооксидантами и антиоксидантными защитными механизмами организма. Антиоксидантные ферменты, такие как супероксиддисмутаза (СОД), играют ключевую роль в снижении оксидативного стресса в естественных условиях. Таким образом, уменьшение образования активных форм кислорода, а также активации процессов перекисного окисления липидов за счет экзогенного поступления СОД могло бы стать эффективным методом профилактики и лечения ряда заболеваний. В данной работе мы предлагаем обзор результатов экспериментальных и клинических исследований по использованию внутривенно вводимых препаратов и пищевых добавок, содержащих СОД, при лечении воспалительных, инфекционных, сердечно-сосудистых и нейродегенеративных заболеваний. В результате введения СОД большинство авторов наблюдали увеличение содержания эндогенных антиоксидантных ферментов (СОД, каталазы, глутатионпероксидазы), т.е. стимуляцию эндогенной антиоксидантной защиты, и, следовательно, снижение уровня оксидативного стресса, что может объяснять механизмы положительных наблюдаемых эффектов.

Об авторах

Т. А. Пушкина
ФГБУ «Государственный научный центр РФ — Федеральный медицинский биофизический центр им. А.И. Бурназяна» ФМБА России
Россия

ассистент кафедры восстановительной медицины, спортивной медицины, курортологии и физиотерапии с курсом сестринского дела,

Москва



Э. С. Токаев
ООО «Академия-Т»
Россия
Москва


Т. С. Попова
ГБУЗ «НИИ скорой помощи им. Н.В. Склифосовского ДЗМ»
Россия
Москва


Е. Н. Бородина
ГБУЗ «НИИ скорой помощи им. Н.В. Склифосовского ДЗМ»
Россия
Москва


Список литературы

1. Davies K.J. Oxidative stress: the paradox of aerobic life // Biochem. Soc. Symp. – 1995. – Vol. 61. – P. 1–31.

2. Heilbronn L., Smith S.R., Ravussin E. Failure of fat cell proliferation, mitochondrial function and fat oxidation results in ectopic fat storage, insulin resistance and type II diabetes mellitus // Int. J. Obes. Relat. Metab. Disord. – 2004. – Vol. 28, Suppl. 4. – S12–S21.

3. Ozata M., Mergen M., Oktenli C., et al. Increased oxidative stress and hypozincemia in male obesity // Clin. Biochem. – 2002. – Vol. 35, N. 8. – P. 627–631.

4. Reuter S., Gupta S.C., Chaturvedi M.M., Aggarwal B.B. Oxidative stress, inflammation, and cancer: How are they linked? // Free Radic. Biol. Med. – 2010. – Vol. 49, N. 11. – P. 1603–1616.

5. Keaney J.F., Larson M.G., Vasan R.S., et al. Obesity and systemic oxidative stress: clinical correlates of oxidative stress in the Framingham Study // Arterioscler Thromb. Vasc. Biol. – 2003. – Vol. 23, N. 3. – P. 434–439.

6. Halliwell B. Oxidants and human disease: some new concepts // FASEB J. – 1987. – Vol. 1, N. 5. – P. 358–364.

7. Olusi S.O. Obesity is an independent risk factor for plasma lipid peroxidation and depletion of erythrocyte cytoprotectic enzymes in humans // Int. J. Obes. Relat. Metab. Disord. – 2002. – Vol. 26, N. 9. – P. 1159–1164.

8. Шанин Ю.Н., Шанин В.Ю., Зиновьев Е.В. Антиоксидантная терапия в клинической практике. – СПб.: ЭЛБИ-СПб., 2003. – 128 с.

9. Carillon J., Fouret G., Feillet-Coudray C., et al. Short-term assessment of toxicological aspects, oxidative and inflammatory response to dietary melon superoxide dismutase in rats // Food Chem. Tox. – 2013. – Vol. 55. – P. 323–328.

10. Feillet-Coudray C., Sutra T., Fouret G., et al. Oxidative stress in rats fed a high-fat high-sucrose diet and preventive effect of polyphenols: involvement of mitochondrial and NAD(P)H oxidase systems // Free Radic. Biol. Med. – 2009. – Vol. 46, N. 5. – P. 624–632.

11. Furukawa S., Fujita T., Shimabukuro M., et al. Increased oxidative stress in obesity and its impact on metabolic syndrome // J. Clin. Invest. – 2004. – Vol. 114, N. 12. – P. 1752–1761.

12. Muchova J., Sustrova M., Garaiova I., et al. Influence of age on activities of antioxidant enzymes and lipid peroxidation products in erythrocytes and neutrophils of down syndrome patients // Free Radic. Biol. Med. – 2001. – Vol. 31, N. 4. – P. 499–508.

13. Nakajima S., Ohsawa I., Nagata K., et al. Oral supplementation with melon superoxide dismutase extract promotes antioxidant defences in the brain and prevents stress-induced impairment of spatial memory // Behav. Brain Res. – 2009. – Vol. 200, N. 1. – P. 15–21.

14. Pincemail J., Bonjean K., Cayeux K., Defraigne J.-O. Physiological action of antioxidant defences // Nutr. Clin. Metabol. – 2002. – Vol. 16. – P. 233–239.

15. Scandalios J.G. Molecular genetics of superoxide dismutase in plants // Oxidative stress and molecular biology of antioxidant defences / ed. J.G. Scandalios. – New York: Cold Spring Harbor Laboratory Press, 1997. – P. 527–568.

16. McCord J.M. The evolution of free radicals and oxidative stress // Am. J. Med. – 2000. – Vol. 108, N. 8. – P. 652–659.

17. Fridovich I. Superoxide radical and superoxide dismutases // Annu Rev. Biochem. – 1995. – Vol. 64. – P. 97–112.

18. Beyer W., Imlay J., Fridovich I. Superoxide dismutases // Prog. Nucleic. Acid. Res. Mol. Biol. – 1991. – Vol. 40. – P. 221–253.

19. Baret A., Jadot G., Michelson A.M. Pharmacokinetics and antiinflammatory properties in the rat of superoxide dismutase (CuSODs and MnSOD) from various species // Biochem. Pharmacol. – 1984. – Vol. 33, N. 17. – P. 2755–2760.

20. Clarke M.B., Wright R., Irwin D., et al. Sustained lung activity of a novel chimeric protein, SOD2/3, after intratracheal administration // Free Radic. Biol. Med. – 2010. – Vol. 49, N. 12. – P. 2032–2039.

21. Chan K., Kan Y.W. Nrf2 is essential for protection against acute pulmonary injury in mice // Proc. Natl. Acad. Sci USA. – 1999. – Vol. 96, N. 22. – P. 12731–12736.

22. Assa’ad A.H., Ballard E.T., Sebastian K.D., et al. Effect of superoxide dismutase on a rabbit model of chronic allergic asthma // Ann. Allergy Asthma Immunol. – 1998. – Vol. 80, N. 3. – P. 215–224.

23. Tanaka K., Tanaka Y., Miyazaki Y., et al. Therapeutic effect of lecithinized superoxide dismutase on pulmonary emphysema // J. Pharmacol. Exp. Ther. – 2011. – Vol. 338, N. 3. – P. 810–818.

24. Laursen J.B., Rajagopalan S., Galis Z., et al. Role of superoxide in angiotensin IIinduced but not catecholamine-induced hypertension // Circulation. – 1997. – Vol. 95, N. 3. – P. 588–593.

25. Wengenack T.M., Curran G.L., Poduslo J.F. Postischemic, systemic administration of polyamine modified superoxide dismutase reduced hippocampal CA1 neurodegeneration in rat global cerebral ischemia // Brain Res. – 1997. – Vol. 754. N. 1–2. – P. 46–54.

26. Gammer W., Broback L.G. Clinical comparison of orgotein and methylprednisolone acetate in the treatment of osteoarthrosis of the knee joint // Scand. J. Rheumatol. – 1984. – Vol. 13, N. 2. – P. 108–112.

27. Talke M. Intra-articular therapy with superoxide dismutase (orgotein) or cortisone in rheumatoid and arthritic inflammatory finger joint lesions // Handchir Mikrochir Plast Chir. – 1984. – Vol. 16, N. 1. – P. 59–63.

28. McIlwain H., Silverfield J.C., Cheatum D.E., et al. Intra-articular orgotein in osteoarthritis of the knee : a placebo-controlled efficacy, safety, and dosage comparison // Am. J. Med. – 1989. – Vol. 87, N. 3. – P. 295–300.

29. Vozenin-Brotons M.C., Sivan V., Gault N., et al. Antifibrotic action of Cu/Zn SOD is mediated by TGF-”1 repression and phenotypic reversion of myofibroblasts // Free Radic. Biol. Med. – 2001. – Vol. 30, N. 1. – P. 30–42.

30. Edeas M.A., Emerit I., Khalfoun Y., et al. Clastogenic factors in plasma of HIV-1 infected patients activate HIV-1 replication in vitro:inhibition by superoxide dismutase // Free Radic. Biol. Med. – 1997. – Vol. 23, N. 4. – P. 571–578.

31. Takehara Y., Yamaoka K., Sato E.F., et al. DNA damage by various forms of active oxygens and its inhibition by different scavengers using plasmid DNA // Physiol. Chem. Phy. Med. – 1994. – Vol. 26, N. 3. – P. 215–226.

32. Carillon J., Rugale C., Rouanet J.M., et al. Endogenous antioxidant defense induction by melon superoxide dismutase reduces cardiac hypertrophy in spontaneously hypertensive rats // Int. J. Food Sci. Nutr. – 2014. – Vol. 65, N. 5. – P. 602–609.

33. Décordé K., Ventura E., Lacan D., et al. A SOD rich melon extract ExtramelO prevents aortic lipids and liver steatosis in diet-induced model of atherosclerosis // Nutr. Metab. Cardiovasc. Dis. – 2010. – Vol. 20, N. 5. – P. 301–307.

34. Lacan D., Baccou J.C. High levels of antioxidant enzymes correlate with delayed senescence in nonnetted muskmelon fruits // Planta. – 1998. – Vol. 204, N. 3. – P. 377–382.

35. Perez-Carreras M., Del Hoyo P., Martin M.A., et al. Defective hepatic mitochondrial respiratory chain in patients with nonalcoholic steatohepatitis // Hepatology. – 2003. – Vol. 38, N. 4. – P. 999–1007.

36. Jadot G. Anti-inflammatory activity of superoxide dismutases studies on adjuvant induced polyarthritis in rats // Free Rad. Res. Comms. – 1985. – Vol. 2, N. 2. – P. 27–42.

37. Regnault C., Roch-Arveiller M., Tissot M., et al. Effect of encapsulation on the anti-inflammatory properties of superoxide dismutase after oral administration // Clin. Chim. Acta. – 1995. – Vol. 240, N. 2. – P. 117–127.

38. Webb C.B., Lehman T.L., McCord K.W. Effects of an oral superoxide dismutase enzyme supplementation on indices of oxidative stress, proviral load, and CD4:CD8 ratios in asymptomatic FIVinfected cats // J. Feline Med. Surg. – 2008. – Vol. 10, N. 5. – P. 423–430.

39. Milesi M.A., Lacan D., Brosse H., et al. Effect of an oral supplementation with a proprietary melon juice concentrate (Extramel®) on stress and fatigue in healthy people: a pilot, double-blind, placebo-controlled clinical trial // Nutr J. – 2009. – Vol. 8. – P. 40.

40. Esco R., Valencia J., Coronel P., et al. Efficacy of orgotein in prevention of late side effects of pelvic irradiation : a randomized study // Int. J. Radiat. Oncol. Biol. Phys. – 2004. – Vol. 60, N. 4. – P. 1211–1219.

41. Dugas B. Glisodin®: A nutraceutical product that promote the oral delivery of superoxide dismutase // Free Radic. Biol. Med. – 2002. – Vol. 33. – S64.

42. Décordé K., Teissedre P.L., Sutra T., et al. Chardonnay grape seed procyanidin extract supplementation prevents high-fat diet-induced obesity in hamsters by improving adipokine imbalance and oxidative stress markers // Mol. Nutr. Food Res. – 2009. – Vol. 53, N. 5. – P. 659–666.

43. Vaille A., Jadot G., Elizagaray A. Anti-inflammatory activity of various superoxide dismutases on polyarthritis in the Lewis rat // Biochem. Pharmacol. – 1990. – Vol. 39, N. 2. – P. 247–255.

44. Vouldoukis I., Lacan D., Kamate C., et al. Antioxidant and antiinflammatory properties of a Cucumis melo LC extract rich in superoxide dismutase activity // J. Ethnopharmacol. – 2004. – Vol. 94, N. 1. – P. 67–75.

45. Arangoa M.A., Campanero M.A., Renedo M.J., et al. Gliadin nanoparticles as carriers for the oral administration of lipophilic drugs. Relationships between bioadhesion and pharmacokinetics // Pharm. Res. – 2001. – Vol. 18, N. 11. – P. 1521–1527.

46. Lund-Olesen K., Menander-Huber K.B. Intra-articular orgotein therapy in osteoarthritis of the knee. A double-blind, placebo-controlled trial // Arzneimittelforschung. – 1983. – Vol. 33, N. 8. – P. 1199–1203.

47. Antonic V., Rabbani Z.N., Jackson I.L., Vujaskovic Z. Subcutaneous administration of bovine superoxide dismutase protects lungs from radiation induced lung injury // Free Radic. Res. – 2015. – Vol. 49, N. 10 – P. 1259–1268.

48. Sorescu D., Griendling K.K. Reactive oxygen species, mitochondria, and NAD(P)H oxidases in the development and progression of heart failure // Congest. Heart Fail. – 2002. – Vol. 8, N. 3. – P. 132–140.

49. Lallès J.P., Bosi P., Smidt H., Stokes C.R. Nutritional management of gut health in pigs around weaning // Proc Nutr Soc. – 2007. – Vol. 66, N. 2. – P. 260–268.

50. Okada F., Shionoya H., Kobayashi M., et al. Prevention of inflammationmediated acquisition of metastatic properties of benign mouse fibrosarcoma cells by administration of an orally available superoxide dismutase // Brit. J. Cancer. – 2006. – Vol. 94, N. 6. – P. 854–862.

51. Vouldoukis I., Conti M., Krauss P., et al. Supplementation with Gliadincombined plant superoxide dismutase extract promotes antioxidant defences and protects against oxidative stress // Phytother. Res. – 2004. – Vol. 18, N. 12. – P. 957–962.

52. Lalles J.P., Lacan D., David J.C. A melon pulp concentrate rich in superoxide dismutase reduces stress proteins along the gastrointestinal tract of pigs // Nutrition. – 2011. – Vol. 27, N. 3. – P. 358–363.

53. Rosenfeld W.N., Davis J.M., Parton L., et al. Safety and pharmacokinetics of recombinant human superoxide dismutase administered intratracheally to premature neonates with respiratory distress syndrome // Pediatrics. – 1996. – Vol. 97, N. 6 (Pt. 1). – P. 811–817.

54. Nelson S.K., Bose S.K., Grunwald G.K., et al. The induction of human superoxide dismutase and catalase in vivo: A fundamentally new approach to antioxidant therapy // Free Radic. Biol. Med. – 2006. – Vol. 40, N. 2. – P. 341–347.

55. Skarpanska-Stejnborn A., Pilaczynska-Szczesniak L., Basta P., et al. Effects of oral supplementation with plant superoxide dismutase extract on selected redox parameters and an inflammatory marker in a 2,000-m rowing-ergometer test // Int. J. Sport. Nutr. Exerc. Metab. – 2011. – Vol. 21, N. 2. – P. 124–134.

56. Izumi M., McDonald M.C., Sharpe M.A., et al. Superoxide dismutase mimetics with catalase activity reduce the organ injury in hemorrhagic shock // Shock. – 2002. – Vol. 18, N. 3. – P. 230–235.

57. Gonzalez P.K., Zhuang J., Doctrow S.R., et al. EUK-8, a synthetic superoxide dismutase and catalase mimetic, ameliorates acute lung injury in endotoxemic swine // J. Pharmacol. Exp. Ther. – 1995. – Vol. 275, N. 2. – P. 798–806.

58. Juurlink B.H. Dietary Nrf2 activators inhibit atherogenic processes // Atherosclerosis. – 2012. – Vol. 225, N. 1. – P. 29–33.

59. Negi G., Kumar A., Joshi R.P., Sharma S.S. Oxidative stress and Nrf2 in the pathophysiology of diabetic neuropathy: old perspective with a new angle // Biochem. Biophys. Res. Commun. – 2011. – Vol. 408. – P. 1–5.

60. Pedruzzi L.M., Stockler-Pinto M.B., Leite M.J., Mafra D. Nrf2-keap1 system versus NF-kB: The good and the evil in chronic kidney disease? // Biochimie. – 2012. – Vol. 94, N. 12. – P. 2461–2466.


Рецензия

Для цитирования:


Пушкина Т.А., Токаев Э.С., Попова Т.С., Бородина Е.Н. СУПЕРОКСИДДИСМУТАЗА В СОСТАВЕ АНТИОКСИДАНТНОЙ ТЕРАПИИ: СОСТОЯНИЕ ВОПРОСА И ПЕРСПЕКТИВЫ (ОБЗОР ЛИТЕРАТУРЫ). Журнал им. Н.В. Склифосовского «Неотложная медицинская помощь». 2016;(4):42-47.

For citation:


Pushkina T.A., Tokayev E.S., Popova T.S., Borodina E.N. SUPEROxIDE DISMUTASE AS A COMPONENT OF ANTIOxIDANT THERAPY: CURRENT STATE OF THE ISSUE AND PROSPECTS. A LITERATURE REVIEW. Russian Sklifosovsky Journal "Emergency Medical Care". 2016;(4):42-47. (In Russ.)

Просмотров: 1926


Creative Commons License
Контент доступен под лицензией Creative Commons Attribution 4.0 License.


ISSN 2223-9022 (Print)
ISSN 2541-8017 (Online)