Українська English

ISSN 2522-9028 (Print)
ISSN 2522-9036 (Online)
DOI: https://doi.org/10.15407/fz

Fiziologichnyi Zhurnal

is a scientific journal issued by the

Bogomoletz Institute of Physiology
National Academy of Sciences of Ukraine

Editor-in-chief: V.F. Sagach

The journal was founded in 1955 as
1955 – 1977 "Fiziolohichnyi zhurnal" (ISSN 0015 – 3311)
1978 – 1993 "Fiziologicheskii zhurnal" (ISSN 0201 – 8489)
1994 – 2016 "Fiziolohichnyi zhurnal" (ISSN 0201 – 8489)
2017 – "Fiziolohichnyi zhurnal" (ISSN 2522-9028)

Fiziol. Zh. 2003; 49(2): 66-72

Metabolism of heme and hemoproteins and some indicies of antioxidantsystem in erythrocytes and rat tissues under anemia, caused by phenylhydrazine administration

P.А. Kaliman, K.V. Strel’chenko, T.V. Barannik, I.V. Nikitchenko, N. N. Inshina, O.V. Pavichenko,V.P. Philimonenko

    Karasin’s National University, Kharkov



Abstract

The decrease of activity of several antioxidant enzymes in erythrocytes in the first hours after injection of phenylhydrazine to rats (7 mg per 100 g body weight) was found to be accompanied by accumulation of heme-containing compounds in rat serum and appearance of free heme in liver and decrease of cytochrome P450 content. Tissue-specific features of dynamics of activity of enzymes studied and reduced glutathione content were revealed, that might be caused by differences in total and free heme content in these organs. The role of key enzymes of heme biosynthesis and degradation in adaptation of metabolism under phenylhydrazine action is discussed.

Full text: (PDF, in Ukrainian)

References

  1. Гублер Е.В., Генкин А.А. Применение непарамет рических критериев статистики в медико-биологических исследованиях. – Л.: Медицина, 1973. – 144 c.
  2. Калиман П.А., Баранник Т.В. Метаболизм гема и оксидативный стресс // Укр.биохим.журн. – 2001. – 73, № 1. – С. 5 – 15.
  3. Ланкин В.З., Гуревич С.М. Ингибирование переокисления липидов и детоксикация липоперекисей защитными ферменативными системами (супероксиддисмутаза, глутатионпероксидаза и глутатионредуктаза) при экспериментальном злокачественном росте// Докл. АН СССР. – 1976. – 226, № 3. – С. 705 – 708.
  4. Мартинчик А. Н., Бондарев Г. И. Активность глутатионредуктазы и глутатион-S-арилтрансферазы в печени крыс в зависимости от содержания восстановленного глутатиона// Вопр. мед. химии. – 1986. – 32, вып. 2. – С. 39 – 43.
  5. Путилина Ф. Е. Определение содержания восстановленного глутатиона в тканях. – В кн..: Методы биохимических исследований.– 1982.– С. 183 – 185.
  6. Саркисов Д.С., Ремезов П.И. Воспроизведение болезней человека в эксперименте. – М, 1960. – 780 с.
  7. Badawy A.A., Evans M. The effects of chemical porphyrogens and drugs on the activity of rat liver tryptophan pyrrolase //Biochem. J. – 1973. – 136, № 4 – Р. 885 – 892.
  8. Bottomley R. H., Pilot H.C., Potter V.R., Morris H.P. Metabolic adaptation in rat hepatomas// Cancer Res. – 1963. – 23, № 3 – Р. 400 – 409.
  9. 9. Edward M. Scott. Purification and Properties of Glutathione Peroxidase of Human Erythrocytes// J. Biol. Chem. – 1963. – 238, № 12. – P. 3928 – 3933.
  10. 10. Ferrali M., Signorine C., Sugherini L. et al. Release of free, redox-active iron in the liver and DNA damage following phenylhydrazine intoxication// Biochem Pharmacol. – 1997. – 53, № 11 – Р. 1743 – 1751.
  11. Fujii S., Dale G.L., Beutler E. Glutathione-dependent protection against oxidative damage of the human red cell membrane// Blood. – 1998. – 34, № 10. – P.1632 – 1644.
  12. Goldstain B. D., Rozen M.G., Kunis R. Role of red cell lipid peroxidation in hemolysis due to phenyl-hydrazine// Biochem. Pharmacol. – 1980. – 29. – Р. 1355 – 1359.
  13. Gutteridge J. M. S., Smith A. Antioxidant protection by haemopexin of haem – stimulated lipid peroxidation // Biochem J. – 1988. – 256, № 3 – Р. 861 – 865.
  14. Hashmi A. N., Saleemuddin M. Phenylhydrazine caused sulfhydryl oxidation and protein aggregation in hemoglobin-free human erythrocyte membranes// Biochem. Mol. Biol. Int. – 1986. – 40, № 3 – Р. 543 – 550.
  15. Hrkal Z., Muller-Ebrhard U. Partial characterization of the hemebinding serum glycoproteins rabbit and human hemopexin// Biochemistry. – 1971. – 10, № 10. – P. 1746 – 1750.
  16. Jain S.K., Hochstein P. Generation of superoxide radicals by hydrazine. Its role in phenylhydrazine-induced hemolytic anemia// Biochem. Biophys. Acta. – 1979. – 586. – Р. 128 – 139.
  17. Llesuy S.F., Tomaro M.L. Heme oxygenase and oxidative stress. Evidence of involvement of bilirubin as physiological protector against oxidative damage// Ibid. – 1994. – 1223, № 1. – P.9 – 14.
  18. Maines M.D. Heme Oxygenase: Clinical Applications and Functions: FL: Inc. Boca Ration, Press CRC, 1992. – Р. 266.
  19. 19. Marver H. S., Collins A., Thshudi D. R. Aminilevulinic acid synthetase. I. Studies in liver homogenate// J. Biol. Chem. – 1966. – 241, № 19. – P. 4323 – 4329.
  20. 20. Matsubara T., Koike M., Touchi A. et. al. Quantitative determination of cytochrome P-450 in rat liver homogenate// Anal. Biochem. – 1976. – 75. – P. 596 – 603.
  21. Miller G.L. Protein determination for large numbers of samples// Anal. Chem. – 1959. – 31, № 5. – P. 964 – 966.
  22. Murklund S., Nordensson J., Back O. Normal Cu, Zn- superoxide dismutase, Mn-Sod, catalase and glutathione peroxidase in Werner“s syndrome// J. Gerontol. – 1981. – 36, № 4. – Р. 405 – 409.
  23. Ohars A. N-Phenylprotoporphyrin IX formation in the hemoglobin-phenylhydrazine reaction// J.Biol. Chem. – 1982. – 257, № 11. – P.6231 – 6241.
  24. Peng J., Jonnes G. L., Watson K. Stress Proteins as Biomarkers of Oxidative Stress: Effects of Antioxidant Supplements//Free Radic. Biol. Med. – 2000. – 28, № 11 – Р. 1598 – 606.2
  25. Paul K. G., Theorell H., Akeson A. The molar light absorption of pyridine ferroprotoporhyrin (pyridine haemochromogen)//Acta Chem. Scand. – 1953. – 7. – P. 1284 – 1287.
  26. Sardana M.K., Sassa S., Kappas A. Hormonal regulation of heme oxygenase induction in avian hepatocyte culture// Biochem. Pharmacol.— 1985. –34, № 16. – Р. 2937-2944.
  27. Verma A., Hirch D. J., Glatt C. E. еt al. Carbon monoxide: a putative neural messenger// Science. – 1993. – 259, № 7. – Р. 381 – 384
© National Academy of Sciences of Ukraine, Bogomoletz Institute of Physiology, 2014-2024.