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Роль окислительного стресса в формировании адаптивных процессов в организме
DOI: https://doi.org/10.29296/24999490-2024-03-02
Введение. Окислительный стресс (ОС) возникает при различных патологических процессах, выступая в качестве неспецифического звена их патогенеза. Меньше известно о его физиологической роли. Цель. Анализ результатов данных мировой литературы и собственных исследований об участии ОС в формировании процессов адаптации в организме, в условиях воздействия на него неблагоприятных факторов внешней среды. Методы. Анализ результатов исследований, опубликованных в российских и международных базах данных (Pubmed, Elsevier), касающихся физиологической роли ОС, опубликованных за последние 20 лет. Результаты. В статье представлены многочисленные сведения о том, что ОС выступает в роли неспецифического звена адаптации организма. Реализация его физиологических эффектов связана с изменением редокс-состояния цитоплазмы и митохондрий клетки, что приводит к обратимому окислению внутриклеточных белков и способствует модуляции их свойств. В результате этого изменяется синтез и модулируется проявление активности целого ряда внутриклеточных белков (ферментов, шаперонов, факторов транскрипции), обеспечивающих защиту от действия повреждающих факторов. Заключение. Авторы делают заключение о нецелесообразности использования антиоксидантов для лечения и профилактики заболеваний, патогенез которых связан с возникновением умеренного ОС (окислительного эустресса).
Ключевые слова:
окислительный стресс, активные формы кислорода, антиоксиданты, альтерация, адаптация
Для цитирования:
Давыдов В.В., Шестопалов А.В., Румянцев С.А. Роль окислительного стресса в формировании адаптивных процессов в организме. Молекулярная медицина, 2024; (3): 10-20https://doi.org/10.29296/24999490-2024-03-02
Список литературы:
- Sies H., Bemdt C., Jones D.P. Oxidative Stress. Annu Rev Biochem. 2017; 86: 715–48. DOI: 10.1146/annurev-biochem-061516-045037
- Miller I.P., Pavlović I., Poljšak B., Šuput D., Milisav I. Beneficial Role of ROS in Cell Survival: Moderate Increases in H2O2 Production Induced by Hepatocyte Isolation Mediate Stress Adaptation and Enhanced Survival. Antioxidants (Basel). 2019; 8 (10): 434. DOI: 10.3390/antiox8100434
- Wilson C., Muñoz-Palma E., González-Billault C. From birth to death: A role for reactive oxygen species in neuronal development. Semin Cell Dev Biol. 2018; 80: 43–9. DOI: 10.1016/j.semcdb.2017.09.012
- Jialin Li, Zhe Wang, Can Li , Yu Song, Yan Wang, Hai Bo, Yong Zhang. Impact of Exercise and Aging on Mitochondrial Homeostasis in Skeletal Muscle: Roles of ROS and Epigenetics. Cells. 2022; 11 (13): 2086. DOI: 10.3390/cells11132086.
- Ramirez A., Vázquez-Sánchez A.Y., Carrión-Robalino N., Camacho J. Ion Channels and Oxidative Stress as a Potential Link for the Diagnosis or Treatment of Liver Diseases. Oxid Med Cell Longev. 2016; 2016: 3928714. DOI: 10.1155/2016/3928714
- Roginsky V.A., Tashlitsky V.N., Skulachev V.P. Chain-breaking antioxidant activity of reduced forms of mitochondria-targeted quinones, a novel type of geroprotectors. Aging (Albany NY). 2009; 1 (5): 481–9. DOI: 10.18632/aging.100049
- Ye Y., Li J., Yuan Z. Effect of antioxidant vitamin supplementation on cardiovascular outcomes: a meta-analysis of randomized controlled trials. PLoS One. 2013; 8 (2): e56803. DOI: 10.1371/journal.pone.0056803
- Myung S.K., Ju W., Cho B., Oh S.W., Park S.M. Efficacy of vitamin and antioxidant supplements in prevention of cardiovascular disease: systematic review and meta-analysis of randomised controlled trials. BMJ. 2013; 346: f10. DOI: 10.1136/bmj.f10
- Baoyi Zhang, Cunyao Pan, Chong Feng, Changqing Yan, Yijing Yu, Zhaoli Chen, Changjiang Guo, Xinxing Wang. Role of mitochondrial reactive oxygen species in homeostasis regulation. Redox Rep. 2022; 27 (1): 45–52. DOI: 10.1080/13510002.2022.2046423
- Fuhrmann D.C., Brüne B. Mitochondrial composition and function under the control of hypoxia. Redox Biol. 2017; 12: 208–15. DOI: 10.1016/j.redox.2017.02.012
- Lennicke C., Cochemé H.M. Redox metabolism: ROS as specific molecular regulators of cell signaling and function. Mol Cell. 2021; 81 (18): 3691–707. DOI: 10.1016/j.molcel.2021.08.018
- Antonucci S., Lisa F.D., Kaludercic N. Mitochondrial reactive oxygen species in physiology and disease. Cell Calcium. 2021; 94: 102344. DOI: 10.1016/j.ceca.2020.102344
- Sies H., Jones D.P. Reactive oxygen species (ROS) as pleiotropic physiological signalling agents. Nat Rev Mol Cell Biol. 2020; 21 (7): 363–83. DOI: 10.1038/s41580-020-0230-3
- Wang R.S., Oldham W.M., Maron B.A., Loscalzo J. Systems Biology Approaches to Redox Metabolism in Stress and Disease States. Antioxid Redox Signal. 2018; 29 (10): 953–72. DOI: 10.1089/ars.2017.7256
- Sies H. Hydrogen peroxide as a central redox signaling molecule in physiological oxidative stress: Oxidative eustress. Redox Biol. 2017; 11: 613–9. DOI:10.1016/j.redox.2016.12.035
- Ježek P., Holendová B., Plecitá-Hlavatá L. Redox Signaling from Mitochondria: Signal Propagation and Its Targets. Biomolecules. 2020; 10 (1): 93. DOI: 10.3390/biom10010093
- Parvez S., Long M.J.C., Poganik J.R., Aye Y. Redox Signaling by Reactive Electrophiles and Oxidants. Chem Rev. 2018; 118 (18): 8798–888. DOI: 10.1021/acs.chemrev.7b00698
- Sies H. Findings in redox biology: From H2O2 to oxidative stress. J. Biol. Chem. 2020; 295 (39): 13458–73. DOI: 10.1074/jbc.X120.015651
- Wang Y., Branicky R., Noë A., Hekimi S. Superoxide dismutases: Dual roles in controlling ROS damage and regulating ROS signaling. J. Cell. Biol. 2018; 217 (6): 1915–28. DOI: 10.1083/jcb.201708007
- Andreyev A.Y., Kushnareva Y.E., Starkova N.N., Starkov A.A. Metabolic ROS Signaling: To Immunity and Beyond. Biochemistry (Mosc). 2020; 85 (12): 1650–67. DOI: 10.1134/S0006297920120160
- Aslihan T.A., Suter D.M. The role of NADPH oxidases in neuronal development. Free Radic Biol Med. 2020; 154: 33–47. DOI: 10.1016/j.freeradbiomed.2020.04.027
- Konno T., Melo E.P., Chambers J.E., Avezov E. Intracellular Sources of ROS/H2O2 in Health and Neurodegeneration: Spotlight on Endoplasmic Reticulum. Cells. 2021; 10 (2): 233. DOI: 10.3390/cells10020233
- Roscoe J.M., Sevier C.S. Pathways for Sensing and Responding to Hydrogen Peroxide at the Endoplasmic Reticulum. Cells. 2020; 9 (10): 2314. DOI: 10.3390/cells9102314
- Wu M.Y., Yiang G.T., Liao W.T., Tsai A.P., Cheng Y.L., Cheng P.W., Li C.Y., Li C.J. Current Mechanistic Concepts in Ischemia and Reperfusion Injury. Cell Physiol Biochem. 2018; 46 (4): 1650–67. DOI: 10.1159/000489241
- Garrido Ruiz D., Sandoval-Perez A., Rangarajan A.V., Gunderson E.L., Jacobson M.P. Cysteine Oxidation in Proteins: Structure, Biophysics, and Simulation. Biochemistry. 2022; 61 (20): 2165–76. DOI: 10.1021/acs.biochem.2c00349
- Groitl B., Jakob U. Thiol-based redox switches. Biochim Biophys Acta. 2014; 1844 (8): 1335–43. DOI: 10.1016/j.bbapap.2014.03.007
- Sies H. Oxidative stress: a concept in redox biology and medicine. Redox Biol. 2015; 4: 180–3. DOI: 10.1016/j.redox.2015.01.002
- Laskar A.A., Younus H. Aldehyde toxicity and metabolism: the role of aldehyde dehydrogenases in detoxification, drug resistance and carcinogenesis. Drug Metab Rev. 2019; 51 (1): 42–64. DOI: 10.1080/03602532.2018.1555587
- Uchida K. 4-hydroxy-2-nonenal: a product and mediator of oxidative stress. Prog Lipid Res. 2003; 42 (4): 318–43. DOI: 10.1016/s0163-7827(03)00014-6
- Brown D.I., Griendling K.K. Regulation of Signal Transduction by Reactive Oxygen Species in the Cardiovascular System. Circ Res. 2015; 116: 531–49. DOI: 10.1161/CIRCRESAHA.116.303584
- Плотников Е.Ю., Силачев Д.Н., Янкаускас С.С., Рокитская Т.И., Чупыркина А.А., Певзнер И.Б., Зорова Л.Д., Исаев Н.К., Антоненко Ю.Н., Скулачев В.П., Зоров Д.Б. Частичное разобщение дыхания и фосфорилирования как один из путей реализации нефро- и нейропротекторного действия проникающих катионов семейства SkQ. Биохимия. 2012; 77 (9): 1240–50. DOI :10.1134/S000629791209010. [Plotnikov E. Y., Silachev D. N., Jankauskas S. S., Rokitskaya T. I., Chupyrkina A. A., Pevzner I. B., Zorova L. D., Isaev N. K., Antonenko Y. N., Skulachev V. P., Zorov D. B. Mild uncoupling of respiration and phosphorylation as a mechanism providing nephro- and n europrotective effects of penetrating cations of the SkQ family. Biochemistry (Mosc). 2012; 77 (9): 1240–50 (in Russian)]
- Li J., Zhang Z., Bo H., Zhang Y. Exercise couples mitochondrial function with skeletal muscle fiber type via ROS-mediated epigenetic modification. Free Radic Biol Med. 2024; 213: 409–25. DOI: 10.1016/j.freeradbiomed.2024.01.036. Epub 2024 Jan 29. PMID: 38295887.
- Tossounian M.A., Zhang B., Gout I. The Writers, Readers, and Erasers in Redox Regulation of GAPDH. Antioxidants (Basel). 2020; 9 (12): 1288. DOI: 10.3390/antiox9121288
- Winterbourn C.C. Biological Production, Detection, and Fate of Hydrogen Peroxide. Antioxid Redox Signal. 2018; 29: 541–51. DOI: 10.1089/ars.2017.7425
- Zhang H., Gong W., Wu S., Perrett S. Hsp70 in Redox Homeostasis. Cells. 2022; 11 (5): 829. DOI: 10.3390/cells11050829
- Reczek C.R., Chandel N.S. ROS-dependent signal transduction. Curr Opin Cell Biol. 2015; 33: 8–13. DOI: 10.1016/j.ceb.2014.09.010
- Zhang H.F., Wang J.H., Wang Y.L., Gao C., Gu Y.T., Huang J., Wang J.H., Zhang Z. Salvianolic Acid A Protects the Kidney against Oxidative Stress by Activating the Akt/GSK-3β/Nrf2 Signaling Pathway and Inhibiting the NF-κB Signaling Pathway in 5/6 Nephrectomized Rats. Oxid Med Cell Longev. 2019; 18: 2853534. DOI: 10.1155/2019/2853534
- Liu S., Pi J., Zhang Q. Signal amplification in the KEAP1-NRF2-ARE antioxidant response pathway. Redox Biol. 2022; 54: 102389. DOI: 10.1016/j.redox.2022.102389
- Shaw P., Chattopadhyay A. Nrf2-ARE signaling in cellular protection: Mechanism of action and the regulatory mechanisms. J Cell Physiol. 2020; 235 (4): 3119–30. DOI: 10.1002/jcp.29219
- 40. Guo Z., Mo Z. Keap1-Nrf2 signaling pathway in angiogenesis and vascular diseases. J. Tissue Eng Regen Med. 2020; 202014 (6): 869–83. DOI: 10.1002/term.3053
- Hu B., Wei H., Song Y., Chen M., Fan Z., Qiu R., Zhu W., Xu W., Wang F. NF-κB and Keap1 Interaction Represses Nrf2-Mediated Antioxidant Response in Rabbit Hemorrhagic Disease Virus Infection. J. Virol. 2020; 94 (10): e00016-20. DOI: 10.1128/JVI.00016-20
- Basse A.L., Isidor M.S., Winther S., Skjoldborg N.B. Regulation of glycolysis in brown adipocytes by HIF-1α. Sci Rep. 2017; 7 (1): 4052. DOI: 10.1038/s41598-017-04246-y
- Zhao X., Liu L., Li R., Wei X., Luan W., Liu P., Zhao J. Hypoxia –inducible factor 1-α (HIF-1α) induces apoptosis of human uterosacral ligament fibroblasts through the death receptor and mitochondrial pathways. Med Sci Moit, 2018; 24: 8722–33. DOI: 10.12659/MSM.913384
- Mylonis I., Simos G., Paraskeva I. Hypoxia-Inducible Factors and the Regulation of Lipid Metabolism. Cells. 2019; 8: E214. DOI: 10.3390/cells8030214
- Shu S., Wang Y., Zheng M., Liu Z., Cai J., Tang C., Dong Z. Hypoxia and Hypoxia-Inducible Factors in Kidney Injury and Repair. Cells. 2019; 8 (3): 207. DOI: 10.3390/cells8030207.
- Bassoy E.Y., Walch M., Martinvalet D. Reactive Oxygen Species: Do They Play a Role in Adaptive Immunity? Front Immunol. 2021; 12: 755856. DOI: 10.3389/fimmu.2021.755856
- Меерсон Ф.З. Патогенез и предупреждение стрессорных и ишемических повреждений сердца. М.: Медицина, 1984; 270. [Meerson F.Z.Pathogenesis and prevention of ress and ischemi c injures of heart. M.: Medicina, 1984; 270 (in Russian)]
- Du Y., Demillard L.J., Ren J. Catecholamine-induced cardiotoxicity: A critical element in the pathophysiology of stroke-induced heart injury. Life Sci. 2021; 287: 120106. DOI: 10.1016/j.lfs.2021.120106
- Davydov V.V., Bozhkov A.I., Grabovetskaya E.R. Age-related peculiarities of change in content of free radical oxidation products in muscle during stress. Fron Biol. 2014; 9 (4): 283–6. DOI: 10.1007/s11515-014-1315-1
- Podszun M.C., Chung J.Y., Ylaya K., Kleiner D.E., Hewitt S.M., Rotman Y. 4-HNE Immunohistochemistry and Image Analysis for Detection of Lipid Peroxidation in Human Liver Samples Using Vitamin E Treatment in NAFLD as a Proof of Concept. J Histochem Cytochem. 2020; 68 (9): 635–43. DOI: 10.1369/0022155420946402
- Ene C.D., Georgescu S.R., Tampa M., Matei C., Mitran C.I., Mitran M.I., Penescu M.N., Nicolae I. Cellular Response against Oxidative Stress, a Novel Insight into Lupus Nephritis Pathogenesis. J. Pers Med. 2021; 11 (8): 693. DOI: 10.3390/jpm11080693
- Van der Pol A., van Gilst W.H., Voors A., van der Meer P. Treating oxidative stress in heart failure: past, present and future. Eur. J. Heart Fail. 2019; 21 (4): 425–35. DOI: 10.1002/ejhf.1320
- Davydov V.V., Bozhkov A.I., Dobaeva N.M. Possible role of alteration of aldehyde’s scavenger enzymes during aging. Exp Gerontol. 2004; 39 (1): 11–6. DOI: 10.1016/j.exger.2003.08.009
- Davydov V.V. Age-dependent change in aldo-keto reductases composition in the blood of rats. Am. J. Biomed Life Sci. 2014; 2 (6–1): 1–4. DOI: 10.11648/j.ajbls.s.2014020601.11