Effects of prototypic PCBs on benzo[ a ]pyrene mutagenic activity related to vitamin A intake
Identifieur interne : 000C58 ( Istex/Curation ); précédent : 000C57; suivant : 000C59Effects of prototypic PCBs on benzo[ a ]pyrene mutagenic activity related to vitamin A intake
Auteurs : P. Grolier [France] ; P. Cassand [France] ; E. Antignac [France] ; J. F. Narbonne [France] ; R. Albrecht [France] ; V. Azais [France] ; L. W. Robertson [États-Unis] ; F. Oesch [Allemagne]Source :
- Mutation Research - Fundamental and Molecular Mechanisms of Mutagenesis [ 0027-5107 ] ; 1989.
Abstract
The effects of vitamin A dietary intake (2 and 20 IU∗/g of food) on the mutagenic activity of benzo[a]pyrene (B(a)P) toward Salmonella typhimurium (TA98) were studied either in control rats or in animals treated by the PCB congeners 2,4,5,2′,4′,5′-hexachlorobiphenyl ((2,4,5)2Cl) and 3,4,3′,4′-tetrachlorobiphenyl ((3,4)2Cl). (3,4)2Cl (a planar compound) strongly increased B(a)P monooxygenase (B(a)PMO) activity and glutathione transferase, (2,4,5)2Cl (a non-planar PCB) was a strong inducer of epoxide hydrolase and a weak inducer of B(a)PMO. Enzyme induction was not modified by changes in vitamin A dietary intake. A higher mutagenic effect was observed in the (3,4)2Cl group than in the (2,4,5)2Cl one. This could be related to the specific form of cytochrome P-450 induced by (3,4)2Cl. In the untreated animals, the activation of B(a)P was higher in the 2-IU group than in the 20-IU one. Conversely, in PCB-treated rats the mutagenic activity of B(a)P was higher in the 20-IU group than in the 2-IU one. PCB induction increased the liver content of vitamin C in both the 2-IU and the 20-IU groups but only increased the glutathione levels in the 2-IU groups. This suggests that glutathione content in cellular fractions may be one of the determining parameters for the mutagenic activity of B(a)P.
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DOI: 10.1016/0027-5107(89)90114-0
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Antignac</name><affiliation wicri:level="1"><mods:affiliation>Réseau Toxicologie Nutritionelle MRES, Université de Bordeaux I, 33405 Talence Cedex France</mods:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Réseau Toxicologie Nutritionelle MRES, Université de Bordeaux I</wicri:regionArea></affiliation></author><author><name sortKey="Narbonne, J F" sort="Narbonne, J F" uniqKey="Narbonne J" first="J. F." last="Narbonne">J. F. Narbonne</name><affiliation wicri:level="1"><mods:affiliation>Laboratoire de Toxicologie Nutritionelle, Université de Bordeaux I, 33405 Talence Cedex France</mods:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de Toxicologie Nutritionelle, Université de Bordeaux I</wicri:regionArea></affiliation><affiliation wicri:level="1"><mods:affiliation>Correspondence: Dr. J.F. Narbonne, Laboratoire de Toxicologie Alimentaire, Université de Bordeaux I, 33405 Talence Cedex France</mods:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Correspondence: Dr. J.F. Narbonne, Laboratoire de Toxicologie Alimentaire, Université de Bordeaux I</wicri:regionArea></affiliation></author><author><name sortKey="Albrecht, R" sort="Albrecht, R" uniqKey="Albrecht R" first="R." last="Albrecht">R. Albrecht</name><affiliation wicri:level="1"><mods:affiliation>Laboratoire de Biologie CNAM, 75003 Paris France</mods:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de Biologie CNAM</wicri:regionArea></affiliation></author><author><name sortKey="Azais, V" sort="Azais, V" uniqKey="Azais V" first="V." last="Azais">V. Azais</name><affiliation wicri:level="1"><mods:affiliation>Station de Recherches de Nutrition, INRA, CRNZ, 78350, Jouy-en-Josas France</mods:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Station de Recherches de Nutrition, INRA, CRNZ, 78350</wicri:regionArea></affiliation></author><author><name sortKey="Robertson, L W" sort="Robertson, L W" uniqKey="Robertson L" first="L. W." last="Robertson">L. W. Robertson</name><affiliation wicri:level="2"><mods:affiliation>Graduate Center for Toxicology, University of Kentucky, Lexington, KY 40506-0054 U.S.A.</mods:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Kentucky</region></placeName><wicri:cityArea>Graduate Center for Toxicology, University of Kentucky, Lexington</wicri:cityArea></affiliation></author><author><name sortKey="Oesch, F" sort="Oesch, F" uniqKey="Oesch F" first="F." last="Oesch">F. 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(3,4)2Cl (a planar compound) strongly increased B(a)P monooxygenase (B(a)PMO) activity and glutathione transferase, (2,4,5)2Cl (a non-planar PCB) was a strong inducer of epoxide hydrolase and a weak inducer of B(a)PMO. Enzyme induction was not modified by changes in vitamin A dietary intake. A higher mutagenic effect was observed in the (3,4)2Cl group than in the (2,4,5)2Cl one. This could be related to the specific form of cytochrome P-450 induced by (3,4)2Cl. In the untreated animals, the activation of B(a)P was higher in the 2-IU group than in the 20-IU one. Conversely, in PCB-treated rats the mutagenic activity of B(a)P was higher in the 20-IU group than in the 2-IU one. PCB induction increased the liver content of vitamin C in both the 2-IU and the 20-IU groups but only increased the glutathione levels in the 2-IU groups. This suggests that glutathione content in cellular fractions may be one of the determining parameters for the mutagenic activity of B(a)P.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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