Abstract—The activities of isocitrate dehydrogenase, α-ketoglutarate dehydrogenase, malate dehydrogenase, and NADH:ubiquinone reductase in the mitochondrial fraction from the liver tissue of rats fed diets with different sucrose and protein contents have been measured. In animals that received a high-sucrose diet, isocitrate dehydrogenase and malate dehydrogenase activities tend to decline and α-ketoglutarate dehydrogenase activity decreased by a factor of 2.5. Interestingly, the NADH:ubiquinone reductase activity remains at the control level in animals that are fed the high-sucrose diet. In the mitochondrial fraction from the liver tissue of rats that receive a high-sucrose–low-protein diet, the activities of NAD+-dependent dehydrogenases of the Krebs cycle decrease considerably, and the activity of NADH:ubiquinone reductase decreased as well, being more than 2.5 times lower than in the control. This may be one of the steps in the mechanism by which energy generated in the cell is regulated when the sucrose : protein ratio in the diet is imbalanced. These results can be used to develop a strategy for the correction of metabolic disturbances associated with nutrient contents in the diet.
This is a preview of subscription content, log in to check access.
Buy single article
Instant access to the full article PDF.
Price includes VAT for USA
G. Wu, Food Funct. 7 (3), 1251 (2016).
R. V. Tikole, R. Kulkarni, S. Uppinakudru, et al., Int. J. Res. Ayurveda Pharmacy 4 (4), 605 (2013).
J. C. Malta de Oliveira, T. A. Ribeiro, L. P. Tofolo, et al., J. Endocrin. 221 (2), 285 (2014).
M. Maciejczyk, J. Matczuk, M. Żendzian-Piotrowska, et al., Nutrients 10 (10), 1 (2018).
A. Pezeshki, R. Zapata, A. Singh, et al., Sci. Rep. 6. 25145. (2016).
E. F. Mason and J. C. Rathmell, Biochim. Biophys. Acta 1813 (4), 645 (2011).
L. Rui, Compr. Physiol. 4 (1), 177 (2014).
M. G. Radaelli, F. De Cobelli, A. Esposito, et al., Oxid Med. Cell. Longev. 2019, 9796175 (2019).
S. Satapati, N. E. Sunny, B. Kucejova, et al., J. Lipid Res. 53, 1080 (2012).
O. N. Voloshchuk and G. P. Kopylchuk, Biomed. Khim. 62 (2), 169 (2016).
F. Fernandes-Lima, L. Monte, F. Nascimento, and B. Gregorio, Tissues Organs 201 (6), 464 (2016).
O. N. Voloshchuk and G. P. Kopylchuk, Biophysics (Moscow) 60 (3), 420 (2015).
Y.-C. Huang, S. Soundar, and A. F. Colman, Prot. Sci. 9, 104 (2000).
P. Cetica, L. Pintos, G. Dalvit, et al., Reproduction 126, 753 (2003).
G. Kiss, C. Konrad, J. Doczi, et al., FASEB J. 27, 2392 (2013).
I. V. Sharova and N. L. Vekshin, Biophysics (Moscow) 49 (5), 814 (2004).
R. Vatrinet, G. Leone, M. De Luise, et al., Cancer Metab. 5, 3 (2017).
M. J. Kumar, D. G. Nicholls, and J. K. Andersen, J. Biol. Chem. 278, 46432 (2003).
G. E. Gibson, J. P. Blass, M. F. Beal, and V. Bunik, Mol. Neurobiol. 31 (1-3), 43 (2005).
S. M. M. Ragab, S. Kh. A. Elghaffar, T. H. El-Metwally, et al., Lipids Health Dis. 14, 83 (2015).
K. Prasad and I. Dhar, Int. J. Angiol. 23 (4), 217 (2014).
This work was performed as part of the Biochemical and Laser Polarimetric Parameters for Integrated Prediction of Metabolic Disorders research project, State registration ID 0119U100717.
Conflict of Interest
The authors declare that they have no conflict of interest.
Statement of the Welfare of Animals
Manipulations with animals were carried out with regard for the principles of the World Medical Association Declaration of Helsinki of 1964 with amendments of 1975, 1983, and 1989. All applicable international, national, and institutional guidelines for the care and use of animals were followed.
Translated by Victor Gulevich
About this article
Cite this article
Voloshchuk, O.N., Kopylchuk, G.P. & Tazirova, K.A. The Features of Energy Metabolism in Hepatocytes of Rats that Receive Diets with Different Nutrient Contents. BIOPHYSICS 65, 268–271 (2020). https://doi.org/10.1134/S000635092002027X
- Keywords: isocitrate dehydrogenase
- α-ketoglutarate dehydrogenase
- malate dehydrogenase
- NADH:ubiquinone reductase