Regulation of the cytosolic sulfotransferases by nuclear receptors

References

• Aksoy, I. A., Otterness, D. M., Weinshilboum, R. M. (1993a). Cholesterol sulfation in human liver. Catalysis by dehydroepiandrosterone sulfotransferase. Drug Metab Dispos 21:268–276.
   PubMed Web of Science ®Google Scholar
• Aksoy, I. A., Sochorova, V., Weinshilboum, R. M. (1993b). Human liver dehydroepiandrosterone sulfotransferase: nature and extent of individual variation. Clin Pharmacol Ther 54:498–506.
   PubMed Web of Science ®Google Scholar
• Aleksunes, L. M., Klaassen, C. D. (2012). Coordinated regulation of hepatic phase-I and -II drug metabolizing genes and transporters using AhR-, CAR-, PXR-, PPARalpha-, and Nrf2-null mice. Drug Metab Dispos 40:1366–1379.
   PubMed Web of Science ®Google Scholar
• Alnouti, Y. (2009). Bile acid sulfation: a pathway of bile acid elimination and detoxification. Toxicol Sci 108:225–246.
   PubMed Web of Science ®Google Scholar
• Alnouti, Y., Klaassen, C. D. (2008). Regulation of sulfotransferase enzymes by prototypical microsomal enzyme inducers in mice. J Pharmacol Exp Ther 324:612–621.
   PubMed Web of Science ®Google Scholar
• Assem, M., Schuetz, E. G., Leggas, M., Sun, D., Yasuda, K., Reid, G., et al. (2004). Interactions between hepatic Mrp4 and Sult2a as revealed by the constitutive androstane receptor and Mrp4 knockout mice. J Biol Chem 279:22250–22257.
   PubMed Web of Science ®Google Scholar
• Baes, M., Gulick, T., Choi, H. S., Martinoli, M. G., Simha, D., Moore, D. D. (1994). A new orphan member of the nuclear hormone receptor superfamily that interacts with a subset of retinoic acid response elements. Mol Cell Biol 14:1544–1552.
   PubMed Web of Science ®Google Scholar
• Bai, Q., Zhang, X., Xu, L., Kakiyama, G., Heuman, D., Sanyal, A., et al. (2012). Oxysterol sulfation by cytosolic sulfotransferase suppresses liver X receptor/sterol regulatory element binding protein-1c signaling pathway and reduces serum and hepatic lipids in mouse models of nonalcoholic fatty liver disease. Metabolism 61:836–845.
   PubMed Web of Science ®Google Scholar
• Banoglu, E. (2000). Current status of the cytosolic sulfotransferases in the metabolic activation of promutagens and procarcinogens. Curr Drug Metab 1:1–30.
   PubMed Web of Science ®Google Scholar
• Barnes, S., Buchina, E. S., King, R. J., McBurnett, T., Taylor, K. B. (1989). Bile acid sulfotransferase I from rat liver sulfates bile acids and 3-hydroxy steroids: purification, N-terminal amino acid sequence, and kinetic properties. J Lipid Res 30:529–540.
   PubMed Web of Science ®Google Scholar
• Bertoni, A., Rastoldo, A., Sarasso, C., Di, V. C., Sampietro, S., Nalin, M., et al. (2012). Dehydroepiandrosterone-sulfate inhibits thrombin-induced platelet aggregation. Steroids 77:260–268.
   PubMed Web of Science ®Google Scholar
• Blanchard, R. L. (2005). Nomenclature and molecular biology of the human sulfotransferase family. In: Pacifici, G. M., Coughtrie, M. W. H. (Eds.), Human cytosolic sulfotransferases (pp. 1–26). Boca Raton, Florida, USA: Taylor & Francis.
   Google Scholar
• Bogan, A. A., Dallas-Yang, Q., Ruse, M. D., Jr., Maeda, Y., Jiang, G., Nepomuceno, L., et al. (2000). Analysis of protein dimerization and ligand binding of orphan receptor HNF4alpha. J Mol Biol 302:831–851.
   PubMed Web of Science ®Google Scholar
• Choi, H. S., Chung, M., Tzameli, I., Simha, D., Lee, Y. K., Seol, W., et al. (1997). Differential transactivation by two isoforms of the orphan nuclear hormone receptor CAR. J Biol Chem 272:23565–23571.
   PubMed Web of Science ®Google Scholar
• Cook, I. T., Duniec-Dmuchowski, Z., Kocarek, T. A., Runge-Morris, M., Falany, C. N. (2009). 24-hydroxycholesterol sulfation by human cytosolic sulfotransferases: formation of monosulfates and disulfates, molecular modeling, sulfatase sensitivity, and inhibition of liver x receptor activation. Drug Metab Dispos 37:2069–2078.
   PubMed Web of Science ®Google Scholar
• Coward, P., Lee, D., Hull, M. V., Lehmann, J. M. (2001). 4-Hydroxytamoxifen binds to and deactivates the estrogen-related receptor gamma. Proc Natl Acad Sci U S A 98:8880–8884.
   PubMed Web of Science ®Google Scholar
• Cui, J. Y., Aleksunes, L. M., Tanaka, Y., Fu, Z. D., Guo, Y., Guo, G. L., et al. (2012). Bile acids via FXR initiate the expression of major transporters involved in the enterohepatic circulation of bile acids in newborn mice. Am J Physiol Gastrointest Liver Physiol 302:G979–G996.
   PubMed Web of Science ®Google Scholar
• Ding, X., Lichti, K., Kim, I., Gonzalez, F. J., Staudinger, J. L. (2006). Regulation of constitutive androstane receptor and its target genes by fasting, cAMP, hepatocyte nuclear factor alpha, and the coactivator peroxisome proliferator-activated receptor gamma coactivator-1alpha. J Biol Chem 281:26540–26551.
   PubMed Web of Science ®Google Scholar
• Dooley, T. P., Haldeman-Cahill, R., Joiner, J., Wilborn, T. W. (2000). Expression profiling of human sulfotransferase and sulfatase gene superfamilies in epithelial tissues and cultured cells. Biochem Biophys Res Commun 277:236–245.
   PubMed Web of Science ®Google Scholar
• Duanmu, Z., Weckle, A., Koukouritaki, S. B., Hines, R. N., Falany, J. L., Falany, C. N., et al. (2006). Developmental expression of aryl, estrogen, and hydroxysteroid sulfotransferases in pre- and postnatal human liver. J Pharmacol Exp Ther 316:1310–1317.
   PubMed Web of Science ®Google Scholar
• Duffel, M. W., Binder, T. P., Hosie, L., Baden, H. A., Sanders, J. A., Knapp, S. A., et al. (1991). Purification, immunochemical characterization, and immunohistochemical localization of rat hepatic aryl sulfotransferase IV. Mol Pharmacol 40:36–44.
   PubMed Web of Science ®Google Scholar
• Dumas, N. A., He, D., Frost, A. R., Falany, C. N. (2008). Sulfotransferase 2B1b in human breast: differences in subcellular localization in African American and Caucasian women. J Steroid Biochem Mol Biol 111:171–177.
   PubMed Web of Science ®Google Scholar
• Echchgadda, I., Song, C. S., Oh, T., Ahmed, M., De La Cruz, I. J., Chatterjee, B. (2007). The xenobiotic-sensing nuclear receptors pregnane X receptor, constitutive androstane receptor, and orphan nuclear receptor hepatocyte nuclear factor 4alpha in the regulation of human steroid-/bile acid-sulfotransferase. Mol Endocrinol 21:2099–2111.
   PubMed Web of Science ®Google Scholar
• Echchgadda, I., Song, C. S., Oh, T. S., Cho, S. H., Rivera, O. J., Chatterjee, B. (2004a). Gene regulation for the senescence marker protein DHEA-sulfotransferase by the xenobiotic-activated nuclear pregnane X receptor (PXR). Mech Ageing Dev 125:733–745.
   PubMed Web of Science ®Google Scholar
• Echchgadda, I., Song, C. S., Roy, A. K., Chatterjee, B. (2004b). Dehydroepiandrosterone sulfotransferase is a target for transcriptional induction by the vitamin D receptor. Mol Pharmacol 65:720–729.
   PubMed Web of Science ®Google Scholar
• Epstein, E. H., Williams, M. L., Elias, P. M. (1984). The epidermal cholesterol sulfate cycle. J Am Acad Dermatol 10:866–868.
   PubMed Web of Science ®Google Scholar
• Falany, C. N., Comer, K. A., Dooley, T. P., Glatt, H. (1995a). Human dehydroepiandrosterone sulfotransferase. Purification, mole-cular cloning, and characterization. Ann N Y Acad Sci 774:59–72.
   PubMed Web of Science ®Google Scholar
• Falany, C. N., He, D., Dumas, N., Frost, A. R., Falany, J. L. (2006). Human cytosolic sulfotransferase 2B1: isoform expression, tissue specificity and subcellular localization. J Steroid Biochem Mol Biol 102:214–221.
   PubMed Web of Science ®Google Scholar
• Falany, C. N., He, D., Li, L., Falany, J. L., Wilborn, T. W., Kocarek, T. A., et al. (2009). Regulation of hepatic sulfotransferase (SULT) 1E1 expression and effects on estrogenic activity in cystic fibrosis (CF). J Steroid Biochem Mol Biol 114:113–119.
   PubMed Web of Science ®Google Scholar
• Falany, C. N., Krasnykh, V., Falany, J. L. (1995b). Bacterial expression and characterization of a cDNA for human liver estrogen sulfotransferase. J Steroid Biochem Mol Biol 52:529–539.
   PubMed Web of Science ®Google Scholar
• Falany, C. N., Vazquez, M. E., Heroux, J. A., Roth, J. A. (1990). Purification and characterization of human liver phenol-sulfating phenol sulfotransferase. Arch Biochem Biophys 278:312–318.
   PubMed Web of Science ®Google Scholar
• Falany, C. N., Vazquez, M. E., Kalb, J. M. (1989). Purification and characterization of human liver dehydroepiandrosterone sulphotransferase. Biochem J 260:641–646.
   PubMed Web of Science ®Google Scholar
• Falany, C. N., Wheeler, J., Oh, T. S., Falany, J. L. (1994). Steroid sulfation by expressed human cytosolic sulfotransferases. J Steroid Biochem Mol Biol 48:369–375.
   PubMed Web of Science ®Google Scholar
• Falany, J. L., Falany, C. N. (1996). Expression of cytosolic sulfotransferases in normal mammary epithelial cells and breast cancer cell lines. Cancer Res 56:1551–1555.
   PubMed Web of Science ®Google Scholar
• Falany, J. L., Greer, H., Kovacs, T., Sorscher, E. J., Falany, C. N. (2002a). Elevation of hepatic sulphotransferase activities in mice with resistance to cystic fibrosis. Biochem J 364:115–120.
   PubMed Web of Science ®Google Scholar
• Falany, J. L., Macrina, N., Falany, C. N. (2002b). Regulation of MCF-7 breast cancer cell growth by beta-estradiol sulfation. Breast Cancer ResTreat 74:167–176.
   PubMed Web of Science ®Google Scholar
• Fan, J., Liu, S., Du, Y., Morrison, J., Shipman, R., Pang, K. S. (2009). Up-regulation of transporters and enzymes by the vitamin D receptor ligands, 1alpha,25-dihydroxyvitamin D3 and vitamin D analogs, in the Caco-2 cell monolayer. J Pharmacol Exp Ther 330:389–402.
   PubMed Web of Science ®Google Scholar
• Fan, L. Q., You, L., Brown-Borg, H., Brown, S., Edwards, R. J., Corton, J. C. (2004). Regulation of phase I and phase II steroid metabolism enzymes by PPAR alpha activators. Toxicology 204:109–121.
   PubMed Web of Science ®Google Scholar
• Fang, H. L., Strom, S. C., Cai, H., Falany, C. N., Kocarek, T. A., Runge-Morris, M. (2005). Regulation of human hepatic hydroxysteroid sulfotransferase gene expression by the peroxisome proliferator-activated receptor alpha transcription factor. Mol Pharmacol 67:1257–1267.
   PubMed Web of Science ®Google Scholar
• Fang, H. L., Strom, S. C., Ellis, E., Duanmu, Z., Fu, J., Duniec-Dmuchowski, Z., et al. (2007). Positive and negative regulation of human hepatic hydroxysteroid sulfotransferase (SULT2A1) gene transcription by rifampicin: roles of hepatocyte nuclear factor 4alpha and pregnane X receptor. J Pharmacol Exp Ther 323:586–598.
   PubMed Web of Science ®Google Scholar
• Forman, B. M., Tzameli, I., Choi, H. S., Chen, J., Simha, D., Seol, W., et al. (1998). Androstane metabolites bind to and deactivate the nuclear receptor CAR-beta. Nature 395:612–615.
   PubMed Web of Science ®Google Scholar
• Frohling, W., Stiehl, A. (1976). Bile salt glucuronides: identification and quantitative analysis in the urine of patients with cholestasis. Eur J Clin Invest 6:67–74.
   PubMed Web of Science ®Google Scholar
• Fuda, H., Javitt, N. B., Mitamura, K., Ikegawa, S., Strott, C. A. (2007). Oxysterols are substrates for cholesterol sulfotransferase. J Lipid Res 48:1343–1352.
   PubMed Web of Science ®Google Scholar
• Fuda, H., Lee, Y. C., Shimizu, C., Javitt, N. B., Strott, C. A. (2002). Mutational analysis of human hydroxysteroid sulfotransferase SULT2B1 isoforms reveals that exon 1B of the SULT2B1 gene produces cholesterol sulfotransferase, whereas exon 1A yields pregnenolone sulfotransferase. J Biol Chem 277:36161–36166.
   PubMed Web of Science ®Google Scholar
• Gamage, N., Barnett, A., Hempel, N., Duggleby, R. G., Windmill, K. F., Martin, J. L., et al. (2006). Human sulfotransferases and their role in chemical metabolism. Toxicol Sci 90:5–22.
   PubMed Web of Science ®Google Scholar
• Gartside, S. E., Griffith, N. C., Kaura, V., Ingram, C. D. (2010). The neurosteroid dehydroepiandrosterone (DHEA) and its metabolites alter 5-HT neuronal activity via modulation of GABAA receptors. J Psychopharmacol 24:1717–1724.
   PubMed Web of Science ®Google Scholar
• Geese, W. J., Raftogianis, R. B. (2001). Biochemical characterization and tissue distribution of human SULT2B1. Biochem Biophys Res Commun 288:280–289.
   PubMed Web of Science ®Google Scholar
• Ghose, R., Omoluabi, O., Gandhi, A., Shah, P., Strohacker, K., Carpenter, K. C., et al. (2011). Role of high-fat diet in regulation of gene expression of drug metabolizing enzymes and transporters. Life Sci 89:57–64.
   PubMed Web of Science ®Google Scholar
• Gibbs, T. T., Russek, S. J., Farb, D. H. (2006). Sulfated steroids as endogenous neuromodulators. Pharmacol Biochem Behav 84:555–567.
   PubMed Web of Science ®Google Scholar
• Giguere, V., Tini, M., Flock, G., Ong, E., Evans, R. M., Otulakowski, G. (1994). Isoform-specific amino-terminal domains dictate DNA-binding properties of ROR alpha, a novel family of orphan hormone nuclear receptors. Genes Dev 8:538–553.
   PubMed Web of Science ®Google Scholar
• Gill, A. M., Leiter, E. H., Powell, J. G., Chapman, H. D., Yen, T. T. (1994). Dexamethasone-induced hyperglycemia in obese Avy/a (viable yellow) female mice entails preferential induction of a hepatic estrogen sulfotransferase. Diabetes 43:999–1004.
   PubMed Web of Science ®Google Scholar
• Gill, S., Chow, R., Brown, A. J. (2008). Sterol regulators of cholesterol homeostasis and beyond: the oxysterol hypothesis revisited and revised. Prog Lipid Res 47:391–404.
   PubMed Web of Science ®Google Scholar
• Glatt, H., Boeing, H., Engelke, C. E., Ma, L., Kuhlow, A., Pabel, U., et al. (2001). Human cytosolic sulphotransferases: genetics, characteristics, toxicological aspects. Mutat Res 482:27–40.
   PubMed Web of Science ®Google Scholar
• Gong, H., Guo, P., Zhai, Y., Zhou, J., Uppal, H., Jarzynka, M. J., et al. (2007). Estrogen deprivation and inhibition of breast cancer growth in vivo through activation of the orphan nuclear receptor liver X receptor. Mol Endocrinol 21:1781–1790.
   PubMed Web of Science ®Google Scholar
• Gooderham, N. J., Murray, S., Lynch, A. M., Yadollahi-Farsani, M., Zhao, K., Boobis, A. R., et al. (2001). Food-derived heterocyclic amine mutagens: variable metabolism and significance to humans. Drug Metab Dispos 29:529–534.
   PubMed Web of Science ®Google Scholar
• Greschik, H., Wurtz, J. M., Sanglier, S., Bourguet, W., van Dorsselaer, A., Moras, D., et al. (2002). Structural and functional evidence for ligand-independent transcriptional activation by the estrogen-related receptor 3. Mol Cell 9:303–313.
   PubMed Web of Science ®Google Scholar
• He, D., Falany, C. N. (2006). Characterization of proline-serine-rich carboxyl terminus in human sulfotransferase 2B1b: immunogenicity, subcellular localization, kinetic properties, and phosphorylation. Drug Metab Dispos 34:1749–1755.
   PubMed Web of Science ®Google Scholar
• He, D., Falany, C. N. (2007). Inhibition of SULT2B1b expression alters effects of 3beta-hydroxysteroids on cell proliferation and steroid hormone receptor expression in human LNCaP prostate cancer cells. Prostate 67:1318–1329.
   PubMed Web of Science ®Google Scholar
• He, D., Wilborn, T. W., Falany, J. L., Li, L., Falany, C. N. (2008). Repression of CFTR activity in human MMNK-1 cholangiocytes induces sulfotransferase 1E1 expression in co-cultured HepG2 hepatocytes. Biochim Biophys Acta 1783:2391–2397.
   PubMed Web of Science ®Google Scholar
• Her, C., Szumlanski, C., Aksoy, I. A., Weinshilboum, R. M. (1996). Human jejunal estrogen sulfotransferase and dehydroepiandrosterone sulfotransferase: immunochemical characterization of individual variation. Drug Metab Dispos 24:1328–1335.
   PubMed Web of Science ®Google Scholar
• Her, C., Wood, T. C., Eichler, E. E., Mohrenweiser, H. W., Ramagli, L. S., Siciliano, M. J., et al. (1998). Human hydroxysteroid sulfotransferase SULT2B1: two enzymes encoded by a single chromosome 19 gene. Genomics 53:284–295.
   PubMed Web of Science ®Google Scholar
• Higashi, Y., Fuda, H., Yanai, H., Lee, Y., Fukushige, T., Kanzaki, T., et al. (2004). Expression of cholesterol sulfotransferase (SULT2B1b) in human skin and primary cultures of human epidermal keratinocytes. J Invest Dermatol 122:1207–1213.
   PubMed Web of Science ®Google Scholar
• Honkakoski, P., Zelko, I., Sueyoshi, T., Negishi, M. (1998). The nuclear orphan receptor CAR-retinoid X receptor heterodimer activates the phenobarbital-responsive enhancer module of the CYP2B gene. Mol Cell Biol 18:5652–5658.
   PubMed Web of Science ®Google Scholar
• Huang, C., Zhou, T., Chen, Y., Sun, T., Zhang, S., Chen, G. (2011). Estrogen-related receptor ERRalpha-mediated downregulation of human hydroxysteroid sulfotransferase (SULT2A1) in Hep G2 cells. Chem Biol Interact 192:264–271.
   PubMed Web of Science ®Google Scholar
• Jancova, P., Anzenbacher, P., Anzenbacherova, E. (2010). Phase II drug metabolizing enzymes. Biomed Pap Med Fac Univ Palacky Olomouc Czech Repub 154:103–116.
   PubMed Web of Science ®Google Scholar
• Janowski, B. A., Grogan, M. J., Jones, S. A., Wisely, G. B., Kliewer, S. A., Corey, E. J., et al. (1999). Structural requirements of ligands for the oxysterol liver X receptors LXRalpha and LXRbeta. Proc Natl Acad Sci U S A 96:266–271.
   PubMed Web of Science ®Google Scholar
• Jetten, A. M., Kurebayashi, S., Ueda, E. (2001). The ROR nuclear orphan receptor subfamily: critical regulators of multiple biological processes. Prog Nucleic Acid Res Mol Biol 69:205–247.
   PubMed Web of Science ®Google Scholar
• Jiang, Y. J., Kim, P., Elias, P. M., Feingold, K. R. (2005). LXR and PPAR activators stimulate cholesterol sulfotransferase type 2 isoform 1b in human keratinocytes. J Lipid Res 46:2657–2666.
   PubMed Web of Science ®Google Scholar
• Johnston, S. D., Liu, X., Zuo, F., Eisenbraun, T. L., Wiley, S. R., Kraus, R. J., et al. (1997). Estrogen-related receptor alpha 1 functionally binds as a monomer to extended half-site sequences including ones contained within estrogen-response elements. Mol Endocrinol 11:342–352.
   PubMed Web of Science ®Google Scholar
• Kachaylo, E. M., Pustylnyak, V. O., Lyakhovich, V. V., Gulyaeva, L. F. (2011). Constitutive androstane receptor (CAR) is a xenosensor and target for therapy. Biochemistry (Mosc.) 76:1087–1097.
   PubMed Web of Science ®Google Scholar
• Kallen, J., Schlaeppi, J. M., Bitsch, F., Delhon, I., Fournier, B. (2004). Crystal structure of the human RORalpha Ligand binding domain in complex with cholesterol sulfate at 2.2 A. J Biol Chem 279:14033–14038.
   PubMed Web of Science ®Google Scholar
• Kallen, J. A., Schlaeppi, J. M., Bitsch, F., Geisse, S., Geiser, M., Delhon, I., et al. (2002). X-ray structure of the hRORalpha LBD at 1.63 A: structural and functional data that cholesterol or a cholesterol derivative is the natural ligand of RORalpha. Structure 10:1697–1707.
   PubMed Web of Science ®Google Scholar
• Kang, H. S., Angers, M., Beak, J. Y., Wu, X., Gimble, J. M., Wada, T., et al. (2007). Gene expression profiling reveals a regulatory role for ROR alpha and ROR gamma in phase I and phase II metabolism. Physiol Genomics 31:281–294.
   PubMed Web of Science ®Google Scholar
• Kashiwagi, M., Ohba, M., Chida, K., Kuroki, T. (2002). Protein kinase C eta (PKC eta): its involvement in keratinocyte differentiation. J Biochem 132:853–857.
   PubMed Web of Science ®Google Scholar
• Khor, V. K., Dhir, R., Yin, X., Ahima, R. S., Song, W. C. (2010). Estrogen sulfotransferase regulates body fat and glucose homeostasis in female mice. Am J Physiol Endocrinol Metab 299:E657–E664.
   PubMed Web of Science ®Google Scholar
• Kim, M. S., Shigenaga, J., Moser, A., Grunfeld, C., Feingold, K. R. (2004). Suppression of DHEA sulfotransferase (Sult2A1) during the acute-phase response. Am J Physiol Endocrinol Metab 287:E731–E738.
   PubMed Web of Science ®Google Scholar
• Kitada, H., Miyata, M., Nakamura, T., Tozawa, A., Honma, W., Shimada, M., et al. (2003). Protective role of hydroxysteroid sulfotransferase in lithocholic acid-induced liver toxicity. J Biol Chem 278:17838–17844.
   PubMed Web of Science ®Google Scholar
• Kliewer, S. A., Moore, J. T., Wade, L., Staudinger, J. L., Watson, M. A., Jones, S. A., et al. (1998). An orphan nuclear receptor activated by pregnanes defines a novel steroid signaling pathway. Cell 92:73–82.
   PubMed Web of Science ®Google Scholar
• Kocarek, T. A., Duanmu, Z., Fang, H. L., Runge-Morris, M. (2008). Age- and sex-dependent expression of multiple murine hepatic hydroxysteroid sulfotransferase (SULT2A) genes. Biochem Pharmacol 76:1036–1046.
   PubMed Web of Science ®Google Scholar
• Kodama, S., Hosseinpour, F., Goldstein, J. A., Negishi, M. (2011). Liganded pregnane X receptor represses the human sulfotransferase SULT1E1 promoter through disrupting its chromatin structure. Nucleic Acids Res 39:8392–8403.
   PubMed Web of Science ®Google Scholar
• Kohjitani, A., Fuda, H., Hanyu, O., Strott, C. A. (2006). Cloning, characterization, and tissue expression of rat SULT2B1a and SULT2B1b steroid/sterol sulfotransferase isoforms: divergence of the rat SULT2B1 gene structure from orthologous human and mouse genes. Gene 367:66–73.
   PubMed Web of Science ®Google Scholar
• Kotov, A., Falany, J. L., Wang, J., Falany, C. N. (1999). Regulation of estrogen activity by sulfation in human Ishikawa endometrial adenocarcinoma cells. J Steroid Biochem Mol Biol 68:137–144.
   PubMed Web of Science ®Google Scholar
• Kushida, A., Hattori, K., Yamaguchi, N., Kobayashi, T., Date, A., Tamura, H. (2011). Sulfation of estradiol in human epidermal keratinocyte. Biol Pharm Bull 34:1147–1151.
   PubMed Web of Science ®Google Scholar
• Lampe, M. A., Williams, M. L., Elias, P. M. (1983). Human epidermal lipids: characterization and modulations during differentiation. J Lipid Res 24:131–140.
   PubMed Web of Science ®Google Scholar
• Lau, P., Fitzsimmons, R. L., Raichur, S., Wang, S. C., Lechtken, A., Muscat, G. E. (2008). The orphan nuclear receptor, RORalpha, regulates gene expression that controls lipid metabolism: staggerer (SG/SG) mice are resistant to diet-induced obesity. J Biol Chem 283:18411–18421.
   PubMed Web of Science ®Google Scholar
• Lee, J. H., Gong, H., Khadem, S., Lu, Y., Gao, X., Li, S., et al. (2008). Androgen deprivation by activating the liver X receptor. Endocrinology 149:3778–3788.
   PubMed Web of Science ®Google Scholar
• Lee, K. A., Fuda, H., Lee, Y. C., Negishi, M., Strott, C. A., Pedersen, L. C. (2003). Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3′-phosphoadenosine 5′-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms. J Biol Chem 278:44593–44599.
   PubMed Web of Science ®Google Scholar
• Lehmann, J. M., McKee, D. D., Watson, M. A., Willson, T. M., Moore, J. T., Kliewer, S. A. (1998). The human orphan nuclear receptor PXR is activated by compounds that regulate CYP3A4 gene expression and cause drug interactions. J Clin Invest 102:1016–1023.
   PubMed Web of Science ®Google Scholar
• Leiter, E. H., Chapman, H. D. (1994). Obesity-induced diabetes (diabesity) in C57BL/KsJ mice produces aberrant trans-regulation of sex steroid sulfotransferase genes. J Clin Invest 93:2007–2013.
   PubMed Web of Science ®Google Scholar
• Lewis, A. J., Walle, U. K., King, R. S., Kadlubar, F. F., Falany, C. N., Walle, T. (1998). Bioactivation of the cooked food mutagen N-hydroxy-2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine by estrogen sulfotransferase in cultured human mammary epithelial cells. Carcinogenesis 19:2049–2053.
   PubMed Web of Science ®Google Scholar
• Li, L., He, D., Wilborn, T. W., Falany, J. L., Falany, C. N. (2009). Increased SULT1E1 activity in HepG2 hepatocytes decreases growth hormone stimulation of STAT5b phosphorylation. Steroids 74:20–29.
   PubMed Web of Science ®Google Scholar
• Liyou, N. E., Buller, K. M., Tresillian, M. J., Elvin, C. M., Scott, H. L., Dodd, P. R., et al. (2003). Localization of a brain sulfotransferase, SULT4A1, in the human and rat brain: an immunohistochemical study. J Histochem Cytochem 51:1655–1664.
   PubMed Web of Science ®Google Scholar
• Luchetti, S., Bossers, K., Frajese, G. V., Swaab, D. F. (2010). Neurosteroid biosynthetic pathway changes in substantia nigra and caudate nucleus in Parkinson’s disease. Brain Pathol 20:945–951.
   PubMed Web of Science ®Google Scholar
• Makino, I., Hashimoto, H., Shinozaki, K., Yoshino, K., Nakagawa, S (1975). Sulfated and nonsulfated bile acids in urine, serum, and bile of patients with hepatobiliary diseases. Gastroenterology 68:545–553.
   PubMed Web of Science ®Google Scholar
• Makino, I., Shinozaki, K., Nakagawa, S., Mashimo, K. (1974). Measurement of sulfated and nonsulfated bile acids in human serum and urine. J Lipid Res 15:132–138.
   PubMed Web of Science ®Google Scholar
• Makishima, M., Lu, T. T., Xie, W., Whitfield, G. K., Domoto, H., Evans, R. M., et al. (2002). Vitamin D receptor as an intestinal bile acid sensor. Science 296:1313–1316.
   PubMed Web of Science ®Google Scholar
• Matsubara, T., Li, F., Gonzalez, F. J. (2012). FXR signaling in the enterohepatic system. Mol Cell Endocrinol May 17. [Epub ahead of print].
   PubMed Web of Science ®Google Scholar
• Meinl, W., Glatt, H. (2001). Structure and localization of the human SULT1B1 gene: neighborhood to SULT1E1 and a SULT1D pseudogene. Biochem Biophys Res Commun 288:855–862.
   PubMed Web of Science ®Google Scholar
• Meloche, C. A., Falany, C. N. (2001). Expression and characterization of the human 3 beta-hydroxysteroid sulfotransferases (SULT2B1a and SULT2B1b). J Steroid Biochem Mol Biol 77:261–269.
   PubMed Web of Science ®Google Scholar
• Miyata, M., Matsuda, Y., Tsuchiya, H., Kitada, H., Akase, T., Shimada, M., et al. (2006a). Chenodeoxycholic acid-mediated activation of the farnesoid X receptor negatively regulates hydroxysteroid sulfotransferase. Drug Metab Pharmacokinet 21:315–323.
   PubMed Web of Science ®Google Scholar
• Miyata, M., Watase, H., Hori, W., Shimada, M., Nagata, K., Gonzalez, F. J., et al. (2006b). Role for enhanced faecal excretion of bile acid in hydroxysteroid sulfotransferase-mediated protection against lithocholic acid-induced liver toxicity. Xenobiotica 36:631–644.
   PubMed Web of Science ®Google Scholar
• Nagata, K., Shimada, M., Yamazoe, Y (2005). Species differences in cytosolic sulfotransferases. In: Pacifici, G. M., Coughtrie, M. W. H. (Eds.), Human cytosolic sUlfotransferases (pp. 253–278). Boca Raton, Florida, USA: Taylor & Francis.
   Google Scholar
• Nagata, K., Yamazoe, Y (2000). Pharmacogenetics of sulfotransferase. Annu Rev Pharmacol Toxicol 40:159–176.
   PubMed Web of Science ®Google Scholar
• Nakamura, Y., Suzuki, T., Fukuda, T., Ito, A., Endo, M., Moriya, T., et al. (2006). Steroid sulfatase and estrogen sulfotransferase in human prostate cancer. Prostate 66:1005–1012.
   PubMed Web of Science ®Google Scholar
• Nelissen, K., Mulder, M., Smets, I., Timmermans, S., Smeets, K., Ameloot, M., et al. (2012). Liver X receptors regulate cholesterol homeostasis in oligodendrocytes. J Neurosci Res 90:60–71.
   PubMed Web of Science ®Google Scholar
• Ngan, C. H., Beglov, D., Rudnitskaya, A. N., Kozakov, D., Waxman, D. J., Vajda, S. (2009). The structural basis of pregnane X receptor binding promiscuity. Biochemistry 48:11572–11581.
   PubMed Web of Science ®Google Scholar
• Nilsson, E., de la Torre, B., Hedman, M., Goobar, J., Thorner, A. (1994). Blood dehydroepiandrosterone sulphate (DHEAS) levels in polymyalgia rheumatica/giant cell arteritis and primary fibromyalgia. Clin Exp Rheumatol 12:415–417.
   PubMed Web of Science ®Google Scholar
• Owen, B. M., Milona, A., van Mil, S., Clements, P., Holder, J., Boudjelal, M., et al. (2010). Intestinal detoxification limits the activation of hepatic pregnane X receptor by lithocholic acid. Drug Metab Dispos 38:143–149.
   PubMed Web of Science ®Google Scholar
• Pakharukova, M., Smetanina, M., Kaledin, V., Obut, T., Merkulova, T. (2010). The increased CAR-dependent metabolism of thyroid hormones in mice with high cancer susceptibility. Life Sci 87:439–444.
   PubMed Web of Science ®Google Scholar
• Peeters, R. P., Kester, M. H., Wouters, P. J., Kaptein, E., van Toor, H., Visser, T. J., et al. (2005). Increased thyroxine sulfate levels in critically ill patients as a result of a decreased hepatic type I deiodinase activity. J Clin Endocrinol Metab 90:6460–6465.
   PubMed Web of Science ®Google Scholar
• Qian, Y. M., Sun, X. J., Tong, M. H., Li, X. P., Richa, J., Song, W. C. (2001). Targeted disruption of the mouse estrogen sulfotransferase gene reveals a role of estrogen metabolism in intracrine and paracrine estrogen regulation. Endocrinolog, 142:5342–5350.
   PubMed Web of Science ®Google Scholar
• Radominska, A., Comer, K. A., Zimniak, P., Falany, J., Iscan, M., Falany, C. N. (1990). Human liver steroid sulphotransferase sulphates bile acids. Biochem J 272:597–604.
   PubMed Web of Science ®Google Scholar
• Radovic, B., Hussong, R., Gerhauser, C., Meinl, W., Frank, N., Becker, H., et al. (2010). Xanthohumol, a prenylated chalcone from hops, modulates hepatic expression of genes involved in thyroid hormone distribution and metabolism. Mol Nutr Food Res 54(Suppl 2):S225–S235.
   PubMed Web of Science ®Google Scholar
• Rainey, W. E., Carr, B. R., Sasano, H., Suzuki, T., Mason, J. I. (2002). Dissecting human adrenal androgen production. Trends Endocrinol Metab 13:234–239.
   PubMed Web of Science ®Google Scholar
• Riches, Z., Stanley, E. L., Bloomer, J. C., Coughtrie, M. W. (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.
   PubMed Web of Science ®Google Scholar
• Robinson, E., Grieve, D. J. (2009). Significance of peroxisome proliferator-activated receptors in the cardiovascular system in health and disease. Pharmacol Ther 122:246–263.
   PubMed Web of Science ®Google Scholar
• Runge-Morris, M., Kocarek, T. A. (2009). Regulation of sulfotransferase and UDP-glucuronosyltransferase gene expression by the PPARs. PPAR Res 2009:728941.
   PubMedGoogle Scholar
• Rutgers, M., Heusdens, F. A., Visser, T. J. (1991). Deiodination of iodothyronine sulfamates by type I iodothyronine deiodinase of rat liver. Endocrinology 129:1375–1381.
   PubMed Web of Science ®Google Scholar
• Saini, S. P., Sonoda, J., Xu, L., Toma, D., Uppal, H., Mu, Y., et al. (2004). A novel constitutive androstane receptor-mediated and CYP3A-independent pathway of bile acid detoxification. Mol Pharmacol 65:292–300.
   PubMed Web of Science ®Google Scholar
• Sakakibara, Y., Yanagisawa, K., Katafuchi, J., Ringer, D. P., Takami, Y., Nakayama, T., et al. (1998). Molecular cloning, expression, and characterization of novel human SULT1C sulfotransferases that catalyze the sulfonation of N-hydroxy-2-acetylaminofluorene. J Biol Chem 273:33929–33935.
   PubMed Web of Science ®Google Scholar
• Salman, E. D., Faye-Peterson, O., Falany, C. N. (2011a). Hydroxysteroid sulfotransferase 2B1b expression and localization in normal human brain. Hormone Mol Biol Clin Invest 8:445–454.
   Google Scholar
• Salman, E. D., He, D., Runge-Morris, M., Kocarek, T. A., Falany, C. N. (2011b). Site-directed mutagenesis of human cytosolic sulfotransferase (SULT) 2B1b to phospho-mimetic Ser348Asp results in an isoform with increased catalytic activity. J Steroid Biochem Mol Biol 127:315–323.
   PubMed Web of Science ®Google Scholar
• Sankpal, U. T., Pius, H., Khan, M., Shukoor, M. I., Maliakal, P., Lee, C. M., et al. (2012). Environmental factors in causing human cancers: emphasis on tumorigenesis. Tumour Biol 33:1265–1274.
   PubMedGoogle Scholar
• Seely, J., Amigh, K. S., Suzuki, T., Mayhew, B., Sasano, H., Giguere, V., et al. (2005). Transcriptional regulation of dehydroepiandrosterone sulfotransferase (SULT2A1) by estrogen-related receptor alpha. Endocrinology 146:3605–3613.
   PubMed Web of Science ®Google Scholar
• Shimizu, C., Fuda, H., Yanai, H., Strott, C. A. (2003). Conservation of the hydroxysteroid sulfotransferase SULT2B1 gene structure in the mouse: pre- and postnatal expression, kinetic analysis of isoforms, and comparison with prototypical SULT2A1. Endocrinology 144:1186–1193.
   PubMed Web of Science ®Google Scholar
• Shiraki, T., Kamiya, N., Shiki, S., Kodama, T. S., Kakizuka, A., Jingami, H. (2005). Alpha,beta-unsaturated ketone is a core moiety of natural ligands for covalent binding to peroxisome proliferator-activated receptor gamma. J Biol Chem 280:14145–14153.
   PubMed Web of Science ®Google Scholar
• Shoda, J., Tanaka, N., Osuga, T., Matsuura, K., Miyazaki, H. (1990). Altered bile acid metabolism in liver disease: concurrent occurrence of C-1 and C-6 hydroxylated bile acid metabolites and their preferential excretion into urine. J Lipid Res 31:249–259.
   PubMed Web of Science ®Google Scholar
• Song, C. S., Echchgadda, I., Baek, B. S., Ahn, S. C., Oh, T., Roy, A. K., et al. (2001). Dehydroepiandrosterone sulfotransferase gene induction by bile acid activated farnesoid X receptor. J Biol Chem 276:42549–42556.
   PubMed Web of Science ®Google Scholar
• Song, C. S., Echchgadda, I., Seo, Y. K., Oh, T., Kim, S., Kim, S. A., et al. (2006). An essential role of the CAAT/enhancer binding protein-alpha in the vitamin D-induced expression of the human steroid/bile acid-sulfotransferase (SULT2A1). Mol Endocrinol 20:795–808.
   PubMed Web of Science ®Google Scholar
• Song, C. S., Jung, M. H., Kim, S. C., Hassan, T., Roy, A. K., Chatterjee, B. (1998). Tissue-specific and androgen-repressible regulation of the rat dehydroepiandrosterone sulfotransferase gene promoter. J Biol Chem 273:21856–21866.
   PubMed Web of Science ®Google Scholar
• Spaulding, S. W., Smith, T. J., Hinkle, P. M., Davis, F. B., Kung, M. P., Roth, J. A. (1992). Studies on the biological activity of triiodothyronine sulfate. J Clin Endocrinol Metab 74:1062–1067.
   PubMed Web of Science ®Google Scholar
• Spiegelman, B. M., Hu, E., Kim, J. B., Brun, R. (1997). PPAR gamma and the control of adipogenesis. Biochimie 79:111–112.
   PubMed Web of Science ®Google Scholar
• Staudinger, J. L., Goodwin, B., Jones, S. A., Hawkins-Brown, D., MacKenzie, K. I., LaTour, A., et al. (2001). The nuclear receptor PXR is a lithocholic acid sensor that protects against liver toxicity. Proc Natl Acad Sci U S A 98:3369–3374.
   PubMed Web of Science ®Google Scholar
• Stehlin-Gaon, C., Willmann, D., Zeyer, D., Sanglier, S., Van Dorrselaer, A., Renaud, J. P., et al. (2003). All-trans retinoic acid is a ligand for the orphan nuclear receptor ROR beta. Nat Struct Biol 10:820–825.
   PubMedGoogle Scholar
• Stiehl, A., Becker, M., Czygan, P., Frohling, W., Kommerell, B., Rotthauwe, H. W., et al. (1980). Bile acids and their sulphated and glucuronidated derivatives in bile, plasma, and urine of children with intrahepatic cholestasis: effects of phenobarbital treatment. Eur J Clin Invest 10:307–316.
   PubMed Web of Science ®Google Scholar
• Strassburg, C. P., Strassburg, A., Kneip, S., Barut, A., Tukey, R. H., Rodeck, B., et al. (2002). Developmental aspects of human hepatic drug glucuronidation in young children and adults. Gut 50:259–265.
   PubMed Web of Science ®Google Scholar
• Strott, C. A. (2002). Sulfonation and molecular action. Endocr Rev 23:703–732.
   PubMed Web of Science ®Google Scholar
• Strott, C. A., Higashi, Y. (2003). Cholesterol sulfate in human physiology: what’s it all about? J Lipid Res 44:1268–1278.
   PubMed Web of Science ®Google Scholar
• Sueyoshi, T., Green, W. D., Vinal, K., Woodrum, T. S., Moore, R., Negishi, M. (2011). Garlic extract diallyl sulfide (DAS) activates nuclear receptor CAR to induce the Sult1e1 gene in mouse liver. PLoS One 6:e21229.
   PubMed Web of Science ®Google Scholar
• Sueyoshi, T., Kawamoto, T., Zelko, I., Honkakoski, P., Negishi, M. (1999). The repressed nuclear receptor CAR responds to phenobarbital in activating the human CYP2B6 gene. J Biol Chem 274:6043–6046.
   PubMed Web of Science ®Google Scholar
• Suzuki, T., Miki, Y., Nakamura, Y., Ito, K., Sasano, H. (2011). Steroid sulfatase and estrogen sulfotransferase in human carcinomas. Mol Cell Endocrinol 340:148–153.
   PubMed Web of Science ®Google Scholar
• Takahashi, S., Sakakibara, Y., Mishiro, E., Kouriki, H., Nobe, R., Kurogi, K., et al. (2009). Molecular cloning, expression and characterization of a novel mouse SULT6 cytosolic sulfotransferase. J Biochem 146:399–405.
   PubMed Web of Science ®Google Scholar
• Tanaka, H., Leung, P. S., Kenny, T. P., Gershwin, M. E., Bowlus, C. L. (2012). Immunological orchestration of liver fibrosis. Clin Rev Allergy Immunol 43:220–229.
   PubMed Web of Science ®Google Scholar
• Tashiro, A, Sasano, H, Nishikawa, T, Yabuki, N, Muramatsu, Y, Coughtrie, MW, et al. (2000). Expression and activity of dehydroepiandrosterone sulfotransferase in human gastric mucosa. J Steroid Biochem Mol Biol 72:149–154.
   PubMed Web of Science ®Google Scholar
• Tremblay, G. B., Kunath, T., Bergeron, D., Lapointe, L., Champigny, C., Bader, J. A., et al. (2001). Diethylstilbestrol regulates trophoblast stem cell differentiation as a ligand of orphan nuclear receptor ERR beta. Genes Dev 15:833–838.
   PubMed Web of Science ®Google Scholar
• Tsoi, C., Falany, C. N., Morgenstern, R., Swedmark, S. (2001). Identification of a new subfamily of sulphotransferases: cloning and characterization of canine SULT1D1. Biochem J 356:891–897.
   PubMed Web of Science ®Google Scholar
• Uppal, H., Saini, S. P., Moschetta, A., Mu, Y., Zhou, J., Gong, H., et al. (2007). Activation of LXRs prevents bile acid toxicity and cholestasis in female mice. Hepatology 45:422–432.
   PubMed Web of Science ®Google Scholar
• Vanacker, J. M., Bonnelye, E., Chopin-Delannoy, S., Delmarre, C., Cavailles, V., Laudet, V. (1999). Transcriptional activities of the orphan nuclear receptor ERR alpha (estrogen receptor-related receptor-alpha). Mol Endocrinol 13:764–773.
   PubMed Web of Science ®Google Scholar
• Visser, T. J. (1996). Pathways of thyroid hormone metabolism. Acta Med Austriaca 23:10–16.
   PubMedGoogle Scholar
• Wang, Y., Kumar, N., Solt, L. A., Richardson, T. I., Helvering, L. M., Crumbley, C., et al. (2010). Modulation of retinoic acid receptor-related orphan receptor alpha and gamma activity by 7-oxygenated sterol ligands. J Biol Chem 285:5013–5025.
   PubMed Web of Science ®Google Scholar
• Watkins, R. E., Wisely, G. B., Moore, L. B., Collins, J. L., Lambert, M. H., Williams, S. P., et al. (2001). The human nuclear xenobiotic receptor PXR: structural determinants of directed promiscuity. Science 292:2329–2333.
   PubMed Web of Science ®Google Scholar
• Waxman, D. J., Holloway, M. G. (2009). Sex differences in the expression of hepatic drug metabolizing enzymes. Mol Pharmacol 76:215–228.
   PubMed Web of Science ®Google Scholar
• Willson, T. M., Jones, S. A., Moore, J. T., Kliewer, S. A. (2001). Chemical genomics: functional analysis of orphan nuclear receptors in the regulation of bile acid metabolism. Med Res Rev 21:513–522.
   PubMed Web of Science ®Google Scholar
• Willy, P. J., Murray, I. R., Qian, J., Busch, B. B., Stevens, W. C., Jr., Martin, R., et al. (2004). Regulation of PPARgamma coactivator 1alpha (PGC-1alpha) signaling by an estrogen-related receptor alpha (ERRalpha) ligand. Proc Natl Acad Sci U S A 101:8912–8917.
   PubMed Web of Science ®Google Scholar
• Wong, J., Quinn, C. M., Gelissen, I. C., Brown, A. J. (2008). Endogenous 24(S),25-epoxycholesterol fine-tunes acute control of cellular cholesterol homeostasis. J Biol Chem 283:700–707.
   PubMed Web of Science ®Google Scholar
• Wyde, M. E., Kirwan, S. E., Zhang, F., Laughter, A., Hoffman, H. B., Bartolucci-Page, E., et al. (2005). Di-n-butyl phthalate activates constitutive androstane receptor and pregnane X receptor and enhances the expression of steroid-metabolizing enzymes in the liver of rat fetuses. Toxicol Sci 86:281–290.
   PubMed Web of Science ®Google Scholar
• Xie, W., Barwick, J. L., Downes, M., Blumberg, B., Simon, C. M., Nelson, M. C., et al. (2000). Humanized xenobiotic response in mice expressing nuclear receptor SXR. Nature 406:435–439.
   PubMed Web of Science ®Google Scholar
• Xu, L., Bai, Q., Rodriguez-Agudo, D., Hylemon, P. B., Heuman, D. M., Pandak, W. M., et al. (2010). Regulation of hepatocyte lipid metabolism and inflammatory response by 25-hydroxycholesterol and 25-hydroxycholesterol-3-sulfate. Lipids 45:821–832.
   PubMed Web of Science ®Google Scholar
• Yanagiba, Y., Ito, Y., Kamijima, M., Gonzalez, F. J., Nakajima, T. (2009). Octachlorostyrene induces cytochrome P450, UDP-glucuronosyltransferase, and sulfotransferase via the aryl hydrocarbon receptor and constitutive androstane receptor. Toxicol Sci 111:19–26.
   PubMed Web of Science ®Google Scholar
• Yang, C., McDonald, J. G., Patel, A., Zhang, Y., Umetani, M., Xu, F., et al. (2006). Sterol intermediates from cholesterol biosynthetic pathway as liver X receptor ligands. J Biol Chem 281:27816–27826.
   PubMed Web of Science ®Google Scholar
• Yin, L., Ma, H., Ge, X., Edwards, P. A., Zhang, Y. (2011). Hepatic hepatocyte nuclear factor 4alpha is essential for maintaining triglyceride and cholesterol homeostasis. Arterioscler Thromb Vasc Biol 31:328–336.
   PubMed Web of Science ®Google Scholar
• Zadjali, F., Santana-Farre, R., Mirecki-Garrido, M., Ellis, E., Norstedt, G., Fernandez-Perez, L., et al. (2011). Liver X receptor agonist downregulates growth hormone signaling in the liver. Hormone Mol Biol Clin Invest 8:471–478.
   Google Scholar
• Zhang, H., Varmalova, O., Vargas, F. M., Falany, C. N., Leyh, T. S. (1998). Sulfuryl transfer: the catalytic mechanism of human estrogen sulfotransferase. J Biol Chem 273:10888–10892.
   PubMed Web of Science ®Google Scholar
• Zheng, P. (2009). Neuroactive steroid regulation of neurotransmitter release in the CNS: action, mechanism, and possible significance. Prog Neurobiol 89:134–152.
   PubMed Web of Science ®Google Scholar
• Zollner, G., Wagner, M., Fickert, P., Silbert, D., Gumhold, J., Zatloukal, K., et al. (2007). Expression of bile acid synthesis and detoxification enzymes and the alternative bile acid efflux pump MRP4 in patients with primary biliary cirrhosis. Liver Int 27:920–929.
   PubMed Web of Science ®Google Scholar