Neuroscience and Behavioral Physiology

, Volume 48, Issue 2, pp 220–224 | Cite as

Effects of Melatonin on the Interaction between the Level of Accumulation of Oxidatively Modified Proteins, the Activity of Antioxidant Enzymes, and the State of Proteolysis in the Basal Ganglia of the Brain in Acute Hypoxia

  • I. Yu. Sopova
  • I. I. Zamorskii

The effects of melatonin on the interaction between the level of accumulation of oxidatively modified proteins, the activity of antioxidant enzymes, and the state of the proteolysis system in the basal ganglia (caudate nucleus, globus pallidus, nucleus accumbens, amygdaloid complex) of the brain were studied in conditions of acute hypoxia. Acute hypoxia was found to increase protein peroxidation and proteolysis intensity in the basal ganglia, and also to decrease the activity of antioxidant defense enzymes. Administration of melatonin (1 mg/kg) before modeling of acute hypoxia was accompanied by a decrease in the content of protein peroxidation products, an increase in the activity of the antioxidant enzymes, and normalization of the intensity of proteolysis.


melatonin oxidatively modified proteins antioxidant defense enzymes proteolysis basal ganglia acute hypoxia 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    V. N. Anisimov, Melatonin: Its Role in the Body and its Use in Clinical Practice, Sistema, St. Petersburg (2007).Google Scholar
  2. 2.
    A. I. Arakov and I. M. Mosokhoev, “Modification of proteins by active oxygen and their degradation,” Biokhimiya, 54, No. 2, 179–186 (1989).Google Scholar
  3. 3.
    E. B. Arushanyan, “The antistress potential of epiphyseal melatonin,” in: Melatonin in Health and Disease, Moscow (2004), pp. 198–222.Google Scholar
  4. 4.
    E. B. Arushanyan, “The epiphyseal hormone melatonin in the combined pharmacotherapy of brain diseases and somatic pathology,” Eksperim. Klin. Farmakol., 74, No. 9, 39–45 (2011).Google Scholar
  5. 5.
    V. A. Baraboi and D. A. Sumkovoi, “Oxidant-Antioxidant Homeostasis in Health and Disease, Kiev (1997).Google Scholar
  6. 6.
    I. A. Zborovskaya and M. V. Bannikova, “The antioxidant system of the body and its importance in metabolism. Clinical aspects,” Vestn. Russ. Akad. Med. Nauk., No. 6, 53–59 (1995).Google Scholar
  7. 7.
    O. V. Goiko, Practical Application of Statistica for Analysis of Medical and Biological Data, Kiev (2004).Google Scholar
  8. 8.
    M. A. Korolyuk, L. I. Ivanova, I. G. Maiorov, and V. E. Tokarev, “A method for assay of catalase activity,” Lab. Delo, No. 1, 16–18 (1988).Google Scholar
  9. 9.
    V. Yu. Kulikov and L. B. Kim, An Oxygen Regime for Adaptation of Humans to the Far North, Novosibirsk (1987).Google Scholar
  10. 10.
    L. V. Pastushenkov, “Basic methods for assessing the protective action of antioxidants in experimental studies and their influences on metabolic processes in cells,” in: Pharmacological Correction of Hypoxic States, Meditsina, Moscow (1989), pp. 118–124.Google Scholar
  11. 11.
    L. V. Savchenkova, “Biochemical basis of the pathogenesis of hypoxic syndrome,” Ukr. Biokhimich. Alman., No. 1, 90–99 (1998).Google Scholar
  12. 12.
    R. D. Sinel’nikov and Ya. R. Sinel’nikov, Atlas of Human Anatomy, Meditsina, Moscow (1994).Google Scholar
  13. 13.
    Current Study and Clinical Investigation Methods of the Central Science Research Laboratory, Bukovina State Medical Academy, Bukovina State Medical Academy, Chernovtsy (2001).Google Scholar
  14. 14.
    I. A. Tregubova, V. A. Kosolapov, and A. S. Spasov, “Antioxidants: current status and perspectives,” Usp. Fiziol. Nauk., 43, No. 1, 75–94 (2012).PubMedGoogle Scholar
  15. 15.
    C. Chevari, I. Chaba, and I. Sekei, “The role of superoxide dismutase in oxidative processes in cells and a method for assaying it in biological materials,” Lab. Delo, No. 11, 678–681 (1985).Google Scholar
  16. 16.
    A. L. Dafre, N. S. Arteni, I. R. Siqueira, and C. A. Netto, “Perturbations in the thiol homeostasis following neonatal cerebral hypoxia-ischemia in rats,” Neurosci. Lett., 345, No. 1, 65–68 (2003).CrossRefPubMedGoogle Scholar
  17. 17.
    A. Korkmaz and R. J. Reiter, “Epigenetic regulation: a new research area for melatonin?” J. Pineal. Res., 44, No. 1, 41–44 (2008).PubMedGoogle Scholar
  18. 18.
    D. Ozdemir, N. Uysal, S. Gonenc, et al., “Effect of melatonin on brain oxidative damage induced by traumatic brain injury in immature rats,” Physiol. Res., 10, 18–22 (2005).Google Scholar
  19. 19.
    C. Rodriguez, J. C. Mayo, R. M. Sainz, et al., “Regulation of antioxidant enzymes: a significant role for melatonin,” J. Pineal Res., 36, 1–9 (2004).CrossRefPubMedGoogle Scholar
  20. 20.
    R. J. Reiter, D. X. Tan, and M. A. Pappolla, “Melatonin relieves the neural oxidative burden that contributes to dementias,” Ann. N. Y. Acad. Sci., 1035, 179–196 (2004).CrossRefPubMedGoogle Scholar
  21. 21.
    R. J. Reiter, D. X. Tan, and M. P. Terron, “Melatonin: potential utility for improving public health,” TAF Prev. Med. Bull., 5, 131–158 (2006).CrossRefGoogle Scholar
  22. 22.
    T. Zitnanova, K. Sumegova, and M. Simko, “Protein carbonyls as a biomarker of hypoxic stress,” Clin. Biochem., 40, No. 8, 567–570 (2007).CrossRefPubMedGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Bukovina State Medical UniversityChernovtsyUkraine

Personalised recommendations