Effects of pentachlorophenol and hydroxylated polychlorinated biphenyls on thyroid hormone conjugation in a rat and a human hepatoma cell line

Toxicology in Vitro

Volumn 13, Issue 3, 1999, Pages 417-425

  Schuur, A G ^a   Bergman, Å ^c   Brouwer, A ^a   Visser, T J ^b  

^a WAGENINGEN UNIVERSITY   (Netherlands)

^b ERASMUS MEDICAL CENTER   (Netherlands)

^c STOCKHOLM UNIVERSITY   (Sweden)

Author keywords

FaO; HepG2; PCB metabolites; Pentachlorophenol; Sulfation; Thyroid hormone

Indexed keywords

3,3' DIIODOTHYRONINE; DRUG METABOLITE; PENTACHLOROPHENOL; POLYCHLORINATED BIPHENYL; THYROID HORMONE;

ANIMAL CELL; ARTICLE; CYTOSOL; DRUG CONJUGATION; GLUCURONIDATION; HEPATOMA CELL; NONHUMAN; RAT; SULFATION; THYROID HORMONE METABOLISM;

EID: 0032865121     PISSN: 08872333     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0887-2333(99)00005-3     Document Type: Article

References (33)

1. Adams C., Lans M. C., Klasson Wehler E., van Engelen J. G. M., Visser T. J. and Brouwer A. (1990) Hepatic thyroid hormone 5′-deiodinase, another target-protein for monohydroxy metabolites of 3,3′,4,4′-tetrachlorobiphenyl. In Organohalogen Compounds, ed. O. Hutzinger and H. Fielder, Vol. 1, pp. 51-54. Ecoinforma Press, Bayreuth, Germany.
2. Bergman Å, Klasson-Wehler E., Kuroki H. Selective retention of hydroxylated PCB metabolites in blood. Environmental Health Perspectives. 102:1994;464-469.
3. Bergman Å, Klasson-Wehler E., Kuroki H., Nilsson A. Synthesis and mass spectrometry of some methoxylated PCBs. Chemosphere. 30:1995;1921-1938.
4. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry. 72:1976;248-254.
5. Brouwer A., Morse D.C., Lans M.C., Schuur A.G., Murk A.J., Klasson-Wehler E., Bergman A., Visser T.J. Interactions of persistent environmental organohalogens with the thyroid hormone system: Mechanisms and possible consequences for animal and human health. Toxicological and Industrial Health. 14:1998;59-84.
6. Dawson J.R., Adams D.J., Wolf C.R. Induction of drug metabolizing enzymes in human liver cell line Hep G2. FEBS Letters. 183:1985;219-222.
7. De Jong M., Rolleman E.J., Bernard H.F. T2 and triac are sulfated in HEPG2 cells, whereas T3 sulfation is absent. Thyroid. 5:(Suppl. 1):1995;S125.
8. Eaton E.A., Walle U.K., Lewis A.J., Hudson T., Wilson A.A., Walle T. Flavonoids, potent inhibitors of the human p-form phenolsulfotransferase. Drug Metabolism and Disposition. 24:1996;232-237.
9. Kaptein E., van Haasteren G.A.C., Linkels E., de Greef W.J., Visser T.J. Characterization of iodothyronine sulfotransferase activity in rat liver. Endocrinology. 138:1997;5136-5143.
10. Klasson-Wehler E., Brunstrom B., Rannug U. and Bergman A. 1990. 3,3′,4,4′-tetrachlorobiphenyl: metabolism by chick embryo in ovo, Chemico-Biological Interactions 73. 121-132.
11. Koster H., Halsema I., Scholtens E., Meerman J.H.N., Pang K.S., Mulder G.J. Selective inhibition of sulfate conjugation in the rat - pharmacokinetics and characterization of the inhibitory effect of 2,6-dichloro-4-nitrophenol. Biochemical Pharmacology. 31:1982;1919-1924.
12. Lans M.C., Klasson-Wehler E., Willemsen M., Meussen E., Safe S., Brouwer A. Structure-dependent, competitive interaction of hydroxy-polychlorobiphenyls, -dibenzo-p-dioxins and -dibenzofurans with human transthyretin. Chemico-Biological Interactions. 88:1993;7-21.
13. Lans M.C., Spiertz C., Brouwer A., Koeman J.H. Different competition of thyroxine binding to transthyretin and thyroxine-binding globulin by hydroxy-PCBs, PCDDs and PCDFs. European Journal of Pharmacology. 270:1994;129-136.
14. Meerman J.H.N., Sterenborg H.M.J., Mulder G.J. Use of pentachlorophenol as long-term inhibitor of sulfation of phenols and hydroamic acids in the rat in vivo. Biochemical Pharmacology. 32:1983;1587-1593.
15. Morse D.C., Klasson-Wehler E., Wesseling W., Koeman J.H., Brouwer A. Alterations in rat brain thyroid hormone status following pre- and postnatal exposure to polychlorinated biphenyls (Aroclor 1254). Toxicology and Applied Pharmacology. 136:1996;269-279.
16. Mulder G.J., Scholtens E. Phenol sulphotransferase and uridine diphosphate glucuronyltransferase from rat liver in vivo and in vitro. 2,6-Dichloro-4-nitrophenol as a selective inhibitor of sulphation. Biochemical Journal. 165:1977;553-559.
17. Otten M.H., Mol J.A., Visser T.J. Sulfation preceding deiodination of iodothyronines in rat hepatocytes. Science. 221:1983;81-83.
18. Rutgers M., Bonthuis F., de Herder W.W., Visser T.J. Accumulation of plasma triiodothyronine sulfate in rats treated with propylthiouracil. Journal of Clinical Investigation. 80:1987;758-762.
19. Santini F., Chopra I.J., Wu S.Y., Solomon D.H., Chua Teco G.N. Metabolism of 3,5,3′-triiodothyronine sulfate by tissues of the foetal rat: A consideration of the role of desulfation of 3,5,3′-triiodothyronine sulfate as a source of T3. Pediatric Research. 31:1992;541-544.
20. Santini F., Hurd R.E., Chopra I.J. A study of metabolism of deaminated and sulfoconjugated iodothyronines by rat placental iodothyronine 5-monodeiodinase. Endocrinology. 131:1992;1689-1694.
21. Schuur A.G., Legger F.F., van Meeteren M.E., Moonen M.J.H., van Leeuwen-Bol I., Bergman Å, Visser T.J., Brouwer A. In vitro inhibition of thyroid hormone sulfation by hydroxylated metabolites of halogenated aromatic hydrocarbons. Chemical Research in Toxicology. 11:1998;1075-1081.
22. Schuur A.G., van Leeuwen-Bol I., Jong W.M.C., Bergman Å, Coughtrie M.W.H., Brouwer A., Visser T.J. In vitro inhibition of thyroid hormone sulfation by polychlorobiphenylols: isozyme specificity and inhibition kinetics. Toxicological Sciences. 45:1998;188-194.
23. Shali N.A., Curtis C.G., Powell G.M., Roy A.B. Sulphation of the flavonoids quercetin and catechin by rat liver. Xenobiotica. 21:1991;881-893.
24. Shwed J.A., Walle U.K., Walle T. HepG2 cell line as a human model for sulphate conjugation of drugs. Xenobiotica. 22:1992;973-982.
25. Spaulding S.W., Smith T.J., Hinkle P.M., Davis F.B., Kung M.P., Roth J.A. Studies on the biological activity of triiodothyronine sulfate. Journal of Clinical Endocrinology and Metabolism. 74:1992;1062-1067.
26. Utesch D., Oesch F. Dependency of the in vitro stabilization of differentiated functions in liver parenchymal cells on the type of cell line used for co-culture. In vitro Cell Development and Biology. 28A:1992;193-198.
27. Van Stralen P.G.J., van der Hoek H.J., Docter R., de Jong M., Krenning E. Reduced T3 deiodination by the human hepatoblastoma cell line HepG2 caused by deficient T3 sulfation. Biochimica et Biophysica Acta. 1157:1993;114-118.
28. Visser T. J. (1990) Importance of deiodination and conjugation in the hepatic metabolism of thyroid hormone. In The Thyroid Gland, ed. M. A. Greer, pp. 255-283. Raven Press, New York.
29. Visser T.J. Role of sulfation in thyroid hormone metabolism. Chemico-Biological Interactions. 92:1994;293-303.
30. Visser T.J., Fekker D., Docter R., Hennemann G. Sequential deiodination of thyroxine in rat liver homogenate. Biochemical Journal. 174:1978;221-229.
31. Visser T.J., Kaptein E., Glatt H., Bartsch I., Hagen M., Coughtrie M.W.H. Characterization of thyroid hormone sulfotransferases. Chemico-Biological Interactions. 109:1998;279-291.
32. Visser T.J., Otten M.H., Mol J.A., Docter R., Henneman G. Sulfation facilitates hepatic deiodination of iodothyronines. Hormone and Metabolism Research. 14:1984;35-41.
33. Visser T.J., van Buuren J.C.J., Rutgers M., Eelkman Rooda S.J., de Herder W.W. The role of sulfation in thyroid hormone metabolism. Trends in Endocrinology and Metabolism. 1:1990;211-218.