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Research ArticleArticle

17β-Estradiol Induces Sulfotransferase 2A1 Expression through Estrogen Receptor α

Wei Li, Miaoran Ning, Kwi Hye Koh, Heesue Kim and Hyunyoung Jeong
Drug Metabolism and Disposition April 2014, 42 (4) 796-802; DOI: https://doi.org/10.1124/dmd.113.055178
Wei Li
Department of Pharmacy Practice (W.L., K.H.K., H.K., H.J.) and Department of Biopharmaceutical Sciences (M.N., H.J.), College of Pharmacy, University of Illinois at Chicago, Chicago, Illinois; and Medical College, Yangzhou University, Yangzhou, Jiangsu, China (W.L.)
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Miaoran Ning
Department of Pharmacy Practice (W.L., K.H.K., H.K., H.J.) and Department of Biopharmaceutical Sciences (M.N., H.J.), College of Pharmacy, University of Illinois at Chicago, Chicago, Illinois; and Medical College, Yangzhou University, Yangzhou, Jiangsu, China (W.L.)
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Kwi Hye Koh
Department of Pharmacy Practice (W.L., K.H.K., H.K., H.J.) and Department of Biopharmaceutical Sciences (M.N., H.J.), College of Pharmacy, University of Illinois at Chicago, Chicago, Illinois; and Medical College, Yangzhou University, Yangzhou, Jiangsu, China (W.L.)
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Heesue Kim
Department of Pharmacy Practice (W.L., K.H.K., H.K., H.J.) and Department of Biopharmaceutical Sciences (M.N., H.J.), College of Pharmacy, University of Illinois at Chicago, Chicago, Illinois; and Medical College, Yangzhou University, Yangzhou, Jiangsu, China (W.L.)
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Hyunyoung Jeong
Department of Pharmacy Practice (W.L., K.H.K., H.K., H.J.) and Department of Biopharmaceutical Sciences (M.N., H.J.), College of Pharmacy, University of Illinois at Chicago, Chicago, Illinois; and Medical College, Yangzhou University, Yangzhou, Jiangsu, China (W.L.)
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Abstract

Sulfotransferase (SULT) 2A1 catalyzes sulfonation of drugs and endogenous compounds and plays an important role in xenobiotic metabolism as well as in the maintenance of steroid and lipid homeostasis. A recent study showed that 17β-estradiol (E2) increases the mRNA levels of SULT2A1 in human hepatocytes. Here we report the underlying molecular mechanisms. E2 enhanced SULT2A1 expression in human hepatocytes and HepG2-ER cells (HepG2 stably expressing ERα). SULT2A1 induction by E2 was abrogated by antiestrogen ICI 182,780, indicating a key role of ERα in the induction. Results from deletion and mutation assays of SULT2A1 promoter revealed three cis-elements located within –257/+140 region of SULT2A1 that are potentially responsible for the induction. Chromatin immunoprecipitation assay verified the recruitment of ERα to the promoter region. Electrophoretic mobility shift assays revealed that AP-1 proteins bind to one of the cis-elements. Interestingly, SULT2A1 promoter assays using ERα mutants revealed that the DNA-binding domain of ERα is indispensable for SULT2A1 induction by E2, suggesting that direct ERα binding to the SULT2A1 promoter is also necessary for the induction. Taken together, our results indicate that E2 enhances SULT2A1 expression by both the classical and nonclassical mechanisms of ERα action.

Footnotes

    • Received October 8, 2013.
    • Accepted February 3, 2014.
  • This work was supported by the National Institutes of Health Eunice Kennedy Shriver National Institute of Child Health and Human Development [Grant HD065532].

  • dx.doi.org/10.1124/dmd.113.055178.

  • ↵Embedded ImageThis article has supplemental material available at dmd.aspetjournals.org.

  • Copyright © 2014 by The American Society for Pharmacology and Experimental Therapeutics
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Drug Metabolism and Disposition: 42 (4)
Drug Metabolism and Disposition
Vol. 42, Issue 4
1 Apr 2014
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Research ArticleArticle

SULT2A1 Induction by E2

Wei Li, Miaoran Ning, Kwi Hye Koh, Heesue Kim and Hyunyoung Jeong
Drug Metabolism and Disposition April 1, 2014, 42 (4) 796-802; DOI: https://doi.org/10.1124/dmd.113.055178

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Research ArticleArticle

SULT2A1 Induction by E2

Wei Li, Miaoran Ning, Kwi Hye Koh, Heesue Kim and Hyunyoung Jeong
Drug Metabolism and Disposition April 1, 2014, 42 (4) 796-802; DOI: https://doi.org/10.1124/dmd.113.055178
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