Quantitative distribution of mRNAs encoding the 19 human UDP-glucuronosyltransferase enzymes in 26 adult and 3 fetal tissues

References

• Barbier O, Torra IP, Sirvent A, Claudel T, Blanquart C, Duran-Sandoval D, Kuipers F, Kosykh V, Fruchart JC, Staels B. (2003). FXR induces the UGT2B4 enzyme in hepatocytes: A potential mechanism of negative feedback control of FXR activity. Gastroenterology 124:1926–1940.
   PubMed Web of Science ®Google Scholar
• Coughtrie MW, Burchell B, Leakey JE, Hume R. (1988). The inadequacy of perinatal glucuronidation: Immunoblot analysis of the developmental expression of individual UDP-glucuronosyltransferase isoenzymes in rat and human liver microsomes. Mol Pharmacol 34:729–735.
   PubMed Web of Science ®Google Scholar
• Courillon F, Gerhardt MF, Myara A, Daffos F, Forestier F, Trivin F. (1998). Serum C24 bile acids in the developing human fetus. Biol Neonate 73:76–88.
   PubMedGoogle Scholar
• Court MH, Krishnaswamy S, Hao Q, Duan SX, Patten CJ, Von Moltke LL, Greenblatt DJ. (2003). Evaluation of 3′-azido-3′-deoxythymidine, morphine, and codeine as probe substrates for UDP-glucuronosyltransferase 2B7 (UGT2B7) in human liver microsomes: Specificity and influence of the UGT2B7*2 polymorphism. Drug Metab Dispos 31:1125–1133.
   PubMed Web of Science ®Google Scholar
• Court MH. (2005). Isoform-selective probe substrates for in vitro studies of human UDP-glucuronosyltransferases. Meth Enzymol 400:104–116.
   PubMed Web of Science ®Google Scholar
• Court MH, Hazarika S, Krishnaswamy S, Finel M, Williams JA. (2008). Novel polymorphic human UDP-glucuronosyltransferase (UGT) 2A3: Cloning, functional characterization of enzyme variants, comparative tissue expression, and gene induction. Mol Pharmacol 74:744–754.
   PubMed Web of Science ®Google Scholar
• Court MH. (2010). Inter-individual variability in hepatic drug glucuronidation: Studies into the role of age, sex, enzyme inducers, and genetic polymorphism using the human liver bank as a model system. Drug Metab Rev 42:209–224.
   PubMed Web of Science ®Google Scholar
• Guillemette C, Lévesque E, Harvey M, Bellemare J, Menard V. (2010). UGT genomic diversity: Beyond gene duplication. Drug Metab Rev 42:24–44.
   PubMed Web of Science ®Google Scholar
• Itäaho K, Court MH, Uutela P, Kostiainen R, Radominska-Pandya A, Finel M. (2009). Dopamine is a low-affinity and high-specificity substrate for the human UDP-glucuronosyltransferase 1A10. Drug Metab Dispos 37:768–775.
   PubMed Web of Science ®Google Scholar
• Izukawa T, Nakajima M, Fujiwara R, Yamanaka H, Fukami T, Takamiya M, Aoki Y, Ikushiro S, Sakaki T, Yokoi T. (2009). Quantitative analysis of UDP-glucuronosyltransferase (UGT) 1A and UGT2B expression levels in human livers. Drug Metab Dispos 37:1759–1768.
   PubMed Web of Science ®Google Scholar
• Jedlitschky G, Cassidy AJ, Sales M, Pratt N, Burchell B. (1999). Cloning and characterization of a novel human olfactory UDP-glucuronosyltransferase. Biochem J 340:837–843.
   PubMed Web of Science ®Google Scholar
• Jemnitz K, Heredi-Szabo K, Janossy J, Ioja E, Vereczkey L, Krajcsi P. (2010). ABCC2/Abcc2: A multispecific transporter with dominant excretory functions. Drug Metab Rev 42:402–436.
   PubMed Web of Science ®Google Scholar
• Jeong EJ, Liu X, Jia X, Chen J, Hu M. (2005). Coupling of conjugating enzymes and efflux transporters: Impact on bioavailability and drug interactions. Curr Drug Metab 6:455–468.
   PubMed Web of Science ®Google Scholar
• Jin CJ, Mackenzie PI, Miners JO. (1997). The regio- and stereo-selectivity of C19 and C21 hydroxysteroid glucuronidation by UGT2B7 and UGT2B11. Arch Biochem Biophys 341:207–211.
   PubMed Web of Science ®Google Scholar
• Kaivosaari S, Toivonen P, Hesse LM, Koskinen M, Court MH, Finel M. (2007). Nicotine glucuronidation and the human UDP-glucuronosyltransferase UGT2B10. Mol Pharmacol 72:761–768.
   PubMed Web of Science ®Google Scholar
• Karlen Y, McNair A, Perseguers S, Mazza C, Mermod N. (2007). Statistical significance of quantitative PCR. BMC Bioinformatics 8:131.
   PubMed Web of Science ®Google Scholar
• Laakkonen L, Finel M. (2010). A molecular model of the human UDP-glucuronosyltransferase 1A1, its membrane orientation, and the interactions between different parts of the enzyme. Mol Pharmacol 77:931–939.
   PubMed Web of Science ®Google Scholar
• Lazard D, Zupko K, Poria Y, Nef P, Lazarovits J, Horn S, Khen M, Lancet D. (1991). Odorant signal termination by olfactory UDP glucuronosyl transferase. Nature 349:790–793.
   PubMed Web of Science ®Google Scholar
• Mackenzie PI, Bock KW, Burchell B, Guillemette C, Ikushiro S, Iyanagi T, Miners JO, Owens IS, Nebert DW. (2005). Nomenclature update for the mammalian UDP glycosyltransferase (UGT) gene superfamily. Pharmacogenet Genomics 15:677–685.
   PubMed Web of Science ®Google Scholar
• Mahone PR, Scott K, Sleggs G, D’Antoni T, Woods JR Jr. (1994). Cocaine and metabolites in amniotic fluid may prolong fetal drug exposure. Am J Obstet Gynecol 171:465–469.
   PubMed Web of Science ®Google Scholar
• Manevski N, Kurkela M, Höglund C, Mauriala T, Court MH, Yli-Kauhaluoma J, Finel M. (2010). Glucuronidation of psilocin and 4-hydroxyindole by the human UDP-glucuronosyltransferases. Drug Metab Dispos 38:386–395.
   PubMed Web of Science ®Google Scholar
• Nakamura A, Nakajima M, Yamanaka H, Fujiwara R, Yokoi T. (2008). Expression of UGT1A and UGT2B mRNA in human normal tissues and various cell lines. Drug Metab Dispos 36:1461–1464.
   PubMed Web of Science ®Google Scholar
• Nishimura M, Naito S. (2006). Tissue-specific mRNA expression profiles of human phase I metabolizing enzymes except for cytochrome P450 and phase II metabolizing enzymes. Drug Metab Pharmacokinet 21:357–374.
   PubMed Web of Science ®Google Scholar
• Ohno S, Nakajin S. (2009). Determination of mRNA expression of human UDP-glucuronosyltransferases and application for localization in various human tissues by real-time reverse transcriptase-polymerase chain reaction. Drug Metab Dispos 37:32–40.
   PubMed Web of Science ®Google Scholar
• Pillot T, Ouzzine M, Fournel-Gigleux S, Lafaurie C, Radominska A, Burchell B, Siest G, Magdalou J. (1993). Glucuronidation of hyodeoxycholic acid in human liver. Evidence for a selective role of UDP-glucuronosyltransferase 2B4. J Biol Chem 268:25636–25642.
   PubMed Web of Science ®Google Scholar
• Radominska-Pandya A, Czernik PJ, Little JM, Battaglia E, Mackenzie PI. (1999). Structural and functional studies of UDP-glucuronosyltransferases. Drug Metab Rev 31:817–899.
   PubMed Web of Science ®Google Scholar
• Shoda J, Mahara R, Osuga T, Tohma M, Ohnishi S, Miyazaki H, Tanaka N, Matsuzaki Y. (1988). Similarity of unusual bile acids in human umbilical cord blood and amniotic fluid from newborns and in sera and urine from adult patients with cholestatic liver diseases. J Lipid Res 29:847–858.
   PubMed Web of Science ®Google Scholar
• Sneitz N, Court MH, Zhang X, Laajanen K, Yee KK, Dalton P, Ding X, and Finel M. (2009). Human UDP-glucuronosyltransferase UGT2A2: cDNA construction, expression, and functional characterization in comparison with UGT2A1 and UGT2A. Pharmacogenet Genomics 19:923–934.
   PubMed Web of Science ®Google Scholar
• Somers GI, Lindsay N, Lowdon BM, Jones AE, Freathy C, Ho S, Woodrooffe AJ, Bayliss MK, Manchee GR. (2007). A comparison of the expression and metabolizing activities of phase I and II enzymes in freshly isolated human lung parenchymal cells and cryopreserved human hepatocytes. Drug Metab Dispos 35:1797–1805.
   PubMed Web of Science ®Google Scholar
• Strassburg CP, Strassburg A, Kneip S, Barut A, Tukey RH, Rodeck B, Manns MP. (2002). Developmental aspects of human hepatic drug glucuronidation in young children and adults. Gut 50:259–265.
   PubMed Web of Science ®Google Scholar
• Tchernof A, Levesque E, Beaulieu M, Couture P, Despres JP, Hum DW, Belanger A. (1999). Expression of the androgen metabolizing enzyme UGT2B15 in adipose tissue and relative expression measurement using a competitive RT-PCR method. Clin Endocrinol 50:637–642.
   PubMed Web of Science ®Google Scholar
• Tukey RH, Strassburg CP. (2000). Human UDP-glucuronosyltransferases: Metabolism, expression, and disease. Annu Rev Pharmacol Toxicol 40:581–616.
   PubMed Web of Science ®Google Scholar
• Tukey RH, Strassburg CP. (2001). Genetic multiplicity of the human UDP-glucuronosyltransferases and regulation in the gastrointestinal tract. Mol Pharmacol 59:405–414.
   PubMed Web of Science ®Google Scholar
• Turgeon D, Carrier JS, Levesque E, Hum DW, Belanger A. (2001). Relative enzymatic activity, protein stability, and tissue distribution of human steroid-metabolizing UGT2B subfamily members. Endocrinology 142:778–787.
   PubMed Web of Science ®Google Scholar
• Wells PG, Mackenzie PI, Chowdhury JR, Guillemette C, Gregory PA, Ishii Y, Hansen AJ, Kessler FK, Kim PM, Chowdhury NR, Ritter JK. (2004). Glucuronidation and the UDP-glucuronosyltransferases in health and disease. Drug Metab Dispos 32:281–290.
   PubMed Web of Science ®Google Scholar
• Wilson W 3rd, Pardo-Manuel de Villena F, Lyn-Cook BD, Chatterjee PK, Bell TA, Detwiler DA, Gilmore RC, Valladeras IC, Wright CC, Threadgill DW, Grant DJ. (2004). Characterization of a common deletion polymorphism of the UGT2B17 gene linked to UGT2B15. Genomics 84:707–714.
   PubMed Web of Science ®Google Scholar
• Xue Y, Sun D, Daly A, Yang F, Zhou X, Zhao M, Huang N, Zerjal T, Lee C, Carter NP, Hurles ME, Tyler-Smith C. (2008). Adaptive evolution of UGT2B17 copy-number variation. Am J Hum Genet 83:337–346.
   PubMed Web of Science ®Google Scholar
• Zhou D, Guo J, Linnenbach AJ, Booth-Genthe CL, Grimm SW. (2010). Role of human UGT2B10 in N-glucuronidation of tricyclic antidepressants, amitriptyline, imipramine, clomipramine, and trimipramine. Drug Metab Dispos 38:863–870.
   PubMed Web of Science ®Google Scholar