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ISSN 2522-9028 (Print)
ISSN 2522-9036 (Online)
DOI: https://doi.org/10.15407/fz

Fiziologichnyi Zhurnal

is a scientific journal issued by the

Bogomoletz Institute of Physiology
National Academy of Sciences of Ukraine

Editor-in-chief: V.F. Sagach

The journal was founded in 1955 as
1955 – 1977 "Fiziolohichnyi zhurnal" (ISSN 0015 – 3311)
1978 – 1993 "Fiziologicheskii zhurnal" (ISSN 0201 – 8489)
1994 – 2016 "Fiziolohichnyi zhurnal" (ISSN 0201 – 8489)
2017 – "Fiziolohichnyi zhurnal" (ISSN 2522-9028)

Fiziol. Zh. 2020; 66(6): 82-87


THE RATIO OF UBIQUINON REDOX FORMS IN THE RAT LIVER MITOCHONDRIA UNDER CONDITIONS OF DIFFERENT NUTRIENT SUPPLY

O.M. Voloshchuk, G. P. Kopylchuk, М.S. Ursatyу

    Yuriy Fedkovych Chernivtsi National University, Ukraine
DOI: https://doi.org/10.15407/fz66.06.082

Abstract

The relationship between the quantitative ratio of redox forms of ubiquinone and the degree of free radical damage to mitochondrial proteins in rat liver against the background of nutritional imbalance was investigated. The animals were divided into the following experimental groups: I – animals receiving full-value semi-synthetic ration (control group); II – animals receiving high-sucrose diet; III – animals receiving low-protein high-sucrose diet. The content of total and oxidized ubiquinone was determined spectrophotometrically at 275 nm, the content of reduced ubiquinone was determined by the difference between the content of total and oxidized ubiquinone. The intensity of the oxidative modification of proteins was assessed by the accumulation of carbonyl derivatives in the reaction with 2,4-dinitrophenylhydrazine (2,4-DNPH), the content of free SH-groups was assessed by using the Elman reagent. It was found that the most pronounced decrease in the content of total ubiquinone (almost twice) and the redistribution of its redox forms (reduction of the content of reduced ubiquinone by 7.2 times against the background of an increase in the level of oxidized ubiquinone by 2 times) in rat liver mitochondria is observed in animals that received a diet high in sucrose against the background of alimentary protein deprivation. In addition, the animals of this group showed the most pronounced free radical oxidation of mitochondrial proteins, as evidenced by a 3.5-fold increase in the content of carbonyl derivatives and a 2.6-fold decrease in the content of free protein SH- groups. It was shown that nutritional protein deficiency is a critical factor affecting the intensity of free radical processes in mitochondria. The established changes in the ratio of the redox forms of ubiquinone and the degree of oxidative modification of mitochondrial proteins in rat liver could be considered as prerequisites for deepening the energy imbalance and violation of the functional activity of mitochondria under conditions of nutritional imbalance.

Keywords: mitochondria; ubiquinone; oxidative modification of proteins; nutrients.

References

  1. Mantle D, Hargreaves I. Coenzyme Q10 and degenerative disorders affecting longevity: an overview. Antioxidants. 2019 Feb;8(44):1-10. CrossRef PubMed PubMedCentral
  2. Varela-López A, Giampieri F, Battino M, Quiles JL. Coenzyme Q and its role in the dietary therapy against aging. Molecules. 2016 Mar;21(373):1-26. CrossRef PubMed PubMedCentral
  3. Casagrande D, Waib PH, Jordão Júnior AA. Mechanisms of action and effects of the administration of Coenzyme Q10 on metabolic syndrome. J Nutr Intermed Metab. 2018 Aug;13:26-32. CrossRef
  4. Strutynska NA, Timoshchuk SV, Vavilova GL, Kotsuruba AV, Sagach VF. Expression of mitochondrial uncoupling protein 3 and the sensitivity of mitochondrial permeability transition pore opening to Ca2+ in old rat heart under activation of biosynthesis of coenzyme Q. Fiziol Zh. 2009;55(3):44-54. [Ukrainian].
  5. Voloshchuk ON, Kopylchuk GP, Holinei TYu. Biochemical markers of the functional state of liver in rats fed diets with different protein and sucrose content. Vopr Pitan. 2019 Nov;88(6):61-7. [Russian].
  6. Sinha S, Patro N, Patro IK. Maternal protein malnutrition: current and future perspectives of spirulina supplementation in neuroprotection. Front Neurosci. 2018 Dec;12(988):1-18. CrossRef PubMed PubMedCentral
  7. Litvitsky PF, Mal'tseva LD. Protein, amino acids and nucleic acids metabolism disorders. Vopr Sovremen Pediatr. 2015 Feb;14(1):95-107. [Russian]. CrossRef
  8. Voloshchuk ON, Kopylchuk GP. Characteristics of water-salt balance in protein-deficiency rats with acetaminophen-induced toxic injury. Fiziol Zh. 2019 Feb;65(3):28-33. [Ukrainian]. CrossRef
  9. Falfushynska HI, Horyn OI, Gnatyshyna LL, Buyak BB, Rusnak NI, Fedoruk OO, et al. Carassius auratus as a novel model for the hyperglycemia study. Ukr Biochem J. 2019 Dec;91(4):58-69. CrossRef
  10. Kursov SV, Nikonov VV. Stress hyperglycemia: discussion of ways to eliminate it with the help of sugar alcohols. Emergency medicine (Medicina neotložnyh sostoânij). 2019 Mar;4(99):30-7. [Russian]. CrossRef
  11. Prokhorova MI. Biochemical research methods (lipid and energy metabolism). Prokhorova MI, editor. Leningrad: Publisher LGU; 1982. [Russian].
  12. Kitagawa Y, Sugimoto E. Estimation of the in vivo translational activity of rat liver mitochondria without use of an antibiotic. J Biochem. 1980 Mar;88(3):689-93. CrossRef PubMed
  13. Dubinina EE, Morozova MG, Leonova NV, Gamper NL, Soliternova IB, Nuller JUL, Butoma GB, Kovrugina SV. Oxidative modification blood plasma proteins in patients with mental disorders (depression and depersonalization). Vopr Med Chemistry. 2000;46(4):398-409. [Russian].
  14. 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 Jan;260:359-64. CrossRef PubMed PubMedCentral
  15. Timoshchuk SV, Vavilova GL, Strutynska NA, Talanov SA, Petukhov DM, Kuchmenko OB, et al. Cardioprotective action of the coenzyme Q under activation of its endogenous synthesis during ischemia-reperfusion in old rat heart. Fiziol Zh. 2009;55(4):58-63. [Ukrainian].
  16. Voloshchuk ON, Kopylchuk GP. The ratio of ubiqiunon redox forms in the liver mitochondric under toxic hepatitis induced on the background of alimentary protein deficiency. Vopr Pitan. 2015 Oct;84(5):82-7. [Russian].
  17. Wangand Y, Hekimi S. Molecular genetics of ubiquinone biosynthesis in animals. Crit Rev Biochem Mol Biol. 2013 Jan-Feb;48(1):69-88. CrossRef PubMed PubMedCentral
  18. Rötig A. Human diseases with impaired mitochondrial protein synthesis. Biochim Biophys Acta. 2011 Jun; 1807 (9):1198-205. CrossRef PubMed
  19. Ametov AS, Solovieva OL. Oxidative stress in type 2 diabetes mellitus and methods for its correction. Probl Endocrinol. 2011 Dec;6:52-6. [Russian]. CrossRef

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