Changes in the biogenesis of mitochondria in brain tissue in animals under conditions of cerebral ischemia

DOI: 10.29296/2618723X-2021-03-07

Pozdnyakov D. I., Associate professor of the Department of Pharmacology with a course of clinical pharmacology (the author responsible for correspondence), ORCID 0000-0002-5595-8182;
Mamleev A.V., Associate Professor of the Department of Pharmacology with the course of clinical Pharmacology, ORCID 0000-0001-9657-2246;
Sarkisyan K. H., Associate Professor of the Department of Pharmacology with the course of Clinical Pharmacology, ORCID 0000-002-1756-0026

Pyatigorsk Medical and Pharmaceutical Institute-branch of the Volga State Medical University
357532, Russia, Stavropol Territory, 11 Kalinin Ave., Pyatigorsk
Е-mail: [email protected]

Keywords: brain ischemia mitochondrial dysfunction mitochondrial biogenesis

For citation:

Pozdnyakov D. I., Mamleev A.V., Sarkisyan K. H. Changes in the biogenesis of mitochondria in brain tissue in animals under conditions of cerebral ischemia. Laboratory Animals for Science. 2021; 3.


Mitochondrial dysfunction is a universal pathogenetic mechanism that plays an essential role in ischemic brain damage. At the same time, the study of mitochondrial biogenesis will significantly improve the effectiveness of targeted therapeutic effects on the mitochondria of the cell.

The aim of the study was to evaluate changes in mitochondrial biogenesis in rat brain tissue under conditions of permanent focal ischemia.

Material and methods. Cerebral ischemia was modeled in male rats by irreversible right-sided coagulation of the middle cerebral artery. Mitochondrial biogenesis was assessed by changes in the activity of succinate dehydrogenase and cytochrome-c oxidase in rats in the dynamics by the spectrophotometric method. Also, in rats, the change in the size of the brain necrosis zone was determined by the degree of recovery of formazan triphenyltetrazolium chloride.

Results. The study showed that the most pronounced changes in the activity of succinate dehydrogenase and cytochrome-c oxidase were noted 72 hours after the simulation of ischemia. At the same time, in comparison with sham-operated animals, the activity of enzymes decreased by 53.1% (p<0.05) and 60% (p<0.05), respectively. It is worth noting that changes in the enzymatic activity of succinate dehydrogenase and cytochrome-c oxidase correlated with an increase in the brain necrosis zone with the values of correlation coefficients r=0.71324 and r=0.83629, respectively.

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Conflict of interest

The authors declare no conflicts of interest.


  1. Rabinstein A.A. Update on Treatment of Acute Ischemic Stroke // Continuum (Minneap Minn). 2020. Vol.26. №.2. P. 268-286.
  2. Yang J.L., Mukda S., Chen S.D. Diverse roles of mitochondria in ischemic stroke // Redox Biol. 2018. Vo.16. P. 263-275.
  3. Andrabi S.S, Parvez S., Tabassum H. Ischemic stroke and mitochondria: mechanisms and targets // Protoplasma. 2020. Vol.257. № 2. P.335-343.
  4. Huang S., Millar A.H. Succinate dehydrogenase: the complex roles of a simple enzyme // Curr Opin Plant Biol. 2013. Vol.16. № 3. P.344-349.
  5. Rak M., Bénit P., Chrétien D. Mitochondrial cytochrome c oxidase deficiency // Clin Sci (Lond). 2016. Vol. 130. №6. P.393-407.
  6. Percie du Sert N., Hurst V., Ahluwalia A. The ARRIVE guidelines 2.0: Updated guidelines for reporting animal research // PLoS Biol. 2020. Vol.18.№7.P.e3000410.
  7. Tamura A., Graham D.I., McCulloch J., Teasdale G.M. Focal cerebral ischaemia in the rat: 1. Description of technique and early neuropathological consequences following middle cerebral artery occlusion // J Cereb Blood Flow Metab. 1981. Vol.1. № 1. P.53–60
  8. Spinazzi M., Casarin A., Pertegato V., Salviati L., Angelini C. Assessment of mitochondrial respiratory chain enzymatic activities on tissues and cultured cells // Nat Protoc. 2012. Vol.7. № 6. P.1235-1246
  9. Li Y., D'Aurelio M., Deng J.H. An assembled complex IV maintains the stability and activity of complex I in mammalian mitochondria // J Biol Chem. 2007. Vol.282. № 24.P.17557-17562.
  10. Wang H., Huwaimel B., Verma K. Synthesis and Antineoplastic Evaluation of Mitochondrial Complex II (Succinate Dehydrogenase) Inhibitors Derived from Atpenin A5 // ChemMedChem. 2017. Vo.12. № 13. P.1033-1044.
  11. Pozdnyakov D. I., Zolotych D. S., Larsky M. V. Correction of mitochondrial dysfunction by succinic acid derivatives under experimental cerebral ischemia conditions // Current Issues in Pharmacy and Medical Sciences. 2021. Vol. 34. №. 1. P. 42-48.
  12. Anzell A.R., Maizy R., Przyklenk K, Sanderson TH. Mitochondrial Quality Control and Disease: Insights into Ischemia-Reperfusion Injury // Mol Neurobiol. 2018. Vol.55. № 3. P. 2547-2564.
  13. Uzdensky A.B. Apoptosis regulation in the penumbra after ischemic stroke: expression of pro- and antiapoptotic proteins // Apoptosis. 2019. Vol.24. № 9-10. P. 687-702.
  14. Jia L., Wang J., Cao H., Zhang X., Rong W., Xu Z. Activation of PGC-1α and Mitochondrial Biogenesis Protects Against Prenatal Hypoxic-ischemic Brain Injury // Neuroscience. 2020. Vol.432. P.63-72.

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