Chemical Research in Toxicology
Article
methoxylated metabolites in transactivation assays using chinese ovary
substrate inhibition with multi-ring substrates. J. Biol. Chem. 280,
41482−41486.
(35) Nelson, P. R., Wludyka, P. S., and Copeland, K. A. F. (2005)
The Analysis of Means: A Graphical Method for Comparing Means, Rates,
and Proportions, Society for Industrial and Applied Mathematics,
Philadelphia.
cells. Environ. Health Perspect. 117, 1210−1218.
(
17) Auf’mkolk, M., Koehrle, J., Hesch, R.-D., and Cody, V. (1986)
Inhibition of rat liver iodothyronine deiodinase: Interaction of aurones
with the iodothyronine ligand-binding site. J. Biol. Chem. 261, 11623−
11630.
(
18) Schmutzler, C., Hamann, I., Hofmann, P. J., Kovacs, G.,
(36) Hofstee, B. H. J. (1952) On the evaluation of the constants V
and KM in enzyme reactions. Science 116, 329−331.
m
Stemmler, L., Mentrup, B., Schomburg, L., Ambrugger, P., Gruters, A.,
Seidlova-Wuttke, D., Jarry, H., Wuttke, W., and Kohrle, J. (2004)
Endocrine active compounds affect thyrotropin and thyroid hormone
levels in serum as well as endpoints of thyroid hormone action in liver,
heart and kidney. Toxicology 205, 95−102.
(
37) Kester, M. H. A., Kaptein, E., Roest, T. J., van Dijk, C. H.,
Tibboel, D., Meinl, W., Glatt, H., Coughtrie, M. W. H., and Visser, T.
J. (1999) Characterization of human iodothyronine sulfotransferases. J.
Clin. Endocrinol. Metab. 84, 1357−1364.
(38) Hamers, T., Kamstra, J. H., Sonneveld, E., Murk, A. J., Visser, T.
(
19) Butt, C. M., Wang, D., and Stapleton, H. M. (2011)
J., Van Velzen, M. J. M., Brouwer, A., and Bergman, A. (2008)
Biotransformation of brominated flame retardants into potentially
endocrine-disrupting metabolites, with special attention to 2,2′,4,4′-
tetrabromodiphenyl ether (BDE-47). Mol. Nutr. Food Res. 52, 284−
Halogenated phenolic contaminants inhibit the in vitro activity of
the thyroid regulating deiodinases in human liver. Toxicol. Sci. 124,
3
(
39−347.
20) Visser, T. J. (1994) Role of sulfation in thyroid hormone
metabolism. Chem.-Biol. Interact. 92, 293−303.
21) Lindsay, J., Wang, L. L., Li, Y., and Zhou, S. F. (2008) Structure,
2
(
98.
39) Kester, M. H. A., Bulduk, S., Tibboel, D., Meinl, W., Glatt, H.,
(
Falany, C. N., Coughtrie, M. W. H., Bergman, A., Safe, S. H., Kuiper,
G., Schuur, A. G., Brouwer, A., and Visser, T. J. (2000) Potent
inhibition of estrogen sulfotransferase by hydroxylated PCB
metabolites: A novel pathway explaining the estrogenic activity of
PCBs. Endocrinology 141, 1897−1900.
function and polymorphism of human cytosolic sulfotransferases. Curr.
Drug Metab. 9, 99−105.
(
22) Kester, M. H. A., Van Dijk, C. H., Tibboel, D., Hood, A. M.,
Rose, N. J. M., Meinl, W., Pabel, U., Glatt, H., Falany, C. N.,
Coughtrie, M. W. H., and Visser, T. J. (1999) Sulfation of thyroid
hormone by estrogen sulfotransferase. J. Clin. Endocrinol. Metab. 84,
(40) Shevtsov, S., Petrotchenko, E. V., Pedersen, L. C., and Negishi,
M. (2003) Crystallographic analysis of a hydroxylated polychlorinated
biphenyl (OH-PCB) bound to the catalytic estrogen binding site of
human estrogen sulfotransferase. Environ. Health Perspect. 111, 884−
2
(
577−2580.
23) Wu, S. Y., Green, W. L., Huang, W. S., Hays, M. T., and Chopra,
I. J. (2005) Alternate pathways of thyroid hormone metabolism.
8
88.
Thyroid 15, 943−958.
(41) Wang, L. Q., Falany, C. N., and James, M. O. (2004) Triclosan
(
24) Wang, L. Q., and James, M. O. (2006) Inhibition of
as a substrate and inhibitor of 3′-phosphoadenosine-5′-phosphosul-
fate-sulfotransferase and UDP-glucuronosyl transferase in human liver
fractions. Drug Metab. Dispos. 32, 1162−1169.
sulfotransferases by xenobiotics. Curr. Drug Metab., 83−104.
25) Schuur, A. G., Legger, F. F., van Meeteren, M. E., Moonen, M. J.
H., van Leeuwen-Bol, I., Bergman, A., Visser, T. J., and Brouwer, A.
1998) In vitro inhibition of thyroid hormone sulfation by
(
(42) Gamage, N. U., Duggleby, R. G., Barnett, A. C., Tresillian, M.,
(
Latham, C. F., Liyou, N. E., McManus, M. E., and Martin, J. L. (2003)
Structure of a human carcinogen-converting enzyme, SULT1A1:
Structural and kinetic implications of substrate inhibition. J. Biol. Chem.
hydroxylated metabolites of halogenated aromatic hydrocarbons.
Chem. Res. Toxicol. 11, 1075−1081.
(
26) Schuur, A. G., van Leeuwen-Bol, I., Jong, W. M. C., Bergman, A.,
2
78, 7655−7662.
Coughtrie, M. W. H., Brouwer, A., and Visser, T. J. (1998) In vitro
inhibition of thyroid hormone sulfation by polychlorobiphenylols:
Isozyme specificity and inhibition kinetics. Toxicol. Sci. 45, 188−194.
(43) Riches, Z., Stanley, E. L., Bloomer, J. C., and Coughtrie, M. W.
H. (2009) Quantitative Evaluation of the Expression and Activity of
Five Major Sulfotransferases (SULTs) in Human Tissues: The SULT
“Pie”. Drug Metab. Dispos. 37, 2255−2261.
(44) Li, X. Y., and Anderson, R. J. (1999) Sulfation of iodothyronines
by recombinant human liver steroid sulfotransferases. Biochem.
Biophys. Res. Commun. 263, 632−639.
(
27) Visser, T. J., Kaptein, E., Glatt, H., Bartsch, I., Hagen, M., and
Coughtrie, M. W. H. (1998) Characterization of thyroid hormone
sulfotransferases. Chem.-Biol. Interact. 109, 279−291.
(
28) Szabo, D. T., Richardson, V. M., Ross, D. G., Diliberto, J. J.,
Kodavanti, P. R. S., and Birnbaum, L. S. (2009) Effects of Perinatal
PBDE Exposure on Hepatic Phase I, Phase II, Phase III, and
Deiodinase 1 Gene Expression Involved in Thyroid Hormone
Metabolism in Male Rat Pups. Toxicol. Sci. 107, 27−39.
(45) Dong, D., Ako, R., and Wu, B. J. (2012) Crystal structures of
human sulfotransferases: Insights into the mechanisms of action and
substrate selectivity. Expert Opin. Drug Metab. Toxicol. 8, 635−646.
(46) Qiu, X. H., Bigsby, R. M., and Hites, R. A. (2009) Hydroxylated
Metabolites of Polybrominated Diphenyl Ethers in Human Blood
Samples from the United States. Environ. Health Perspect. 117, 93−98.
(
29) Schuur, A. G., Brouwer, A., Bergman, A., Coughtrie, M. W. H.,
and Visser, T. J. (1998) Inhibition of thyroid hormone sulfation by
hydroxylated metabolites of polychlorinated biphenyls. Chem.-Biol.
Interact. 109, 293−297.
(
47) Chopra, I. J., Wu, S. Y., Teco, G. N. C., and Santini, F. (1992) A
radioimmunoassay for measurement of 3,5,3′-triiodothyronine sulfate:
Studies in thyroidal and nonthyroidal diseases, pregnancy, and
neonatal life. J. Clin. Endocrinol. Metab. 75, 189−194.
(
30) Wu, G. S., Robertson, D. H., Brooks, C. L., and Vieth, M.
(
2003) Detailed analysis of grid-based molecular docking: A case study
(48) Esfandiari, A., Gavaret, J. M., Lennon, A. M., Pierre, M., and
of CDOCKER: A CHARMm-based MD docking algorithm. J. Comput.
Chem. 24, 1549−1562.
Courtin, F. (1994) Sulfation after deiodination of 3,5,3′-triiodothyr-
onine in rat cultured astrocytes. Endocrinology 135, 2086−2092.
(
31) Vieth, M., Hirst, J. D., Kolinski, A., and Brooks, C. L. (1998)
(49) Athanasiadou, M., Cuadra, S. N., Marsh, G., Bergman, A., and
Assessing energy functions for flexible docking. J. Comput. Chem. 19,
612−1622.
32) Mattila, K., and Renkonen, R. (2009) Modelling of Bet v 1
Binding to Lipids. Scand. J. Immunol. 70, 116−124.
33) Koska, J., Spassov, V. Z., Maynard, A. J., Yan, L., Austin, N.,
Jakobsson, K. (2008) Polybrominated diphenyl ethers (PBDEs) and
bioaccumulative hydroxylated PBDE metabolites in young humans
from Managua, Nicaragua. Environ. Health Perspect. 116, 400−408.
1
(
(
Flook, P. K., and Venkatachalam, C. M. (2008) Fully Automated
Molecular Mechanics Based Induced Fit Protein-Ligand Docking
Method. J. Chem. Inf. Model. 48, 1965−1973.
(
34) Gamage, N. U., Tsvetanov, S., Duggleby, R. G., McManus, M.
E., and Martin, J. L. (2005) The structure of human SULT1A1
crystallized with estradiol: An insight into active site plasticity and
1
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dx.doi.org/10.1021/tx400342k | Chem. Res. Toxicol. 2013, 26, 1692−1702