Effects of 6-hydroxy-2,2,4-trimethyl-1,2-dihydroquinoline on the oxidative status and activity of dicarboxylic acid metabolism enzymes in toxic liver injury in rats
- Authors: Sinitsyna D.A.1, Popova T.N.1, Kryl’skii E.D.1, Shikhaliev K.S.1, Lebedeva J.I.1, Zherebtsova E.V.1, Popova D.A.1
-
Affiliations:
- Voronezh State University
- Issue: Vol 26, No 1 (2023)
- Pages: 43-48
- Section: Problems of experimental biology and medicine
- URL: https://journals.eco-vector.com/1560-9596/article/view/535046
- DOI: https://doi.org/10.29296/25877313-2023-01-08
- ID: 535046
Cite item
Abstract
One of the widespread public health problems nowadays is toxic liver damage. The key mechanism of the pathogenic action of xenobiotics One of the widespread public health problems nowadays is toxic liver damage. The key mechanism of the pathogenic action of xenobiotics on the liver is the activation of oxidative stress. Excessively generated free radicals damage mitochondrial components in hepatocytes, which can lead to disfunction of mitochondrial dehydrogenases.
The aim of the work was to investigate the influence of antioxidant 6-hydroxy-2,2,4-trimethyl-1,2-dihydroquinoline on oxidative status, activity of succinate dehydrogenase and NAD-dependent malate dehydrogenase in rats with toxic liver damage.
Material and methods. The study included 48 male Wistar rats weighing 200-250 g, divided into 4 groups of 12 animals in each: control group, a group of animals with tetrachloromethane-induced liver damage, rats with pathology that received intragastrically 6-hydroxy-2,2,4-trimethyl-1,2-dihydroquinoline at a dose of 50 mg/kg, and control rats received the tested compound. The level of oxidative modification of proteins was assessed by the method of Reznick et al. with slight modifications, alpha-tocopherol concentration was estimated by the method based on measuring the absorption of chromogenic complex compound Fe2+ and orthophenanthroline. Activity of alanine aminotransferase, aspartate aminotransferase and gamma-glutamyltranspeptidase was determined in blood serum using Olvex Diagnosticum reagent kits (Russia, Saint Petersburg). Cytoplasmic and mitochondrial liver fractions were obtained for analysis of succinate dehydrogenase and NAD-dependent malate dehydrogenase activity.
Results. Results of the work have shown that 6-hydroxy-2,2,4-trimethyl-1,2-dihydroquinoline treatment led to the normalization of the analyzed parameters, which was apparently due to the correction of the redox status in the liver of animals under the action of the tested compound.
Conclusion. The results of the study make it necessary to further investigate the effect of dihydroquinoline derivatives on oxidative metabolic enzymes in pathological
Full Text
About the authors
D. A. Sinitsyna
Voronezh State University
Author for correspondence.
Email: evgenij.krylsky@yandex.ru
Post-Graduate Student, Department of Medical Biochemistry and Microbiology
Russian Federation, VoronezhT. N. Popova
Voronezh State University
Email: evgenij.krylsky@yandex.ru
Dr.Sc. (Biol.), Professor, Dean of Medical and Biological Faculty
Russian Federation, VoronezhE. D. Kryl’skii
Voronezh State University
Email: evgenij.krylsky@yandex.ru
Ph.D. (Biol.), Associate Professor, Department of Medical Biochemistry and Microbiology
Russian Federation, VoronezhKh. S. Shikhaliev
Voronezh State University
Email: evgenij.krylsky@yandex.ru
Dr.Sc. (Chem.), Professor, Head of Organic Chemistry Department
Russian Federation, VoronezhJu. I. Lebedeva
Voronezh State University
Email: evgenij.krylsky@yandex.ru
Student, Department of Medical Biochemistry and Microbiology
Russian Federation, VoronezhE. V. Zherebtsova
Voronezh State University
Email: evgenij.krylsky@yandex.ru
Student, Department of Medical Biochemistry and Microbiology
Russian Federation, VoronezhD. A. Popova
Voronezh State University
Email: evgenij.krylsky@yandex.ru
Student, Department of Medical Biochemistry and Microbiology
Russian Federation, VoronezhReferences
- Liu Y., Wen P.H., Zhang X.X., et al. Breviscapine ameliorates CCl4 induced liver injury in mice through inhibiting inflammatory apoptotic response and ROS generation. Int. J. Mol. Med. 2018; 42: 755–768.
- Forrester S. J., Kikuchi D. S., Hernandes M. S. et al. Reactive oxygen species in metabolic and inflammatory signaling. Circ Res. 2018; 122: 877–902.
- Rutter J., Winge D.R., Schiffman J.D. Succinate dehydrogenase – Assembly, regulation and role in human disease. Mitochondrion. 2010; 10: 393–401.
- Musrati R. A., Kollárová M., Mernik N., et al. Malate Dehydrogenase: Distribution, Function and Properties. Gen Physiol Biophys. 1998; 17: 193–210.
- Iskusnykh I. Y., Krylskii E. D., Brazhnikova D. A. et al. Novel Antioxidant, Deethylated Ethoxyquin, Protects against Carbon Tetrachloride Induced Hepatotoxicity in Rats by Inhibiting NLRP3 Inflammasome Activation and Apoptosis. Antioxidants. 2021; 10: 122.
- Reznick A.Z., Packer L. Oxidative damage to proteins: spectrophotometric method for carbonyl assay. Methods Enzemol. 1994; 233: 357–363.
- Desai I.D., Martinez F.E. Bilirubin interference in the colorimetric assay of plasma vitamin E. Clin. Chim. Acta. 1986; 154: 247–250.
- Bailey C.A., Srinivasan L.J., McGeachin R.B. The effect of ethoxyquin on tissue peroxidation and immune status of single comb White Leg-horn cockerels. Poult Sci. 1996; 75: 9–12.
- Pougeois R., Satre M., Vignais P.V. N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline, a new inhibitor of the mitochondrial F1-ATPase. Biochemistry. 1978; 17: 3018–3023.
- Steverding D., Kadenbach B. Influence of N-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline modification on proton translocation and membrane potential of reconstituted cytochrome-c oxidase support “proton slippage”. Journal of Biological Chemistry. 1991; 266: 8097–8101.