Advertisement

Neurophysiology

, Volume 46, Issue 1, pp 1–9 | Cite as

Thiamine Metabolism in Neurons and Their Vital Capacity Upon the Action of Ethanol and Acetaldehyde

  • Yu. M. ParkhomenkoEmail author
  • G. V. Donchenko
  • S. A. Chornyi
  • O. R. Yanchiy
  • A. O. Strokina
  • S. P. Stepanenko
  • L. I. Chekhovskaya
  • S. Y. Pylypchuk
  • N. Kh. Pogorelaya
Article

We studied the sensitivity of a few reactions of thiamine metabolism in nerve cells upon the action of ethanol and acetaldehyde, as well as effects of the above-mentioned agents on vital capacity of cultured cells of different origins. Experiments were carried out on preparations of isolated nerve endings (synaptosomes), preparations of synaptosomal plasma membranes (SPMs), preparations of enzymes, and cell cultures. We estimated the ІС50 for the effects of ethanol and acetaldehyde on reactions that are the components of metabolism of the mobile thiamine pool in the cells. Ethanol in physiological concentrations inhibited the thiamine-binding activity of SPMs (ІС50 = 3.9 mM). At the same time, this agent used in the above concentrations practically did not influence the thiamine phosphate hydrolase activity of SPMs (estimated by the thiamine triphosphatase activity) and thiamine pyrophosphate kinase (TPK) activity. A product of ethanol metabolism, acetaldehyde, inhibited the thiamine triphosphatase activity with K і = 6.2 μM and the TPK activity with K і = 1.2 μM. The survival indices of cultured cells were estimated under conditions of the addition of ethanol and acetaldehyde to the medium. The cells of an astrocytic origin (line strain 1321 N1) and blood cells (line strain U937) practically did not respond to the presence of ethanol or acetaldehyde even in rather high concentrations in the culture medium. Under conditions of primary culture, neuron-like (differentiated) cultured РС-12 cells and also cerebellar granular neurons responded by significant decreases in the index of vital capacity to the addition of the above agents.

Keywords

thiamine thiamine triphosphate thiamine kinase ethanol acetaldehyde neurons 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Yu. M. Parkhomenko, Z. S. Protasova, and G. V. Donchenko, “Neuroactivity of thiamine: facts and hypotheses,” Ukr. Biokhim. Zh., 68, No. 2, 3-15 (1996).PubMedGoogle Scholar
  2. 2.
    А. Bâ, “Comparative effects of alcohol and thiamine deficiency on the developing central nervous system,” Behav. Brain Res., 225, 235-242 (2011).PubMedCrossRefGoogle Scholar
  3. 3.
    М. Heroux et al., “Alterations of thiamine phosphorylation and of thiamine-dependent enzymes in Alzheimer’s disease,” Metab. Brain Dis., 11, No. 1, 81-88 (1996).PubMedCrossRefGoogle Scholar
  4. 4.
    Khanh vinh quoc Lurong, Lan Thi Hoang Nguyen, “Thiamine and Parkinson’s disease,” J. Neurol. Sci., 316, 1-8 (2012).Google Scholar
  5. 5.
    А. Bâ, “Metabolic and structural role of thiamine in nervous tissues,” Cell. Mol. Neurobiol., 28, No. 7, 923-931 (2008).PubMedCrossRefGoogle Scholar
  6. 6.
    J. H. Pincus, Y. Itokawa, and I. R. Cooper, “Enzyme inhibiting factor in subacute necrotizing enchephalomyelophathy,” Neurology, 19, No. 6, 841-845 (1969).PubMedGoogle Scholar
  7. 7.
    H. O. Nghiem, L. Bettendorff, and J. P. Changeux, “Specific phosphorylation of Torpedo 43K rapsyn by endogenous kinase (s) with thiamine triphosphate as the phosphate donor,” FASEB J., 14, No. 3, 543-554 (2000).PubMedGoogle Scholar
  8. 8.
    L. Bettendorff, “A non-cofactor role of thiamine derivatives in excitable cells?” Arch. Physiol. Biochem., 104, No. 6, 745-751(1996).PubMedCrossRefGoogle Scholar
  9. 9.
    Y. M. Ostrovskiy, “On the mechanism of coenzymic and noncoenzymic action of thiamine,” Vitaminology, 14, 98-102 (1968).CrossRefGoogle Scholar
  10. 10.
    B. Berman and R. A. Fishman, “Thiamine phosphate metabolism and possible coenzyme-independent function of thiamine in brain,” J. Neurochem., 24, No. 3, 457-465 (1975).PubMedCrossRefGoogle Scholar
  11. 11.
    L. Bettendorff and P. Wins, “Thiamine diphosphate in biological chemistry: new aspects of thiamin metabolism, especially triphosphate derivatives acting other than as cofactors,” FEBS J., 276, No. 11, 2917-2925 (2009).PubMedCrossRefGoogle Scholar
  12. 12.
    A. A. Sidorova (Strokina), S. P. Stepanenko, and Yu. M. Parkhomenko, “Characteristics of thiamine triphosphate associated with the plasma membranes of nerve cells,” Ukr. Biokhim. Zh., 81, No. 3, 57-65 (2009).PubMedGoogle Scholar
  13. 13.
    V. A. Postoenko, Yu. M. Parkhomenko, A. I. Vovk, et al., “Isolation and some properties of thiamine-binding protein of rat cerebral synaptosomes,” Biokhimiya, 52, No. 11, 1792-1797 (1987).Google Scholar
  14. 14.
    Yu. M. Parkhomenko, A. A. Strokina, S. Yu. Pilipchuk, et al., “The existence of two different active centers on thiamine-binding protein of synaptosomal plasma membranes,” Ukr. Biokhim. Zh., 82, No. 1, 34-41 (2010).PubMedGoogle Scholar
  15. 15.
    K. Chopra and V. Tiwari, “Alcoholic neuropathy: possible mechanisms and future treatment possibilities,” Br. J. Clin. Pharmacol., 73, No. 3, 348-362 (2012).PubMedCentralPubMedCrossRefGoogle Scholar
  16. 16.
    E. Rees and L. R. Gowing, “Supplementary thiamine is still important in alcohol dependence,” Alcohol Alcoholism, 48, No. 1, 88-92 (2013).PubMedCrossRefGoogle Scholar
  17. 17.
    Yu. M. Parkhomenko, Z. S. Protasova, O. R. Yanchiy, et al., “Localization of thiamine-binding protein in synaptosomes from the rat brain,” Neurophysiology, 33, No. 3, 135-139 (2001).CrossRefGoogle Scholar
  18. 18.
    Yu. M. Ostrovskii, “Thiamine,” in: Experimental Vitaminology, Yu. M. Ostrovskii (ed.), Nauka Tekhnika, Minsk (1979), pp. 176-223.Google Scholar
  19. 19.
    S. Yu. Pilipchuk, Yu. M. Parkhomenko, Z. S. Protasova, et al., “Interaction between thiamine kinase of the rat brain and thiamine and thiamine derivatives,” Ukr.Biokhim. Zh., 73, No. 2, 51-57 (2001).Google Scholar
  20. 20.
    S. A. Chornyy and Y. M. Parkhomenko, “Comparative characteristic of action of thiamine antagonists as apoptosis inducers in different types of nerve cells,” Ukr. Biokhim. Zh., 80, No. 5, 76-84 (2008).PubMedGoogle Scholar
  21. 21.
    V. K. Kibirev, T. V. Osadchouk, O. B. Vadzyuk, et al., “Examination of derivatives of 5-amino-4-acylamino-1Н-pyrazole as furin inhibitors,” Ukr. Biokhim. Zh., 83, No. 1, 30-37 (2011).PubMedGoogle Scholar
  22. 22.
    Y. M. Parkhomenko, P. A. Kudryavtsev, S. Y. Pylypchuk, et al., “Chronic alcoholism in rats induces a compensatory response preserving brain thiamine diphosphate, but the brain 2-oxo acid dehydrogenases are inactivated despite unchanged coenzyme levels,” J. Neurochem., 117, No. 6, 1055-1065 (2011).PubMedCrossRefGoogle Scholar
  23. 23.
    H. Begleiter and B. Kissin, The Pharmacology of Alcohol and Alcohol Dependence, Oxford University Press, New York (1996).Google Scholar
  24. 24.
    K. N. Boyd, T. K. O’Buckley, and A. L. Morrow, “Role of acetaldehyde in ethanol-induced elevation of the neuroactive steroid 3alpha-hydroxy-5alpha-pregnan-20-one in rats,” Alcohol. Clin. Exp. Res., 32, 1774-1781 (2008).PubMedCentralPubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 2014

Authors and Affiliations

  • Yu. M. Parkhomenko
    • 1
    Email author
  • G. V. Donchenko
    • 1
  • S. A. Chornyi
    • 1
  • O. R. Yanchiy
    • 1
  • A. O. Strokina
    • 1
  • S. P. Stepanenko
    • 1
  • L. I. Chekhovskaya
    • 1
  • S. Y. Pylypchuk
    • 1
  • N. Kh. Pogorelaya
    • 2
  1. 1.Palladin Institute of BiochemistryNational Academy of Sciences of UkraineKyivUkraine
  2. 2.Bogomolets Institute of PhysiologyNational Academy of Sciences of UkraineKyivUkraine

Personalised recommendations