Ukr.Biochem.J. 2022; Volume 94, Issue 1, Jan-Feb, pp. 105-113


The NADH-ubiquinone reductase and succinate dehydrogenase activity in the rat kidney mitochondria under the conditions of different protein and sucrose content in the diet

O. M. Voloshchuk*, М. S. Ursatyy, G. P. Kopylchuk

Yuriy Fedkovych Chernivtsi National University, Institute of Biology, Chemistry and Natural Resources, Ukraine;

Received: 11 November 2021; Accepted: 21 January 2022

The NADH-ubiquinone reductase (EC and succinate dehydrogenase (EC activity, the levels of total ubiquinone and its redox forms, and the degree of oxidative modification of mitochondrial proteins in the rat kidney were investigated. It was found that when consuming a low-protein diet there is a decrease in NADH-ubiquinone reductase and succinate dehydrogenase activity by 1.4-1.7 times, a 20% decrease in total ubiquinone and a quantitative redistribution of its oxidized and reduced form with a predominance of oxidized form. Under the studied conditions, there is no accumulation of carbonyl derivatives, but the level of free SH-groups is significantly reduced compared with control. At the same time, in animals consuming a high-sucrose diet there is an increase in NADH-ubiquinone reductase and succinate dehydrogenase activity by 1.5-2 times and maintenance of the total ubiquinone at the control level against the background of redistribution of its redox forms, namely a decrease in reduced ubiquinone and an increase in oxidized ubiquinone on average by 1.5 times. In addition, there is an intensification of the reactions of free radical damage of mitochondrial proteins in kidney cells, as evidenced by an increase in the level of carbonyl derivatives and a significant decrease in the level of free protein SH-groups by approximately 1.4-1.5 times. The most pronounced changes in the studied indicators are found in animals that consumed a low-protein/high-sucrose diet. In particular, an excessive consumption of sucrose on the background of protein deficiency is accompanied by a reduction of NADH-ubiquinone reductase and succinate dehydrogenase activity by 1.7-2 times, a decrease in total ubiquinone level by approximately 1.4 times, and a two-fold decrease in reduced ubiquinone against the background of intensification of the free radical oxidation of mitochondrial proteins, which can be considered as a prerequisite for the impairment of the renal function under the conditions of carbohydrate-protein imbalance.

Keywords: , , , , , ,


  1. Oliveira DT, Fernandes IDC, Sousa GG, Santos TAPD, de Paiva NCN, Carneiro CM, Evangelista EA, Barboza NR, Guerra-Sá R. High-sugar diet leads to obesity and metabolic diseases in ad libitum -fed rats irrespective of caloric intake. Arch Endocrinol Metab. 2020;64(1):71-81. PubMed, CrossRef
  2. Voloshchuk ON, Stus YuV , Kopylchuk GP. Features of free radical processes in the liver of rats with a nutrient imbalance. Biomed Khim. 2020;66(5):386-391. (In Russian). PubMed, CrossRef
  3. Le Couteur DG, Solon-Biet SM, Parker BL, Pulpitel T, Brandon AE, Hunt NJ, Wali JA, Gokarn R, Senior AM, Cooney GJ, Raubenheimer D, Cogger VC, James DE, Simpson SJ. Nutritional reprogramming of mouse liver proteome is dampened by metformin, resveratrol, and rapamycin. Cell Metab. 2021;33(12):2367-2379.e4. PubMed, CrossRef
  4. Sánchez-Solís CN, Cuevas Romero E, Soto-Rodríguez I, de Lourdes Arteaga-Castañeda M, León-Ramírez YMD, Rodríguez-Antolín J, Nicolás-Toledo L. High-sucrose diet potentiates hyperaldosteronism and renal injury induced by stress in young adult rats. Clin Exp Pharmacol Physiol. 2020;47(12):1985-1994. PubMed, CrossRef
  5. Mahajan MS, Upasani CD, Upaganlawar AB, Gulecha VS. Renoprotective effect of co-enzyme Q10 and N-acetylcysteine on streptozotocin-induced diabetic nephropathy in rats. Int J Diabetes Clin Res. 2020;7(2):1-12. CrossRef
  6. Mise K, Galvan DL, Danesh FR. Shaping Up Mitochondria in Diabetic Nephropathy. Kidney360. 2020;1(9):982-992. PubMed, PubMedCentral, CrossRef
  7. Engeham S, Mdaki K, Jewell K, Austin R, Lehner AN, Langley-Evans SC. Mitochondrial respiration is decreased in rat kidney following fetal exposure to a maternal low-protein diet. J Nutr Metab. 2012;2012:989037. PubMed, PubMedCentral, CrossRef
  8. Srivastava SP, Kanasaki K, Goodwin JE. Loss of Mitochondrial Control Impacts Renal Health. Front Pharmacol. 2020;11:543973. PubMed, PubMedCentral, CrossRef
  9. Bhargava P, Schnellmann RG. Mitochondrial energetics in the kidney. Nat Rev Nephrol. 2017;13(10):629-646. PubMed, PubMedCentral, CrossRef
  10. Duann P, Lin PH. Mitochondria Damage and Kidney Disease. Adv Exp Med Biol. 2017;982:529-551.  PubMed, PubMedCentral, CrossRef
  11. Hallan S, Sharma K. The Role of Mitochondria in Diabetic Kidney Disease. Curr Diab Rep. 2016;16(7):61. PubMed, CrossRef
  12. Itoh H, Komatsuda A, Ohtani H, Wakui H, Imai H, Sawada K, Otaka M, Ogura M, Suzuki A, Hamada F. Mammalian HSP60 is quickly sorted into the mitochondria under conditions of dehydration. Eur J Biochem. 2002;269(23):5931-5938. PubMed, CrossRef
  13. Sharova IV, Vekshin NL. Rotenone-insensitive NADH oxydation in mitochondrial suspension occurs by NADH dehydrogenase of respiratory chain fragments. Biofizika. 2004;49(5):814-821. PubMed
  14. Ahmad F, Alamoudi W, Haque S, Salahuddin M, Alsamman K. Simple, reliable, and time-efficient colorimetric method for the assessment of mitochondrial function and toxicity. Bosn J Basic Med Sci. 2018;18(4):367-374. PubMed, PubMedCentral, CrossRef
  15. Pumphrey AM, Redfearn ER. A method for determining the concentration of ubiquinone in mitochondrial preparations. Biochem J. 1960;76(1):61-64. PubMed, PubMedCentral, CrossRef
  16. Kitagawa Y, Sugimoto E. Estimation of the in vivo translational activity of rat liver mitochondria without use of an antibiotic. J Biochem. 1980;88(3):689-693.  PubMed, CrossRef
  17. Parihar MS, Pandit MK. Free radical induced increase in protein carbonyl is attenuated by low dose of adenosine in hippocampus and mid brain: implication in neurodegenerative disorders. Gen Physiol Biophys. 2003;22(1):29-39. PubMed
  18. Murphy ME, Kehrer JP. Oxidation state of tissue thiol groups and content of protein carbonyl groups in chickens with inherited muscular dystrophy. Biochem J. 1989;260(2):359-364. PubMed, PubMedCentral,CrossRef
  19. Fotheringham AK, Solon-Biet SM, Bielefeldt-Ohmann H, McCarthy DA, McMahon AC, Ruohonen K, Li I, Sullivan MA, Whiddett RO, Borg DJ, Cogger VC, Ballard WO, Turner N, Melvin RG, Raubenheimer D, Le Couteur DG, Simpson SJ, Forbes JM. Kidney disease risk factors do not explain impacts of low dietary protein on kidney function and structure. iScience. 2021;24(11):103308. PubMed, PubMedCentral, CrossRef
  20. Hasegawa S, Tanaka T, Saito T, Fukui K, Wakashima T, Susaki EA, Ueda HR, Nangaku M. The oral hypoxia-inducible factor prolyl hydroxylase inhibitor enarodustat counteracts alterations in renal energy metabolism in the early stages of diabetic kidney disease. Kidney Int. 2020;97(5):934-950. PubMed, CrossRef
  21. Sun J, Zhu H, Wang X, Gao Q, Li Z, Huang H. CoQ10 ameliorates mitochondrial dysfunction in diabetic nephropathy through mitophagy. J Endocrinol. 2019;240(3):445-465. PubMed, CrossRef
  22. Varela-López A, Giampieri F, Battino M, Quiles JL. Coenzyme Q and its role in the dietary therapy against aging. Molecules. 2016;21(3):373. PubMed, PubMedCentral, CrossRef
  23. Timoshchuk SV, Vavilova HL, Strutyns’ka NA, Talanov SA, Petukhov DM, Kuchmenko OB, Donchenko HV, Sahach VF. Cardioprotective action of coenzyme Q in conditions of its endogenous synthesis activation in cardiac ischemia-reperfusion in old rats. Fiziol Zh. 2009;55(4):58-63. (In Ukrainian). PubMed
  24. Saini R. Coenzyme Q10: The essential nutrient. J Pharm Bioallied Sci. 2011;3(3):466-467. PubMed, PubMedCentral, CrossRef
  25. Chung HS, Wang SB, Venkatraman V, Murray CI, Van Eyk JE. Cysteine oxidative posttranslational modifications: emerging regulation in the cardiovascular system. Circ Res. 2013;112(2):382-392. PubMed, PubMedCentral, CrossRef
  26. Ametov AS, Solov’eva OL. Oxidative stress in type 2 diabetes mellitus and methods for its correction. Probl Endocrinol. 2011;57(6):52-56. (In Russian). CrossRef

Creative CommonsThis work is licensed under a Creative Commons Attribution 4.0 International License.