Українська English

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. 2022; 68(4): 48-56


INTENSITY OF FREE RADICAL PROCESSES IN RAT SKELETAL MUSCLES UNDER THE CONDITIONS OF DIFFERENT DIETARY SUPPLY WITH NUTRIENTS

O.M. Voloshchuk, Н.P. Kopylchuk

    Yuriy Fedkovych Chernivtsi National University, Ukraine
DOI: https://doi.org/10.15407/fz68.04.048


Abstract

The intensity of free-radical processes in the skeletal muscles of rats at different dietary supply with protein and sucrose was studied. It has been established that the most pronounced intensification of free radical processes in the mitochondria of skeletal muscles is found in animals kept on a low-protein/ high-sucrose diet. In particular, the generation of superoxide anion-radical increases more than 5,3-fold and the generation of hydroxyl radical more than 3,2-fold compared with the control, more than a 14,3-fold increase in the carbonyl derivatives levels, and also decreases by three times in the free protein SH-groups levels against the background of a 1,7-fold decrease in catalase activity. It has been shown that excessive consumption of sucrose is a critical factor influencing the intensity of free radical processes in skeletal muscle mitochondria. The detected changes can be considered as prerequisites for skeletal muscle dysfunction under the conditions of nutrient imbalance.

Keywords: nutrients; skeletal muscles; reactive oxygen species; oxidative modification of proteins; antioxidant enzymes.

References

  1. Paddon-Jones D, Rasmussen BB. Dietary protein recommendations and the prevention of sarcopenia. Current Opin Clin Nutr Metab Care. 2009 Jan;12(1):86-90. CrossRef PubMed PubMedCentral
  2. Aoyama S, Kim H-K, Hirooka R, Tanaka M, Shimoda T, Chijiki H, et al. Distribution of dietary protein intake in daily meals influences skeletal muscle hypertrophy via the muscle clock. Cell Reports. 2021 Jul;36:109336. CrossRef PubMed
  3. Carbone JW, Pasiakos SM. Dietary protein and muscle mass: translating science to application and health benefit. Nutrients. 2019 May;11(5):1136. CrossRef PubMed PubMedCentral
  4. Sarbone JW, McClung JR, Pasiakos SM. Skeletal muscle responses to negative energy balance: effects of dietary protein. Adv Nutr. 2012 Mar;3(2):119-26. CrossRef PubMed PubMedCentral
  5. Ozkan H, Yakan A. Dietary high calories from sunflower oil, sucrose and fructose sources alters lipogenic genes expression levels in liver and skeletal muscle in rats. Ann Hepat. 2019 Oct;18(5):715-24. CrossRef PubMed
  6. Stump CS, Henriksen EJ, Wei Y, Sowers JR. The metabolic syndrome: Role of skeletal muscle metabolism. Ann. Med. 2006 Jul;38(6):389-402. CrossRef PubMed
  7. Zhang D, Lee JH, Shin HE, Kwak SE, Bae JH, Tang L, Song W. The effects of exercise and restriction of sugarsweetened beverages on muscle function and autophagy regulation in high-fat high-sucrose-fed obesity mice. Diabetes Metab J. 2021 Nov;45:773-86. CrossRef PubMed PubMedCentral
  8. Barbieri E, Sestili R. Reactive oxygen species in skeletal muscle signaling. J Signal Trans. 2012 Dec;2012:982794. CrossRef PubMed PubMedCentral
  9. Barreiro E. Role of protein carbonylation in skeletal muscle mass loss associated with chronic conditions. Proteomes. 2016 May;4(2):18-29. CrossRef PubMed PubMedCentral
  10. Barbieri E, Hussain SN. Protein carbonylation in skeletal muscles: impact on function. Antioxid Redox Signal. 2010 Mar;12(3):417-29. CrossRef PubMed
  11. Steinbacher P, Eckl P. Impact of oxidative stress on exercising skeletal muscle. Biomolecules. 2015 Apr;5(2):356-77. CrossRef PubMed PubMedCentral
  12. Baraibar MA, Gueugneau M, Duguez S, Butler-Browne G, Bechet D, Friguet B. Expression and modification proteomics during skeletal muscle ageing. Biogerontology. 2013 Jun;14(3):339-52. CrossRef PubMed
  13. Mason S, Wadley G.D. Skeletal muscle reactive oxygen species: A target of good cop/bad cop for exercise and disease. Redox Report, 2014 Jan;19(3):97-106. CrossRef PubMed PubMedCentral
  14. Chanseaume E, Malpuech-Brugère C, Patrac V, Bielicki G, Paulette Rousset P, Couturier K, et al. Diets high in sugar, fat, and energy induce muscle type-specific adaptations in mitochondrial functions in rats. J Nutr. 2006 Aug;136(8):2194-200. CrossRef PubMed
  15. Voloshchuk OM, Kopylchuk GP, Ursatyu MS. The ratio of ubiquinon redox forms in the rat liver mitochondria under conditions of different nutrient supply. Fiziol Zh. 2020 Dec;66(6):82-7. [Ukrainian]. CrossRef
  16. Figueiredo PA, Powers SK, Ferreira RM, Appell HJ, Duarte JA. Aging impairs skeletal muscle mitochondrial bioenergetic function. J Gerontol: Ser A. 2009 Jan;64A(1):21-33. CrossRef PubMed PubMedCentral
  17. Kostenko VO, Tsebrzhins'kii OI. Production of superoxide anion radical and nitric oxide in renal tissues sutured with different surgical suture material. Fiziol Zh. 2000; 46(5): 56-62. [Ukrainian].
  18. Jiang ZY, Woollard AC, Wolff SP. Hydrogen peroxide production during experimental protein glycation. FEBS Lett. 1990 Jul;268(1): 69-71. CrossRef
  19. Tkachenko MM, Sahach VF, Baziliuk OV, Kotsiuruba AV, Popereka HM, Stepanenko LH, Seniuk OF. Agerelated characteristics of contractile vascular reactions and the content of oxygen free radicals and nitric oxide metabolites in BALB/c mice in conditions of alienation zone. Fiziol Zh. 2005;51(3):32-41. [Ukrainian].
  20. Parihar MS, Pandit MK. Free radical induced increase in protein carbonyl is attenuated by low doses of adenosine in hippocampus and mid brain: implication in neurodegenerative disorders. Gen Physiol Biophys. 2003 Mar; 22(1):29-39.
  21. 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
  22. Koroliuk MA, Ivanova LI, Mayorova IG, Tokarev VE. A method of determining catalase activity. Lab Delo. 1988;(1):16-19. [Russian].
  23. Sirota TV. Novel approach to the study of adrenaline autooxidation and its use for the measurement of superoxide dismutase activity. Vopr Med Khim. 1999;45(3):263-72. [Russian].
  24. Veal EA, Day AM, Morgan BA. Hydrogen peroxide sensing and signaling. Mol Cell. 2007 Apr;26(1):1-14. CrossRef PubMed
  25. Paulsen C, Carroll KS. Orchestrating redox signaling networks through regulatory cysteine switches. ACS Chem Biol. 2010 Jan 15;5(1):47-62. CrossRef PubMed PubMedCentral
  26. Sies H. Hydrogen peroxide as a central redox signaling molecule in physiological oxidative stress: Oxidative eustress. Redox Biol. 2017 Apr;11:613-19. CrossRef PubMed PubMedCentral
  27. Hancock J.T. Oxygen is instrumental for biological signaling: an overview. Oxygen. 2021 Jul;1(1):3-15. CrossRef
  28. Meo SD, Iossa S, Venditti P. Skeletal muscle insulin resistance: role of mitochondria and other ROS sources. J Endocrinol. 2017 Apr;233(1):R15-R42. CrossRef PubMed
  29. McKeegan K, Mason SA, Trewin AJ, Keske MA, Wadley GD, Gatta PAD, Nikolaidis MG, Parker L. Reactive oxygen species in exercise and insulin resistance: Working towards personalized antioxidant treatment. Redox Biol. 2021 May;44:1-17. CrossRef PubMed PubMedCentral
  30. Dos Santos SL, Baraibar MA, LundbergS, Eeg-Olofsson O, LarssonL, Friguet B. Oxidative proteome alterations during skeletal muscle ageing. Redox Biol. 2015 Aug;5:267-74. CrossRef PubMed PubMedCentral
  31. Vilela DD, Peixoto LG, Teixeira RR, Baptista NB, Caixeta DC, de Souza AV, et al. The role of metformin in controlling oxidative stress in muscle of diabetic rats. Oxid Med Cell Longev. 2016 Aug;2016:6978625. CrossRef PubMed PubMedCentral
  32. Arif B, Arif Z, Ahmad J, Perveen K, Bukhari NA, Ashraf JM, et al. Attenuation of hyperglycemia and amadori products by aminoguanidine in alloxandiabetic rabbits occurs via enhancement in antioxidant defenses and control of stress. PLoS ONE. 2022 Jan;17(1):e0262233. CrossRef PubMed PubMedCentral

© National Academy of Sciences of Ukraine, Bogomoletz Institute of Physiology, 2014-2024.