Vet Med - Czech, 2002, 47(10):303-308 | DOI: 10.17221/5839-VETMED

In vitro susceptibility of duck, chicken, and pig erythrocyte lipids to peroxidation

B. Gradinski-Vrbanac, Z. Stojevič, S. Milinkovič-Tur, T. Balenovič, J. Piršljin, M. Zdeler-Tuk
1 Department of Physiology and Radiobiology,
2 Department of Animal Husbandry, Faculty of Veterinary Medicine, University of Zagreb, Croatia

The susceptibility of erythrocyte lipid to in vitro peroxidation as measured by TBARS (thiobarbituric acid-reactive substances) and concentration of reduced glutathione (GSH) in whole blood and erythrocyte suspension before and after incubation with hydrogen peroxide was assessed in ducks, chickens and pigs. A high susceptibility of erythrocytes to peroxidation in vitro was observed in all animals tested, but this susceptibility was of different intensity. Pig erythrocytes exhibited the lowest resistance to oxidative stress in vitro as compared with that in ducks (P < 0.01) and chickens (P < 0.02). A high level of GSH in the erythrocytes of ducks and chickens offers higher resistance to oxidative stress in comparison with that in the pig erythrocytes.

Keywords: duck; chicken; pig; erythrocytes; thiobarbituric acid-reactive substances; glutathione

Published: October 31, 2002  Show citation

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Gradinski-Vrbanac B, Stojevič Z, Milinkovič-Tur S, Balenovič T, Piršljin J, Zdeler-Tuk M. In vitro susceptibility of duck, chicken, and pig erythrocyte lipids to peroxidation. Vet Med - Czech. 2002;47(10-11):303-308. doi: 10.17221/5839-VETMED.
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    References

    1. Aebi H. (1974): In: Bergmeyer H.U.: Methods of Enzymatic Analysis. 2nd ed. Vol. 2, Verlag Chemie, Academic Press, Inc. New York and London. 673 pp.
    2. Avellini L., Spaterna A., Reboldi G.P., Gaiti A. (1993): Defence mechanisms against free radical-induced damage in sheep, cattle and dog erythrocytes. Comp. Biochem. Physiol., 106B, 391-394. Go to original source... Go to PubMed...
    3. Beutler E., Duron B., Kelly M. (1963): Improved method for the determination of blood glutathione. J. Lab. Clin. Med., 62, 882-888.
    4. Cynamon H.A., Isenberg J.N., Nguyen C.H. (1985): Erythrocyte malondialdehyde release in vitro: A functional measure of vitamin E status. Clin. Chim. Acta, 151, 169-176. Go to original source... Go to PubMed...
    5. Duthie G.G., Robertson J.D., Maughan R.J., Morrice P.C. (1990): Blood antioxidant status and erythrocyte lipid peroxidation following distance running. Arch. Biochim. Biophys., 282, 78-83. Go to original source... Go to PubMed...
    6. Edwards C.J., Fuller J. (1996): Oxidative stress in erythrocytes. Comp. Haematol. Int., 6, 24-31. Go to original source...
    7. Engen R.L., Clark C.L. (1990): High-performance liquid chromatography determination of erythrocyte membrane phospholipid composition in several animal species. Am. J. Vet. Res., 51, 577-580. Go to original source...
    8. Gaehtgens P., Schmidt F., Will G. (1981): Comparative rheology of nucleated and non-nucleated red blood cells. I. Microrheology of avian erythrocytes during capillary flow. Pflügers Arch., 390, 278-282. Go to original source... Go to PubMed...
    9. Gaetani G. F., Galiano S., Canepa L., Ferraris A.M., Kirkman H.N. (1989): Catalase and glutathione peroxidase are equally active in detoxification of hydrogen peroxide in human erythrocytes. Blood, 73, 334- 339. Go to original source...
    10. Gradinski-Vrbanac B., Timet D., Kardum P., Kecerin B. (1988): Akatalazemija u eritrocitima nekih ptica (Acatalasemia in erythrocytes of some avian species). Vet. Arhiv, 58, 91-94.
    11. Hebbel R.P. (1986): Erythrocyte antioxidants and membrane vulnerability. J. Lab. Clin. Med., 107, 401- 404.
    12. Jones G.L., Masters C.J. (1976): On the comparative characteristics of mammalian catalases. Comp. Biochem. Physiol., 55B, 511-518. Go to original source... Go to PubMed...
    13. Kaneko J.J., Harvey J.W., Bruss M.L. (1997): Clinical Biochemistry of Domestic Animals. 5th ed. Academic Press, San Diego, London, Boston, New York, Sydney, Tokyo, Toronto. 185, 168.
    14. Kidd P.M. (1997): Glutathione: Systemic protectant against oxidative and free radical damage. Alternative Med. Rew., 2, 155-176.
    15. Maral J., Puget K., Michelson A.M. (1977): Comparative study of superoxide dismutase, catalase and glutathione peroxidase levels in erythrocytes of different animals. Biochem. Biophys. Res. Comm., 77, 1525- 1535. Go to original source... Go to PubMed...
    16. Miyazaki S., Motoi Y. (1992): Tissue distribution of monomeric glutathione peroxidase in broiler chicks. Res. Vet. Sci., 53, 47-51. Go to original source... Go to PubMed...
    17. Phelps D.T., Deneke S.M., Baxter D.F., Fanburg B.L. (1989): Erythrocytes fail to induce glutathione in response to diethyl maleate on hyperoxia. Am. J. Physiol., 257, (Lung. Cell Mol. Physiol. 1), L272- L276. Go to original source...
    18. Placer Z.A., Cushman L.L., Johanson B.C. (1963): Estimation of product of lipid peroxidation (malonyl dialdehyde) in biochemical systems. Anal. Biochem., 16, 359-364. Go to original source... Go to PubMed...
    19. Reglinski J., Hoey S., Smith W.E., Sturrock R.D. (1988): Cellular response to oxidative stress at sulfhydryl group receptor sites on the erythrocyte membrane. J. Biol. Chem., 263, 12360-12366. Go to original source...
    20. Scott M.D., Zuo L., Lubin B.H., Chiu D.T.Y. (1991): NADPH, not glutathione, status modulates oxidant sensitivity in normal and glucose-6-phopsphate dehydrogenase-deficient erythrocytes. Blood, 77, 2059- 2064. Go to original source...
    21. Scott M.D., Wagner C.T., Chiu D.T.Y. (1993): Decreased catalase activity is the underlying mechanism of oxidant susceptibility in glucose-6-phosphate dehydrogenase-deficient erythrocytes. Bichem. Biophys. Acta, 1181, 163-168. Go to original source... Go to PubMed...
    22. Shviro Y., Shaklai N. (1987): Glutathione as a scavenger of free hemin. A mechanism of preventing red cell membrane damage. Bichem. Pharmacol., 36, 3801- 3807. Go to original source... Go to PubMed...
    23. Smith J.E. (1974): Relationship of in vivo erythrocyte glutathione flux to the oxidized glutathione transport system. J. Lab. Clin. Med., 83, 444-450.
    24. Sturkie P.D. (1986): Avian Physiology. Springer-Verlag, New York, Berlin, Heidelberg, Tokyo. 109-116. omas J.P., Maiorino M., Ursini F., Girotti A.W. (1990): Protective action of phospholipid hydroperoxide glutathione peroxidase against membrane-damaging lipid peroxidation. In situ reduction of phospholipd and cholesterol hydroperoxides. J. Biol. Chem., 265, 454-460. Go to original source...
    25. Trotta R.J., Sullivan S.G., Stern A. (1982): Lipid peroxidation and haemoglobin degradation in red blood cells exposed to t-butyl hydroperoxide. Biochem. J., 204, 405-415. Go to original source... Go to PubMed...
    26. Tumbleson M.E., Scholl E. (1981): In: Diseases of Swine. 5th ed. e Iowa State University Press, Ames, Iowa, U.S.A. 27-30.

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