BASIC COMPONENTS OF GLUTATHION SYSTEM IN RAT ERYTHROCYTES UNDER CONDITIONS OF TOXIC DAMAGE ON THE BACKGROUND OF AN ALIMENTAL PROTEIN LACK
DOI:
https://doi.org/10.31861/biosystems2020.01.031Ключові слова:
glutathione, glutathione transferase, glutathione peroxidase, glutathione reductase, glucose-6-phosphate dehydrogenase, erythrocytesАнотація
The article is devoted to the study of the main components of the glutathione system under conditions of toxic damage against the background of nutritional protein deficiency: the content of reduced and oxidized glutathione with the determination of the GSH/GSSG ratio, the activity of glutathione-dependent enzymes – glutathione peroxidase, glutathione transferase, glutathione reductase, and glucose-6-phosphate dehydrogenase. The concentration of reduced glutathione in the erythrocyte hemolysate was studied using Elman's reagent after deproteinization of the samples. Glutathione transferase activity was determined by the rate of formation of glutathione S conjugates by reacting reduced glutathione with a substrate of 1-chloro-2.4-dinitrobenzene. Glutathione peroxidase activity was evaluated by the formation of oxidized glutathione. The activity of glutathione reductase in erythrocytes was determined by the method, is based on measuring the oxidation rate of NADPH+H+, which is recorded by decreasing absorption at a wavelength of 340 nm. A decrease in the ratio of GSH/GSSG in rat erythrocytes under conditions of toxic damage against a nutritional deficiency of protein is indicated by a functional shift in the thiol-disulfide balance towards increased use of the reduced form of
glutathione for antioxidant protection. It was established that toxic damage is a key factor in reducing the level of glutathione transferase against the background of an increase in glutathione peroxidase activity in rat erythrocytes, the activation of which probably prevents the progression of LPO processes. At the same time, under conditions of toxic damage, against the background of alimentary protein deficiency, a decrease in glutathione reductase and glucose-6-phosphate dehydrogenase activity is observed, which leads to blocking of the first stage of glucose-6-phosphate metabolism in the pentose phosphate cycle, resulting in a decrease in the amount of NADPH and, accordingly reduced glutathione.
Посилання
Aashique M., Roy A., Diamond A., Bera S. Subcellular compartmentalization of glutathione peroxidase 1 allelic isoforms differentially impact parameters of energy metabolism 2018. doi: 10.1002/jcb.27610.
Beutler E. Red cell metabolism a manual of biochemical methods. Orlando 1990. 131–134.
Beutler E. Red Cell Metabolism. New York: Grune & Stratton, 1971. 62–64.
Buko I.V., Polonetsky Moiseenok A.G. Antioxidant status and glutathione redox potential of erythrocytes in patients with acute coronary syndrome. Ukr. 114–124. doi: http://dx.doi.org/10.15407/ubj86.03.114
Cimen M.Y. Free radical metabolism in human erythrocytes. Clin Chim Acta. DOI: 10.1016/j.cca.2007.12.025.
Couto N., Wood J., Barber J. reductase and related enzymes on cellular redox homoeostasis network. Free Radic Biol Med. 95: P. 10.1016/j.freeradbiomed.2016.02.028
Dalton T.P., Chen Y., Schneider S.N., Nebert D.W., Shertzer H.G. Genetically altered mice to evaluate glutathione homeostasis in health and disease. Radic Biol Med. 2004; 37(10): 1511 10.1016/j.freeradbiomed.2004.06.040.
D'Autréaux B., Toledano M.B. ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis. Nat Rev Mol 813–824. DOI: 10.1038/nrm2256.
Deponte M. Glutathione catalysis and the reaction mechanisms of glutathione Biochim Biophys Acta. 2013; 1830(5): 3217 DOI: 10.1016/j.bbagen.2012.09.018.
Fang Y.Z., Yang S., Wu G. Free radicals, antioxidants, and nutrition. Nutrition. 2002; 18(10): 872–879. DOI: 10.1016/s0899-9007(02)00916-4.
Gavriliuc L.A., Corcimaru I.F., Robu M.V., Lisii L.T. Glutathione-dependent enzymes and glucose-6- phosphate dehydrogenase of blood in patients with lymphosarcoma (non-hodgkin’s disease). Biomeditsinskaya Khimiya. 2011. Т. 57(2): С. 225– 231. (In Russian).
Giustarini D., Colombo G., Garavaglia M.L., Astori E., Portinaro N.M., Reggiani F., Badalamenti S., Aloisi A.M., Santucci A., Rossi R., Milzani A., DalleDonne I. Assessment of glutathione/glutathione disulphide ratio and S-glutathionylated proteins in human blood, solid tissues, and cultured cells. Free Radic Biol Med. 2017; 112: 360–375. DOI: 10.1016/j.freeradbiomed.2017.08.008.
Grover Z., Ee L.C. Protein energy malnutrition. Pediatr Clin North Am. 2009; 56(5): 1055–1068. DOI: 10.1016/j.pcl.2009.07.001.
Hammond E.G., White P.J. A Brief History of Lipid Oxidation. Journal of the American Oil Chemists' Society. 2011; 88(7): 891–897. DOI: 10.1007/s11746- 011-1761-8.
Hayes J.D., Flanagan J.U., Jowsey I.R. Glutathione transferases. Annual Review of Pharmacology and Toxicology. 2005; 45: 51–88. DOI: 10.1146/annurev.pharmtox.45.120403.095857.
Holzerová E., Prokisch H. Mitochondria: Much ado about nothing? How dangerous is reactive oxygen species production? Int J Biochem Cell Biol. 2015; 63: 16–20. DOI: 10.1016/j.biocel.2015.01.021.
Jones D.P., Liang Y. Measuring the poise of thiol/disulfide couples in vivo. Free Radic Biol Med. 2009; 47(10): 1329–1338. DOI: 10.1016/j.freeradbiomed.2009.08.021.
Kalinina E.V., Chernov N.N., Novichkova M.D. The role of glutathione, glutathione transferase and glutaredoxin in the regulation of redox-dependent processes. Uspehi biologicheskoy himii. 2014; 54: 299–348. DOI: 10.1134/S0006297914130082. (In Russian).
Kamyishnikov V.C. Manual for clinical and biochemical research and laboratory diagnostics. M.: Medpressinform, 2004. 414 с. (In Russian).
Kopylchuk G.P., Voloshchuk O.M. Peculiarities of the free radical processes in rat liver mitochondria under toxic hepatitis on the background of alimentary protein deficiency. Ukr. Biochem. J. 2016; 88(2): 66– 72. DOI: 10.15407/ubj88.02.066.
Kopylchuk H.P., Nykolaichuk I.M., Zhuretska O.M. Rat liver arginase system under acetaminophen-induced toxic injury and protein deprivation. Ukr. Biochem. J. 2017; 89(2): 92–98. doi: https://doi.org/10.15407/ubj89.02.092.
Kopylchuk Н.P., Buchkovska I.M. The state of the glutathione system of liver cells of rats for low-protein diet and acute hepatotoxic injury. Ukr. Biochem. J. 2014; 86(5 Suppl 1): 165–166. (In Ukrainian).
Korzhov V.I., Zhadan V.N., Korzhov M.V. The role of the glutathione system in the processes of detoxification and antioxidant protection. Zhurnal AMN Ukrainа. 2007; 13(1): 3–19. (In Russian).
Kulinsky V.I., Kolesnichenko L.S. Glutathione system I. Synthesis, transport, glutathione transferases, glutathione peroxidases. Biomeditsinskaya Khimiya. 2009; 55(3): 255–277. (In Russian).
Kulinsky V.I., Kolesnichenko L.S. Glutathione system. II. Other enzymes, thiol-disulphide metabolism, inflammation and immunity, functions. Biomeditsinskaya Khimiya. 2009; 55(4): 365–379. (In Russian).
Kulinsky V.I., Leonova Z.A., Kolesnichenko L.S., Malov I.V., Danilov Yu.A. Glutathione system in erythrocytes and blood plasma in viral hepatites. Biomeditsinskaya Khimiya. 2007; 53(1): 91–98. (In Russian).
Kumar C., Igbaria A., D'Autreaux B., Planson A.G., Junot C., Godat E., Bachhawat A.K., DelaunayMoisan A., Toledano M.B. Glutathione revisited: a vital function in iron metabolism and ancillary role in thiol-redox control. EMBO J. 2011; 30(10): 2044– 2056. DOI: 10.1038/emboj.2011.105.
Lushchak V.I. Glutathione homeostasis and functions: potential targets for medical interventions. J Amino Acids. 2012; Article ID 736837: 26 pages, doi:10.1155/2012/736837.
Mashiko S., Ishihara A., Iwaasa H., Sano H., Ito J., Gomori A., Oda Z., Moriya R., Matsushita H., Jitsuoka M., Okamoto O., MacNeil D. J., Van der Ploeg L. H., Fukami T., Kanatani A. A pair-feeding study reveals that a Y5 antagonist causes weight loss in diet-induced obese mice by modulating food intake and energy expenditure. Mol Pharmacol. 2007; 71(2): 602–608. DOI: 10.1124/mol.106.029991.
Nagy P. Kinetics and mechanisms of thiol-disulfide exchange covering direct substitution and thiol oxidation-mediated pathways. Antioxidants & Redox Signaling. 2013;18: 1623–1641. DOI: 10.1089/ars.2012.4973.
Reeves P.G., Nielsen F.H., Fahey G.C. Jr. AIN-93 purified diets for laboratory rodents: final report of the American Institute of Nutrition ad hoc writing committee on the reformulation of the AIN-76A rodent diet. J Nutr. 1993; 123(11): 1939–1951. DOI: 10.1093/jn/123.11.1939.
Rizvi S.I., Srivastava N. L-cysteine influx in diabetic erythrocytes. Biomeditsinskaya Khimiya. 2010; 56(5): 545–551. DOI: 10.18097/pbmc20105605545. (In Russian).
Sedlak J., Lindsay R.H. Estimation of total, proteinbound, and nonprotein sulfhydryl groups in tissue with Ellman's reagent. Anal Biochem. 1968; 25(1): 192– 205. 34. Semba R.D. The Rise and Fall of Protein Malnutrition in Global Health. Ann Nutr Metab. 2016; 69(2): 79– 88. DOI: 10.1159/000449175.
Stantont R. C. Glucose-6-phosphate dehydrogenase, NADPH, and cell survival. IUBMB Life. 2012; 64(5): 362–369. DOI: 10.1002/iub.1017.
Stefanov O.V. Preclinical studies of drugs. Kyiv: Avicenna, 2001. 527 s. (In Ukrainian). 37. Van Wijk R., van Solinge W.W. The energy-less red blood cell is lost: erythrocyte enzyme abnormalities of glycolysis. Blood. 2005; 106(13): 4034–4042. DOI: 10.1182/blood-2005-04-1622.
Vlasova S.N., Shabunina E.I., Pereslegina I.A. The activity of glutathione-dependent erythrocyte enzymes in children with chronic diseases. Laboratory work. 1990; 8: 19–21. (In Russian).
Нabig W.H., Pabst M.J., Jakoby W.B. Glutathione-Stransferases. The first enzymatic step in mercapturic acid formation. J Biol Chem. 1974; 249(22): 7130– 7139.
