Hostname: page-component-586b7cd67f-2brh9 Total loading time: 0 Render date: 2024-11-27T19:48:13.876Z Has data issue: false hasContentIssue false
  • English
  • Français

Modulation of paraquat toxicity by β-carotene at low oxygen partial pressure in chicken embryo fibroblasts

Published online by Cambridge University Press:  09 March 2007

Susan M. Lawlor  and
Nora M. O'Brien
Susan M. Lawlor
Affiliation:
Department of Nutrition, National Food Biotechnology Centre, University College, Cork, Ireland
Nora M. O'Brien
Affiliation:
Department of Nutrition, National Food Biotechnology Centre, University College, Cork, Ireland
Rights & Permissions [Opens in a new window]

Abstract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

The efficiency with which β-carotene protects against oxidative stress in chicken embryo fibrobiasts (CEF) at low O2 partial pressures was assessed. Primary cultures of CEF were grown at low O2 partial pressures and oxidatively stressed by exposure to paraquat (PQ). Activities of the antioxidant enzymes superoxide dismutase (EC 1.15.1.1; SOD), catalase (EC 1.11.1.6; CAT) and glutathione peroxidase (EC 1.11.1.9; GSH-Px) were measured as indices of oxidative stress. CEF incubated with 0·25–1·0 mM—PQ for 18 h exhibited increased SOD and CAT activities compared with non-PQ-treated control cells (P < 0·001). No cytotoxicity as indicated by lactate dehydrogenase (EC 1.1.1.27; LDH) release was observed at PQ concentrations below 2·0 mM. Incorporation of added β-carotene into 0·25 mM-PQ-treated cells prevented the PQ-induced increases in SOD and CAT, and activities were similar to those seen in non-PQ-treated control cells. GSH-Px activity decreased relative to its control value on exposure to 0·25 mM-PQ and β-carotene prevented this decrease in a dose-dependent manner. The proportion of LDH released from the CEF treated with β-carotene remained below the control value of 2·5% at all times.

Keywords

β-CaroteneOxidative stressChicken embryo fibroblastsParaquat
Type
General Nutrition
Information
British Journal of Nutrition , Volume 77 , Issue 1 , January 1997 , pp. 133 - 140
Copyright
Copyright © The Nutrition Society 1997

References

REFERENCES

Baudhuin, P., Beaufay, H., Rahman-Li, Y., Sellinger, O. Z., Wattiaux, R., Jacques, P. & deDuve, C. (1964). Tissue fractionation studies. Intracellular distribution of monoamine oxidase, aspartate aminotransferase, Daminoacid oxidase and catalase in rat liver tissue. Biochemical Journal 92, 179–184.CrossRefGoogle Scholar
Betram, J. S., Pung, A., Churley, M., Kappock, T. J., Wilkens, L. R. & Cooney, R. V. (1991). Diverse carotenoids protect from chemically-induced neoplastic transformation. Carcinogenesis 12, 671–678.CrossRefGoogle Scholar
Bosca, L., Rousseau, G. G. & Hue, L. (1985). Phorbol 12-myristate 13-acetate and insulin increase the concentration of fructose-2,6-bisphosphate and stimulate glycolysis in chicken embryo fibroblasts. Proceedings of the National Academy of Sciences USA 82, 6440–6444.CrossRefGoogle ScholarPubMed
Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72, 248–254.CrossRefGoogle ScholarPubMed
Burton, G. W. (1989). Antioxidant function of carotenoids. Journal of Nutrition 119, 109–111.CrossRefGoogle Scholar
Burton, G. W. & Ingold, K. U. (1984). β-Carotene: an unusual type of lipid antioxidant. Science 224, 569–573.CrossRefGoogle ScholarPubMed
Bus, J. S., Auat, S. D. & Gibson, J. E. (1974). Superoxide and singlet oxygen-catalyzed lipid peroxidation as a possible mechanism for paraquat (methyl viologen) toxicity. Biochemical and Biophysical Research Communications 58, 749–755.CrossRefGoogle ScholarPubMed
Deneke, S. M., & Fanburg, B. L. (1980). Normobaric oxygen toxicity of the lung. New England Journal of Medicine 303, 76–86.CrossRefGoogle ScholarPubMed
Foote, C. S., & Denny, R. W. (1968). Chemistry of singlet oxygen. VII. Quenching by β-carotene. Journal of the American Chemical Society 90, 6233–6235.CrossRefGoogle Scholar
Garewal, H. S., Meyskens, F. L. Jr, Killen, D., Reeves, D., Kiersch, T. A., Elletson, H., Strasbert, A., King, D. & Steinbronn, K. (1990). Response of oral leucoplakia to β-carotene. Journal of Clinical Oncology 8, 1715–1720.CrossRefGoogle ScholarPubMed
Guenzler, W. A., Kremers, H. & Flohe, L. (1974). An improved coupled test procedure for glutathione peroxidase in blood. Zeitschrift für Klinische Chemie und Klinische Biochemie 12, 444–448.Google Scholar
Kennedy, T. A. & Liebler, D. C. (1992). Peroxyl radical scavenging by β-carotene in lipid bilayers. Effect of oxygen partial pressure. Journal of Biological Chemistry 267, 4658–4663.CrossRefGoogle ScholarPubMed
Kono, Y. & Fridovich, I. (1982). Superoxide radical inhibits catalase. Journal of Biological Chemistry 257, 5751–5754.CrossRefGoogle ScholarPubMed
Krall, J., Speranza, M. J. & Lynch, R. E. (1991). Paraquat-resistant Hela Cells: increased cellular content of glutathione peroxidase. Archives of Biochemistry and Biophysics 286, 311–315.CrossRefGoogle ScholarPubMed
Krinksy, N. I. (1989). Carotenoids and cancer in animal models. Journal of Nutrition 119, 123–126.Google Scholar
Krinksy, N. I. (1993). Actions of carotenoids in biological systems. Annual Review of Nutrition 13, 561–587.Google Scholar
Krinksy, N. I. & Deneke, S. M. (1982). Interaction of oxygen and oxy-radicals with carotenoids. Journal of the National Cancer Institute 69, 205–210.Google Scholar
Lawlor, S. M. & O'Brien, N. M. (1994). Development of an in vitro cell culture model to investigate the induction and quantification of oxidative stress and its inhibition by α-tocopherol. Toxicology In Vitro 8, 67–73.CrossRefGoogle Scholar
Lawlor, S. M. & O'Brien, N. M. (1995). Modulation of oxidative stress by β-carotene in chicken embryo fibroblasts. British Journal of Nutrition 73, 841–850.CrossRefGoogle ScholarPubMed
McCord, J. M. & Fridovich, I. (1969). Superoxide dismutase: an enzyme function for erythrocuprein (hemocuprein). Journal of Biological Chemistry 244, 6049–6055.CrossRefGoogle ScholarPubMed
Nicotera, T. M., Block, A. W., Gibas, Z. & Sandberg, A. A. (1985). Induction of superoxide dismutase, chromosomal aberrations and sister-chromatid exhanges by paraquat in Chinese hamster fibroblasts. Mutation Research 151, 263–268.CrossRefGoogle Scholar
Palozza, P. & Krinsky, N. I. (1991). The inhibition of radical-initiated peroxidation of microsomal lipids by both α-tocopherol and β-carotene. Free Radicals in Biology and Medicine 11, 407–414.CrossRefGoogle ScholarPubMed
Pryor, W. A. (1991). The antioxidant nutrients and disease prevention — what do we know and what do we need to find out? American Journal of Clinical Nutrition 53, 391S–393S.CrossRefGoogle ScholarPubMed
Snedecor, G. W. (1964). Sampling from a normally distributed population. In Statistical Methods, p. 45 [Snedecor, G. W. and Cochran, W. G., editors]. Ames, IA: Iowa State University Press.Google Scholar
Stevens, T. M., Boswell, G. A. Jr, Adler, R., Ackerman, N. R. & Kerr, J. S. (1988). Induction of antioxidant enzyme activities by a phenyl urea derivative EDU. Toxicology and Applied Pharmacology 96, 133–142.CrossRefGoogle Scholar
Stocker, R., Yamamoto, Y., McDonagh, A. F., Glazer, A. N. & Ames, B. N. (1987). Bilirubin is an antioxidant of possible physiological importance. Science 235, 1043–1046.CrossRefGoogle ScholarPubMed
Terao, J., Yamauchi, R., Murakami, H. & Matsushita, S. (1980). Inhibitory effects of tocopherols and β-carotene on singlet-oxygen initiated photo-oxidation of methyl linoleate and soyabean oil. Journal of Food Processing and Preservation 4, 79–83.CrossRefGoogle Scholar
Vassault, A. (1983). Lactate dehydrogenase. In Methods of Enzymatic Analysis, pp. 118–126 [Bergmeyer, H. U., editor]. Weinheim, Germany: Verlag Chemie.Google Scholar
Ziegler, R. G. (1991). Vegetables, fruits and carotenoids and the risk of cancer. American Journal of Clinical Nutrition 53, 251S–259S.CrossRefGoogle ScholarPubMed