SULT2B1: unique properties and characteristics of a hydroxysteroid sulfotransferase family

References

• Alnouti Y, Klaassen CD. (2006). Tissue distribution and ontogeny of sulfotransferase enzymes in mice. Toxicol Sci 93:242–255
   PubMed Web of Science ®Google Scholar
• Bai Q, Xu L, Kakiyama G, et al. (2011). Sulfation of 25-hydroxycholesterol by SULT2B1b decreases cellular lipids via the LXR/SREBP-1c signaling pathway in human aortic endothelial cells. Atherosclerosis 214:350–356
   PubMed Web of Science ®Google Scholar
• Bai Q, Zhang X, Xu L, 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
• Baulieu EE, Robel P, Schumacher M. (2001). Neurosteroids: Beginning of the story. Int Rev Neurobiol 46:1–32
   PubMed Web of Science ®Google Scholar
• Beltowski J. (2008). Liver X receptors (LXR) as therapeutic targets in dyslipidemia. Cardiovasc Ther 26:297–316
   PubMed Web of Science ®Google Scholar
• Bieche I, Lerebours F, Tozlu S, et al. (2004). Molecular profiling of inflammatory breast cancer: Identification of a poor-prognosis gene expression signature. Clin Cancer Res 10:6789–6795
   PubMed Web of Science ®Google Scholar
• Bjorkhem I. (2013). Five decades with oxysterols. Biochimie 95:448–454
   PubMed Web of Science ®Google Scholar
• Blanchard RL, Freimuth RR, Buck J, et al. (2004). A proposed nomenclature system for the cytosolic sulfotransferase (SULT) superfamily. Pharmacogenetics 14:199–211
   PubMedGoogle Scholar
• Chen W, Chen G, Head DL, et al. (2007). Enzymatic reduction of oxysterols impairs LXR signaling in cultured cells and the livers of mice. Cell Metab 5:73–79
   PubMed Web of Science ®Google Scholar
• Chen Y, Chen X, Zhang S, et al. (2011). Influenza A virus infection activates cholesterol sulfotransferase (SULT2B1b) in the lung of female C57BL/6 mice. Biol Chem 392:869–876
   PubMed Web of Science ®Google Scholar
• Comer KA, Falany CN. (1992). Immunological characterization of dehydroepiandrosterone sulfotransferase from human liver and adrenal. Mol Pharmacol 41:645–651
   PubMed Web of Science ®Google Scholar
• Cook I, Wang T, Falany CN, et al. (2012). A nucleotide-gated molecular pore selects sulfotransferase substrates. Biochemistry 51:5674–5683
   PubMed Web of Science ®Google Scholar
• Cook IT, Duniec-Dmuchowski Z, Kocarek TA, et al. (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
• Cook IT, Leyh TS, Kadlubar SA, et al. (2010a). Lack of substrate inhibition in a monomeric form of human cytosolic SULT2A1. Horm Mol Biol Clin Investig 3:357–366
   Google Scholar
• Cook IT, Leyh TS, Kadlubar SA, et al. (2010b). Structural rearrangement of SULT2A1: Effects on dehydroepiandrosterone and raloxifene sulfation. Horm Mol Biol Clin Investig 1:81–87
   PubMedGoogle Scholar
• Dharia S, Slane A, Jian M, et al. (2004). Colocalization of P450c17 and cytochrome b5 in androgen-synthesizing tissues of the human. Biol Reprod 71:83–88
   PubMed Web of Science ®Google Scholar
• Dumas NA, He D, Frost AR, et al. (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
• Falany CN. (1997a). Enzymology of human cytosolic sulfotransferases. FASEB J 11:206–216
   PubMed Web of Science ®Google Scholar
• Falany CN. (1997b). Sulfation and sulfotransferases. Introduction: Changing view of sulfation and the cytosolic sulfotransferases. FASEB J 11:1–2
   PubMed Web of Science ®Google Scholar
• Falany CN, He D, Dumas N, et al. (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 CN, Vazquez ME, Kalb JM. (1989). Purification and characterization of human liver dehydroepiandrosterone sulphotransferase. Biochem J 260:641–646
   PubMed Web of Science ®Google Scholar
• Falany CN, Wheeler J, Oh TS, et al. (1994). Steroid sulfation by expressed human cytosolic sulfotransferases. J Steroid Biochem Mol Biol 48:369–375
   PubMed Web of Science ®Google Scholar
• Falany JL, Macrina N, Falany CN. (2004). Sulfation of tibolone and tibolone metabolites by expressed human cytosolic sulfotransferases. J Steroid Biochem Mol Biol 88:383–391
   PubMed Web of Science ®Google Scholar
• Forbes KJ, Hagen M, Glatt H, et al. (1995). Human fetal adrenal hydroxysteroid sulphotransferase: CDNA cloning, stable expression in V79 cells and functional characterisation of the expressed enzyme. Mol Cell Endocrinol 112:53–60
   PubMed Web of Science ®Google Scholar
• Fuda H, Javitt NB, Mitamura K, et al. (2007). Oxysterols are substrates for cholesterol sulfotransferase. J Lipid Res 48:1343–1352
   PubMed Web of Science ®Google Scholar
• Fuda H, Lee YC, Shimizu C, et al. (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
• Geese WJ, Raftogianis RB. (2001). Biochemical characterization and tissue distribution of human SULT2B1. Biochem Biophys Res Commun 288:280–289
   PubMed Web of Science ®Google Scholar
• Gill S, Chow R, Brown AJ. (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
• Hanyu O, Nakae H, Miida T, et al. (2012). Cholesterol sulfate induces expression of the skin barrier protein filaggrin in normal human epidermal keratinocytes through induction of RORalpha. Biochem Biophys Res Commun 428:99–104
   PubMed Web of Science ®Google Scholar
• He D, Falany CN. (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, Frost AR, Falany CN. (2005). Identification and immunohistochemical localization of sulfotransferase 2B1b (SULT2B1b) in human lung. Biochim Biophys Acta 1724:119–126
   PubMed Web of Science ®Google Scholar
• He D, Meloche CA, Dumas NA, et al. (2004). Different subcellular localization of sulphotransferase 2B1b in human placenta and prostate. Biochem J 379:533–540
   PubMed Web of Science ®Google Scholar
• Her C, Wood TC, Eichler EE, 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, 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
• Hofmann AF. (2004). Detoxification of lithocholic acid, a toxic bile acid: Relevance to drug hepatotoxicity. Drug Metab Rev 36:703–722
   PubMed Web of Science ®Google Scholar
• Hornsby P. (1995). Biosynthesis of DHEAS by the human adrenal cortex and its age-related decline. N Y Acad Sci 774:29–46
   PubMed Web of Science ®Google Scholar
• Iwamori M, Moser HW, Kishimoto Y. (1976). Cholesterol sulfate in rat tissues. Tissue distribution, developmental change and brain subcellular localization. Biochim Biophys Acta 441:268–279
   PubMed Web of Science ®Google Scholar
• Javitt NB, Lee YC, Shimizu C, et al. (2001). Cholesterol and hydroxycholesterol sulfotransferases: Identification, distinction from dehydroepiandrosterone sulfotransferase, and differential tissue expression. Endocrinology 142:2978–2984
   PubMed Web of Science ®Google Scholar
• Ji Y, Moon I, Zlatkovic J, et al. (2007). Human hydroxysteroid sulfotransferase SULT2B1 pharmacogenomics: Gene sequence variation and functional genomics. J Pharmacol Exp Ther 322:529–540
   PubMed Web of Science ®Google Scholar
• Jiang YJ, Kim P, Elias PM, et al. (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
• Kakuta Y, Pedersen LG, Pedersen LC, et al. (1998a). Conserved structural motifs in the sulfotransferase family. Trends Biochem Sci 23:129–130
   PubMed Web of Science ®Google Scholar
• Kakuta Y, Petrotchenko EV, Pedersen LC, et al. (1998b). The sulfuryl transfer mechanism. Crystal structure of a vanadate complex of estrogen sulfotransferase and mutational analysis. J Biol Chem 273:27325–27330
   PubMed Web of Science ®Google Scholar
• Kallen J, Schlaeppi JM, Bitsch F, et al. (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
• Kocarek TA, Duanmu Z, Fang HL, et al. (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
• Kohjitani A, Fuda H, Hanyu O, et al. (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
• Kohjitani A, Fuda H, Hanyu O, et al. (2008). Regulation of SULT2B1a (pregnenolone sulfotransferase) expression in rat C6 glioma cells: Relevance of AMPA receptor-mediated NO signaling. Neurosci Lett 430:75–80
   PubMed Web of Science ®Google Scholar
• Koizumi M, Momoeda M, Hiroi H, et al. (2010). Expression and regulation of cholesterol sulfotransferase (SULT2B1b) in human endometrium. Fertil Steril 93:1538–1544
   PubMed Web of Science ®Google Scholar
• Kurogi K, Sakakibara Y, Kamemoto Y, et al. (2010). Mouse cytosolic sulfotransferase SULT2B1b interacts with cytoskeletal proteins via a proline/serine-rich C-terminus. FEBS J 277:3804–3811
   PubMed Web of Science ®Google Scholar
• Li X, Pandak WM, Erickson SK, et al. (2007). Biosynthesis of the regulatory oxysterol, 5-cholesten-3beta,25-diol 3-sulfate, in hepatocytes. J Lipid Res 48:2587–2596
   PubMed Web of Science ®Google Scholar
• Liere P, Pianos A, Eychenne B, et al. (2009). Analysis of pregnenolone and dehydroepiandrosterone in rodent brain: Cholesterol autoxidation is the key. J Lipid Res 50:2430–2444
   PubMed Web of Science ®Google Scholar
• Liu S, Sjovall J, Griffiths WJ. (2003). Neurosteroids in rat brain: Extraction, isolation, and analysis by nanoscale liquid chromatography-electrospray mass spectrometry. Anal Chem 75:5835–5846
   PubMed Web of Science ®Google Scholar
• Longcope C. (1995). Metabolism of dehydroepiandrosterone. Ann N Y Acad Sci 774:143–148
   PubMed Web of Science ®Google Scholar
• Luchetti S, Bossers K, Frajese GV, et al. (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
• Meloche CA, Falany CN. (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
• Meloche CA, Sharma V, Swedmark S, et al. (2002). Sulfation of budesonide by human cytosolic sulfotransferase, dehydroepiandrosterone-sulfotransferase (DHEA-ST). Drug Metab Dispos 30:582–585
   PubMed Web of Science ®Google Scholar
• Musso G, Gambino R, Cassader M. (2013). Cholesterol metabolism and the pathogenesis of non-alcoholic steatohepatitis. Prog Lipid Res 52:175–191
   PubMed Web of Science ®Google Scholar
• Negishi M, Pedersen LG, Petrotchenko E, et al. (2001). Structure and function of sulfotransferases. Arch Biochem Biophys 390:149–157
   PubMed Web of Science ®Google Scholar
• Nelissen K, Mulder M, Smets I, et al. (2012). Liver X receptors regulate cholesterol homeostasis in oligodendrocytes. J Neurosci Res 90:60–71
   PubMed Web of Science ®Google Scholar
• Parker CR Jr, Jian M, Conley AJ. (2000). The localization of DHEA sulfotransferase in steroidogenic and steroid metabolizing tissues of the adult rhesus macaque monkey. Endocr Res 26:517–522
   PubMed Web of Science ®Google Scholar
• Petit GH, Tobin C, Krishnan K, et al. (2011). Pregnenolone sulfate and its enantiomer: Differential modulation of memory in a spatial discrimination task using forebrain NMDA receptor deficient mice. Eur Neuropsychopharmacol 21:211–215
   PubMed Web of Science ®Google Scholar
• Prasad VV, el-Maraghy E, Ponticorvo L, et al. (1985). Detection in extracts of bovine brain of lipophilic complexes of sulfate esters of cholesterol and beta-sitosterol. Proc Natl Acad Sci USA 82:2657–2659
   PubMed Web of Science ®Google Scholar
• Raftogianis RB, Wood TC, Weinshilboum RM. (1999). Human phenol sulfotransferases SULT1A2 and SULT1A1: Genetic polymorphisms, allozyme properties, and human liver genotype--phenotype correlations. Biochem Pharmacol 58:605–616
   PubMed Web of Science ®Google Scholar
• Reschly EJ, Ai N, Welsh WJ, et al. (2008). Ligand specificity and evolution of liver X receptors. J Steroid Biochem Mol Biol 110:83–94
   PubMed Web of Science ®Google Scholar
• Salman E, Faye-Peterson O, Falany C. (2011a). Hydroxysteroid sulfotransferase 2B1b expression and localization in normal human brain. Horm Mol Biol Clin Invest 8:445–454
   Google Scholar
• Salman ED, He D, Runge-Morris M, et al. (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
• Salman ED, Kadlubar SA, Falany CN. (2009). Expression and localization of cytosolic sulfotransferase (SULT) 1A1 and SULT1A3 in normal human brain. Drug Metab Dispos 37:706–709
   PubMed Web of Science ®Google Scholar
• Sasano H, Sato F, Shizawa S, et al. (1995). Immunolocalization of dehydroepiandrosterone sulfotransferase in normal and pathologic human adrenal gland. Mod Pathol 8:891–896
   PubMed Web of Science ®Google Scholar
• Schroder E, Gebel L, Eremeev AA, et al. (2012). Human PAPS synthase isoforms are dynamically regulated enzymes with access to nucleus and cytoplasm. PLoS One 7:e29559
   PubMed Web of Science ®Google Scholar
• Shimada M, Kamiyama Y, Sato A, et al. (2002). A hydroxysteroid sulfotransferase, st2b2, is a skin cholesterol sulfotransferase in mice. J Biochem 131:167–169
   PubMed Web of Science ®Google Scholar
• Shimada M, Matsuda T, Sato A, et al. (2008). Expression of a skin cholesterol sulfotransferase, St2b2, is a trigger of epidermal cell differentiation. Xenobiotica 38:1487–1499
   PubMed Web of Science ®Google Scholar
• Shimizu C, Fuda H, Yanai H, et al. (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
• Strott CA. (2002). Sulfonation and molecular action. Endocr Rev 23:703–732
   PubMed Web of Science ®Google Scholar
• Strott CA, 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
• Tanaka M, Sokabe M. (2012). Continuous de novo synthesis of neurosteroids is required for normal synaptic transmission and plasticity in the dentate gyrus of the rat hippocampus. Neuropharmacology 62:2373–2387
   PubMed Web of Science ®Google Scholar
• Tashiro A, Sasano H, Nishikawa T, 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
• Tsutsui K, Ukena K, Usui M, et al. (2000). Novel brain function: Biosynthesis and actions of neurosteroids in neurons. Neurosci Res 36:261–273
   PubMed Web of Science ®Google Scholar
• Twede V, Tartaglia AL, Covey DF, et al. (2007). The neurosteroids dehydroepiandrosterone sulfate and pregnenolone sulfate inhibit the UNC-49 GABA receptor through a common set of residues. Mol Pharmacol 72:1322–1329
   PubMed Web of Science ®Google Scholar
• Weitzner B, Meehan T, Xu Q, et al. (2008). An unusually small dimer interface is observed in all available crystal structures of cytosolic sulfotransferases. Proteins 75:289--295
   Web of Science ®Google Scholar
• Wojcicka G, Jamroz-Wisniewska A, Horoszewicz K, et al. (2007). Liver X receptors (LXRs). Part I: Structure, function, regulation of activity, and role in lipid metabolism. Postepy Hig Med Dosw (Online) 61:736–759
   PubMedGoogle Scholar
• Yanai H, Javitt NB, Higashi Y, et al. (2004). Expression of cholesterol sulfotransferase (SULT2B1b) in human platelets. Circulation 109:92–96
   PubMed Web of Science ®Google Scholar
• Zhang X, Bai Q, Kakiyama G, et al. (2012a). Cholesterol metabolite, 5-cholesten-3beta-25-diol-3-sulfate, promotes hepatic proliferation in mice. J Steroid Biochem Mol Biol 132:262–270
   PubMed Web of Science ®Google Scholar
• Zhang X, Bai Q, Xu L, et al. (2012b). Cytosolic sulfotransferase 2B1b promotes hepatocyte proliferation gene expression in vivo and in vitro. Am J Physiol Gastrointest Liver Physiol 303:G344–G355
   PubMed Web of Science ®Google Scholar