메뉴 건너뛰기




Volumn 28, Issue 2, 2013, Pages 83-92

Function, genetic polymorphism, and transcriptional regulation of human UDP-glucuronosyltransferase (UGT) 1A1

Author keywords

Aryl hydrocarbon receptor; Bilirubin; Constitutive androstane receptor; Environmental factors; Genetic polymorphism; Nuclear factor (Erythroid derived 2) like 2; Pregnane X receptor; Transcriptional factors; UDP glucuronosyltransferase 1A1; Unconjugated hyperbilirubinemia

Indexed keywords

AROMATIC HYDROCARBON RECEPTOR; ARTEMISININ; CLOFIBRATE; CLOTRIMAZOLE; CONSTITUTIVE ANDROSTANE RECEPTOR; CYCLIC AMP DEPENDENT PROTEIN KINASE; DEXAMETHASONE; ESTRADIOL; ETOPOSIDE; FIRTECAN; GLUCOCORTICOID; GLUCURONIC ACID; GLUCURONOSYLTRANSFERASE 1A1; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HEPATOCYTE NUCLEAR FACTOR 1ALPHA; HEPATOCYTE NUCLEAR FACTOR 4ALPHA; LIPOXIN A; LITHOCHOLIC ACID; PARACETAMOL; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR ALPHA; PREGNANE X RECEPTOR; PROTEIN KINASE C; RETINOID X RECEPTOR; RIFAMPICIN; STEROID RECEPTOR COACTIVATOR 1; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR NRF2; UNINDEXED DRUG; XENOBIOTIC AGENT;

EID: 84876774484     PISSN: 13474367     EISSN: 18800920     Source Type: Journal    
DOI: 10.2133/dmpk.DMPK-12-RV-096     Document Type: Review
Times cited : (81)

References (121)
  • 1
    • 0014870444 scopus 로고
    • Isolation and properties of conjugated bilirubin and bile
    • Ostrow, J. D. and Murphy, N. H.: Isolation and properties of conjugated bilirubin and bile. Biochem. J., 120: 311-327 (1970).
    • (1970) Biochem. J , vol.120 , pp. 311-327
    • Ostrow, J.D.1    Murphy, N.H.2
  • 3
    • 0034128936 scopus 로고    scopus 로고
    • Human UDP-glucuronosyltransfer-ases: Metabolism, expression, and disease
    • Tukey, R. H. and Strassburg, C. P.: Human UDP-glucuronosyltransfer-ases: metabolism, expression, and disease. Annu. Rev. Pharmacol. Toxicol., 40: 581-616 (2000).
    • (2000) Annu. Rev. Pharmacol. Toxicol , vol.40 , pp. 581-616
    • Tukey, R.H.1    Strassburg, C.P.2
  • 5
    • 0030728222 scopus 로고    scopus 로고
    • Genetic defects of the UDP-glucuronosyl-transferase-1 (UGT1) gene that cause familial non-haemolytic uncon-jugated hyperbilirubinaemias
    • Clarke, D. J., Moghrabi, N., Monaghan, G., Cassidy, A., Boxer, M., Hume, R. and Burchell, B.: Genetic defects of the UDP-glucuronosyl-transferase-1 (UGT1) gene that cause familial non-haemolytic uncon-jugated hyperbilirubinaemias. Clin. Chim. Acta, 266: 63-74 (1997).
    • (1997) Clin. Chim. Acta , vol.266 , pp. 63-74
    • Clarke, D.J.1    Moghrabi, N.2    Monaghan, G.3    Cassidy, A.4    Boxer, M.5    Hume, R.6    Burchell, B.7
  • 6
    • 0034695410 scopus 로고    scopus 로고
    • Isolation and characterization of the human UGT2B15 gene, localized within a cluster of UGT2B genes and pseudogenes on chromosome 4
    • Turgeon, D., Carrier, J.-S., Levesque, E., Beatty, B. G., Belanger, A. and Hum, D. W.: Isolation and characterization of the human UGT2B15 gene, localized within a cluster of UGT2B genes and pseudogenes on chromosome 4. J. Mol. Biol., 295: 489-504 (2000).
    • (2000) J. Mol. Biol , vol.295 , pp. 489-504
    • Turgeon, D.1    Carrier, J.-S.2    Levesque, E.3    Beatty, B.G.4    Belanger, A.5    Hum, D.W.6
  • 8
    • 0026701911 scopus 로고
    • A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase iozymes with identical carboxyl termini
    • Ritter, J. K., Chen, F., Sheen, Y. Y., Tran, H. M., Kimura, S., Yeatman, M. T. and Owens, I. S.: A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase iozymes with identical carboxyl termini. J. Biol. Chem., 267: 3257-3261 (1992).
    • (1992) J. Biol. Chem , vol.267 , pp. 3257-3261
    • Ritter, J.K.1    Chen, F.2    Sheen, Y.Y.3    Tran, H.M.4    Kimura, S.5    Yeatman, M.T.6    Owens, I.S.7
  • 9
    • 0141592530 scopus 로고    scopus 로고
    • Cloning and characterization of the human UDP-glucuronosyltransferase 1A8, 1A9, and 1A10 gene ptomoters
    • Gregory, P. A., Gardner-Stephen, D. A., Lewinsky, H. H., Duncliffe, K. N. and Mackenzie, P. I.: Cloning and characterization of the human UDP-glucuronosyltransferase 1A8, 1A9, and 1A10 gene ptomoters. J. Biol. Chem., 278: 36107-36114 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 36107-36114
    • Gregory, P.A.1    Gardner-Stephen, D.A.2    Lewinsky, H.H.3    Duncliffe, K.N.4    Mackenzie, P.I.5
  • 10
    • 58149467072 scopus 로고    scopus 로고
    • Determination of mRNA expression of human UDP-glucuronosyltransferases and application for localization in various human tissues by real-time reverse transcriptase-polymerase chain reaction
    • Ohno, S. and Nakajin, S.: 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 (2009).
    • (2009) Drug Metab. Dispos , vol.37 , pp. 32-40
    • Ohno, S.1    Nakajin, S.2
  • 11
    • 0001438682 scopus 로고
    • Congenital familial non-hemolytic jaundice with kernicterus
    • Crigler, J. F., Jr. and Najjar, V. A.: Congenital familial non-hemolytic jaundice with kernicterus. Pediatrics, 10: 169-180 (1952).
    • (1952) Pediatrics , vol.10 , pp. 169-180
    • Crigler, J.F.1    Najjar, V.A.2
  • 12
    • 0036765343 scopus 로고    scopus 로고
    • Pharmacogenomics of human UDP-glucuronosyltransferases and irinotecan toxicity
    • Tukey, R. H., Strassburg, C. P. and Mackenzie, P. I.: Pharmacogenomics of human UDP-glucuronosyltransferases and irinotecan toxicity. Mol. Pharmacol., 62: 446-450 (2002).
    • (2002) Mol. Pharmacol , vol.62 , pp. 446-450
    • Tukey, R.H.1    Strassburg, C.P.2    Mackenzie, P.I.3
  • 14
    • 83755172199 scopus 로고    scopus 로고
    • Reduced expression of UGT1A1 in intestines of humanized UGT1 mice via inactivation of NF-B leads to hyperbilirubinemia
    • Fujiwara, R., Chen, S., Karin, M. and Tukey, R. H.: Reduced expression of UGT1A1 in intestines of humanized UGT1 mice via inactivation of NF-B leads to hyperbilirubinemia. Gastroenterology., 142: 109-118 (2012).
    • (2012) Gastroenterology , vol.142 , pp. 109-118
    • Fujiwara, R.1    Chen, S.2    Karin, M.3    Tukey, R.H.4
  • 15
    • 84864348294 scopus 로고    scopus 로고
    • Pregnane-X-receptor controls hepatic glucuronidation during pregnancy and neonatal development in humanized mice
    • Chen, S., Yueh, M.-F., Evans, R. M. and Tukey, R. H.: Pregnane-X-receptor controls hepatic glucuronidation during pregnancy and neonatal development in humanized mice. Hepatology, 56: 658-667 (2012).
    • (2012) Hepatology , vol.56 , pp. 658-667
    • Chen, S.1    Yueh, M.-F.2    Evans, R.M.3    Tukey, R.H.4
  • 16
    • 0024272881 scopus 로고
    • The inadequacy of perinatal glucuronidation: Immunoblot analysis of the developmental expression of individual UDP-glucuronosyltransferase isoenzymes in rat and human liver microsomes
    • Coughtrie, M. W. H., Burchell, B., Leakey, J. E. A. and Hume, R.: 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 (1988).
    • (1988) Mol. Pharmacol , vol.34 , pp. 729-735
    • Coughtrie, M.W.H.1    Burchell, B.2    Leakey, J.E.A.3    Hume, R.4
  • 17
    • 77950395654 scopus 로고    scopus 로고
    • Effect of oncostatin M on uridine diphosphate-5A-glucuronosyltransferase 1A1 through cross talk with constitutive androstane receptor
    • Masuyama, H., Nakatsukasa, H. and Hiramatsu, Y.: Effect of oncostatin M on uridine diphosphate-5A-glucuronosyltransferase 1A1 through cross talk with constitutive androstane receptor. Mol. Endocrinol., 24: 745-753 (2010).
    • (2010) Mol. Endocrinol , vol.24 , pp. 745-753
    • Masuyama, H.1    Nakatsukasa, H.2    Hiramatsu, Y.3
  • 18
    • 14944341677 scopus 로고    scopus 로고
    • Transcriptional regulation of human UGT1A1 gene expression: Activated glucocorticoid receptor enhances constitutive androstane receptor/pregnane X receptor-mediated UDP-glucuronosyltransferase 1A1 regulation with glucocorticoid receptor-interacting protein 1
    • Sugatani, J., Nishitani, S., Yamakawa, K., Yoshinari, K., Sueyoshi, T., Negishi, M. and Miwa, M.: Transcriptional regulation of human UGT1A1 gene expression: Activated glucocorticoid receptor enhances constitutive androstane receptor/pregnane X receptor-mediated UDP-glucuronosyltransferase 1A1 regulation with glucocorticoid receptor-interacting protein 1. Mol. Pharmacol., 67: 845-855 (2005).
    • (2005) Mol. Pharmacol , vol.67 , pp. 845-855
    • Sugatani, J.1    Nishitani, S.2    Yamakawa, K.3    Yoshinari, K.4    Sueyoshi, T.5    Negishi, M.6    Miwa, M.7
  • 19
    • 0035197725 scopus 로고    scopus 로고
    • Interindividual variability in acetaminophen glucuronidation by human liver microsomes: Identification of relevant acetaminophen UDP-glucuronosyltransferase isoforms
    • Court, M. H., Duan, S. X., von Moltke, L. L., Greenblatt, D. J., Patten, C. J., Miners, J. O. and Mackenzie, P. I.: Interindividual variability in acetaminophen glucuronidation by human liver microsomes: identification of relevant acetaminophen UDP-glucuronosyltransferase isoforms. J. Pharmacol. Exp. Ther., 299: 998-1006 (2001).
    • (2001) J. Pharmacol. Exp. Ther , vol.299 , pp. 998-1006
    • Court, M.H.1    Duan, S.X.2    von Moltke, L.L.3    Greenblatt, D.J.4    Patten, C.J.5    Miners, J.O.6    Mackenzie, P.I.7
  • 20
    • 0033786733 scopus 로고    scopus 로고
    • The specificity of glucuronidation of entacapone and tolcapone by recombinant human UDP-glucuronosyltransferases
    • Lautala, P., Ethell, B. T., Taskinen, J. and Burchell, B.: The specificity of glucuronidation of entacapone and tolcapone by recombinant human UDP-glucuronosyltransferases. Drug Metab. Dispos., 28: 1385-1389 (2000).
    • (2000) Drug Metab. Dispos , vol.28 , pp. 1385-1389
    • Lautala, P.1    Ethell, B.T.2    Taskinen, J.3    Burchell, B.4
  • 21
    • 0037404036 scopus 로고    scopus 로고
    • Glucuronidation of etoposide in human liver microsomes is specifically catalyzed by UDP-glucuronosyltransferase 1A1
    • Watanabe, Y., Nakajima, M., Ohashi, N., Kume, T. and Yokoi, T.: Glucuronidation of etoposide in human liver microsomes is specifically catalyzed by UDP-glucuronosyltransferase 1A1. Drug Metab. Dispos., 31: 589-595 (2003).
    • (2003) Drug Metab. Dispos , vol.31 , pp. 589-595
    • Watanabe, Y.1    Nakajima, M.2    Ohashi, N.3    Kume, T.4    Yokoi, T.5
  • 22
    • 0042679455 scopus 로고    scopus 로고
    • Isoform selectivity and kinetics of morphine 3-and 6-glucuronidation by human udp-glucuronosyltransferases: Evidence for atypical glucuronidation kinetics by UGT2B7
    • Stone, A. N., Mackenzie, P. I., Galetin, A., Houston, J. B. and Miners, J. O.: Isoform selectivity and kinetics of morphine 3-and 6-glucuronidation by human udp-glucuronosyltransferases: evidence for atypical glucuronidation kinetics by UGT2B7. Drug Metab. Dispos., 31: 1086-1089 (2003).
    • (2003) Drug Metab. Dispos , vol.31 , pp. 1086-1089
    • Stone, A.N.1    Mackenzie, P.I.2    Galetin, A.3    Houston, J.B.4    Miners, J.O.5
  • 23
    • 81255203621 scopus 로고    scopus 로고
    • Glucuronidation of the steroid enantiomers ent-17β-estradiol, ent-androsterone and ent-etiocholanolone by the human UDP-glucuronosyltransferases
    • Sneitz, N., Krishnan, K., Covey, D. F. and Finel, M.: Glucuronidation of the steroid enantiomers ent-17β-estradiol, ent-androsterone and ent-etiocholanolone by the human UDP-glucuronosyltransferases. J. Steroid Biochem. Mol. Biol., 127: 282-288 (2011).
    • (2011) J. Steroid Biochem. Mol. Biol , vol.127 , pp. 282-288
    • Sneitz, N.1    Krishnan, K.2    Covey, D.F.3    Finel, M.4
  • 24
    • 79251474385 scopus 로고    scopus 로고
    • Correlation between bilirubin glucuronidation and estradiol-3-glucuronidation in the presence of model UDP-glucuronosyltransferase 1A1 substrates/inhibitors
    • Zhou, J., Tracy, T. S. and Remmel, R. P.: Correlation between bilirubin glucuronidation and estradiol-3-glucuronidation in the presence of model UDP-glucuronosyltransferase 1A1 substrates/inhibitors. Drug Metab. Dispos., 39: 322-329 (2011).
    • (2011) Drug Metab. Dispos , vol.39 , pp. 322-329
    • Zhou, J.1    Tracy, T.S.2    Remmel, R.P.3
  • 25
    • 0031015504 scopus 로고    scopus 로고
    • Inhibition of angiogenesis and breast cancer in mice by the microtubule inhibitors 2-methoxyestradiol and taxol
    • Klauber, N., Parangi, S., Flynn, E., Hamel, E. and D'Amato, R. J.: Inhibition of angiogenesis and breast cancer in mice by the microtubule inhibitors 2-methoxyestradiol and taxol. Cancer Res., 57: 81-86 (1997).
    • (1997) Cancer Res , vol.57 , pp. 81-86
    • Klauber, N.1    Parangi, S.2    Flynn, E.3    Hamel, E.4    D'Amato, R.J.5
  • 26
    • 0027991904 scopus 로고
    • Investigation of the substrate specificity of a cloned expressed human bilirubin UDP-glucuronosyltransferase: UDP-sugar specificity and involvement in steroid and xenobiotic glucuronidation
    • Senafi, S. B., Clarke, D. J. and Burchell, B.: Investigation of the substrate specificity of a cloned expressed human bilirubin UDP-glucuronosyltransferase: UDP-sugar specificity and involvement in steroid and xenobiotic glucuronidation. Biochem. J., 303: 233-240 (1994).
    • (1994) Biochem. J , vol.303 , pp. 233-240
    • Senafi, S.B.1    Clarke, D.J.2    Burchell, B.3
  • 29
    • 84876755525 scopus 로고    scopus 로고
    • UDP-glucuronosyltransferase alleles nomenclature committee
    • UDP-glucuronosyltransferase alleles nomenclature committee.: UGT1A1 and common exons allele nomenclature (2010). http://www.pharmacogenomics.pha.ulaval.ca/cms/ugt_alleles
    • (2010) UGT1A1 and Common Exons Allele Nomenclature
  • 31
    • 0030030762 scopus 로고    scopus 로고
    • Genetic variation in bilirubin UPD-glucuronosyltransferase gene promoter and Gilbert's syndrome
    • Monaghan, G., Ryan, M., Seddon, R., Hume, R. and Burchell, B.: Genetic variation in bilirubin UPD-glucuronosyltransferase gene promoter and Gilbert's syndrome. Lancet, 347: 578-581 (1996).
    • (1996) Lancet , vol.347 , pp. 578-581
    • Monaghan, G.1    Ryan, M.2    Seddon, R.3    Hume, R.4    Burchell, B.5
  • 33
    • 0028904620 scopus 로고
    • Analysis of genes for bilirubin UDP-glucuronosyltransferase in Gilbert's syndrome
    • Aono, S., Adachi, Y., Uyama, E., Yamada, Y., Keino, H., Nanno, T., Koiwai, O. and Sato, H.: Analysis of genes for bilirubin UDP-glucuronosyltransferase in Gilbert's syndrome. Lancet, 345: 958-959 (1995).
    • (1995) Lancet , vol.345 , pp. 958-959
    • Aono, S.1    Adachi, Y.2    Uyama, E.3    Yamada, Y.4    Keino, H.5    Nanno, T.6    Koiwai, O.7    Sato, H.8
  • 34
    • 0034324675 scopus 로고    scopus 로고
    • Prolonged unconjugated hyperbilirubinemia associated with breast milk and mutations of the bilirubin uridine diphosphate-glucuronosyltrans-ferase gene
    • Maruo, Y., Nishizawa, K., Sato, H., Sawa, H. and Shimada, M.: Prolonged unconjugated hyperbilirubinemia associated with breast milk and mutations of the bilirubin uridine diphosphate-glucuronosyltrans-ferase gene. Pediatrics, 106: E59 (2000).
    • (2000) Pediatrics , vol.106
    • Maruo, Y.1    Nishizawa, K.2    Sato, H.3    Sawa, H.4    Shimada, M.5
  • 35
    • 0033001454 scopus 로고    scopus 로고
    • Association of neonatal hyperbilirubinemia with bilirubin UDP-glucuronosyltransferase polymorphism
    • Maruo, Y., Nishizawa, K., Sato, H., Doida, Y. and Shimada, M.: Association of neonatal hyperbilirubinemia with bilirubin UDP-glucuronosyltransferase polymorphism. Pediatrics, 103: 1224-1227 (1999).
    • (1999) Pediatrics , vol.103 , pp. 1224-1227
    • Maruo, Y.1    Nishizawa, K.2    Sato, H.3    Doida, Y.4    Shimada, M.5
  • 36
    • 0033841077 scopus 로고    scopus 로고
    • Association of human liver bilirubin UDP-glucuronyltransferase activity with a polymorphism in the promoter region of the UGT1A1 gene
    • Raijmakers, M. T., Jansen, P. L., Steegers, E. A. and Peters, W. H.: Association of human liver bilirubin UDP-glucuronyltransferase activity with a polymorphism in the promoter region of the UGT1A1 gene. J. Hepatol., 33: 348-351 (2000).
    • (2000) J. Hepatol , vol.33 , pp. 348-351
    • Raijmakers, M.T.1    Jansen, P.L.2    Steegers, E.A.3    Peters, W.H.4
  • 37
    • 0031864410 scopus 로고    scopus 로고
    • Contribution of two missense mutations (G71R and Y486D) of the bilirubin UDP glycosyltransferase (UGT1A1) gene to phenotypes of Gilbert's syndrome and Crigler-Najjar syndrome type II
    • Yamamoto, K., Sato, H., Fujiyama, Y., Doida, Y. and Bamba, T.: Contribution of two missense mutations (G71R and Y486D) of the bilirubin UDP glycosyltransferase (UGT1A1) gene to phenotypes of Gilbert's syndrome and Crigler-Najjar syndrome type II. Biochim. Biophys. Acta, 1406: 267-273 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1406 , pp. 267-273
    • Yamamoto, K.1    Sato, H.2    Fujiyama, Y.3    Doida, Y.4    Bamba, T.5
  • 38
    • 0032493441 scopus 로고    scopus 로고
    • Racial variability in the UDP-glucuronosyltransferase 1 (UGT1A1) promoter: A balanced polymorphism for regulation of bilirubin metabolism
    • Beutler, E., Gelbary, T. and Demina, A.: Racial variability in the UDP-glucuronosyltransferase 1 (UGT1A1) promoter: A balanced polymorphism for regulation of bilirubin metabolism? Proc. Natl. Acad. Sci. USA, 95: 8170-8174 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8170-8174
    • Beutler, E.1    Gelbary, T.2    Demina, A.3
  • 39
    • 59849128188 scopus 로고    scopus 로고
    • Can UGT1A1 genotyping reduce morbidity and mortality in patients with metastatic colorectal cancer treated with irinotecan? An evidence-based review
    • Palomaki, G. E., Bradley, L. A., Douglas, M. P., Kolor, K. and Dotson, W. D.: Can UGT1A1 genotyping reduce morbidity and mortality in patients with metastatic colorectal cancer treated with irinotecan? An evidence-based review. Genet. Med., 11: 21-34 (2009).
    • (2009) Genet. Med , vol.11 , pp. 21-34
    • Palomaki, G.E.1    Bradley, L.A.2    Douglas, M.P.3    Kolor, K.4    Dotson, W.D.5
  • 40
    • 0034654290 scopus 로고    scopus 로고
    • Drug-mediated toxicity caused by genetic deficiency of UDP-glucuronosyltransferases
    • Burchell, B., Soars, M., Monaghan, G., Cassidy, A., Smith, D. and Ethell, B.: Drug-mediated toxicity caused by genetic deficiency of UDP-glucuronosyltransferases. Toxicol. Lett., 112-113: 333-340 (2000).
    • (2000) Toxicol. Lett , vol.112-113 , pp. 333-340
    • Burchell, B.1    Soars, M.2    Monaghan, G.3    Cassidy, A.4    Smith, D.5    Ethell, B.6
  • 41
    • 0033799997 scopus 로고    scopus 로고
    • Genetic lesions of bilirubin uridine-diphospho-glucuronate glucuronosyltransferase (UGT1A1) causing Crigler-Najjar and Gilbert syndromes: Correlation of genotype to phenotype
    • Kadakol, A., Ghosh, S. S., Sappal, B. S., Sharma, G., Chowdhury, J. R. and Chowdhury, N. R.: Genetic lesions of bilirubin uridine-diphospho-glucuronate glucuronosyltransferase (UGT1A1) causing Crigler-Najjar and Gilbert syndromes: correlation of genotype to phenotype. Hum. Mutat., 16: 297-306 (2000).
    • (2000) Hum Mutat , vol.16 , pp. 297-306
    • Kadakol, A.1    Ghosh, S.S.2    Sappal, B.S.3    Sharma, G.4    Chowdhury, J.R.5    Chowdhury, N.R.6
  • 42
    • 0014664802 scopus 로고
    • Hepatic bilirubin udp-glucuronyl transferase activity in liver disease and gilbert's syndrome
    • Black, M. and Billing, B. H.: Hepatic bilirubin udp-glucuronyl transferase activity in liver disease and gilbert's syndrome. N. Engl. J. Med., 280: 1266-1271 (1969).
    • (1969) N. Engl. J. Med , vol.280 , pp. 1266-1271
    • Black, M.1    Billing, B.H.2
  • 43
    • 0019927156 scopus 로고
    • Hepatic bilirubin-conjugating enzymes of man in the normal state and in liver disease
    • Adachi, Y. and Yamamoto, T.: Hepatic bilirubin-conjugating enzymes of man in the normal state and in liver disease. Gastroenterol. Jpn., 17: 235-240 (1982).
    • (1982) Gastroenterol. Jpn , vol.17 , pp. 235-240
    • Adachi, Y.1    Yamamoto, T.2
  • 46
    • 0032705521 scopus 로고    scopus 로고
    • Diagnosis and management of Crigler-Najjar syndrome
    • Jansen, P. L. M.: Diagnosis and management of Crigler-Najjar syndrome. Eur. J. Pediatr., 158 Suppl. 2: S89-S94 (1999).
    • (1999) Eur. J. Pediatr , Issue.158 SUPPL. 2
    • Jansen, P.L.M.1
  • 47
    • 0026717412 scopus 로고
    • Management of neonatal hyper-bilirubinaemia and prevention of kernicterus
    • Rubaltelli, F. F. and Griffith, P. F.: Management of neonatal hyper-bilirubinaemia and prevention of kernicterus. Drugs, 43: 864-872 (1992).
    • (1992) Drugs , vol.43 , pp. 864-872
    • Rubaltelli, F.F.1    Griffith, P.F.2
  • 48
    • 0032791711 scopus 로고    scopus 로고
    • Expression and inducibility of the human bilirubin UDP-glucuronosyltransferase UGT1A1 in liver and cultured primary hepatocytes: Evidence for both genetic and environmental influences
    • Ritter, J. K., Kessier, F. K., Thompson, M. T., Grove, A. D., Auveung, D. J. and Fisher, R. A.: Expression and inducibility of the human bilirubin UDP-glucuronosyltransferase UGT1A1 in liver and cultured primary hepatocytes: evidence for both genetic and environmental influences. Hepatology, 30: 476-484 (1999).
    • (1999) Hepatology , vol.30 , pp. 476-484
    • Ritter, J.K.1    Kessier, F.K.2    Thompson, M.T.3    Grove, A.D.4    Auveung, D.J.5    Fisher, R.A.6
  • 49
    • 0036547516 scopus 로고    scopus 로고
    • Pharmacological interventions for the treatment of neonatal jaundice
    • Dennery, P. A.: Pharmacological interventions for the treatment of neonatal jaundice. Semin. Neonatol., 7: 111-119 (2002).
    • (2002) Semin Neonatol , vol.7 , pp. 111-119
    • Dennery, P.A.1
  • 50
    • 0014031478 scopus 로고
    • Enhancement of glucuronide-conjugating capacity in a hyperbilirubinemic infant due to apparent enzyme induction by phenobarbital
    • Yaffe, S. J., Levym, G., Matsuzawa, T. and Baliah, T.: Enhancement of glucuronide-conjugating capacity in a hyperbilirubinemic infant due to apparent enzyme induction by phenobarbital. N. Engl. J. Med., 275: 1461-1466 (1966).
    • (1966) N. Engl. J. Med , vol.275 , pp. 1461-1466
    • Yaffe, S.J.1    Levym, G.2    Matsuzawa, T.3    Baliah, T.4
  • 51
    • 0033525886 scopus 로고    scopus 로고
    • The repressed nuclear receptor CAR responds to phenobarbital in activating the human CYP2B6 gene
    • Sueyoshi, T., Kawamoto, T., Zelko, I., Honkakoski, P. and Negishi, M.: The repressed nuclear receptor CAR responds to phenobarbital in activating the human CYP2B6 gene. J. Biol. Chem., 274: 6043-6046 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 6043-6046
    • Sueyoshi, T.1    Kawamoto, T.2    Zelko, I.3    Honkakoski, P.4    Negishi, M.5
  • 52
    • 0035029401 scopus 로고    scopus 로고
    • The phenobarbital response enhancer module in the human bilirubin UDP-glucuronosyl-transferase UGT1A1 gene and regulation by the nuclear receptor CAR
    • Sugatani, J., Kojima, H., Ueda, A., Kakizaki, S., Yoshinari, K., Gong, Q. H., Owens, I. S., Negishi, M. and Sueyoshi, T.: The phenobarbital response enhancer module in the human bilirubin UDP-glucuronosyl-transferase UGT1A1 gene and regulation by the nuclear receptor CAR. Hepatology, 33: 1232-1238 (2001).
    • (2001) Hepatology , vol.33 , pp. 1232-1238
    • Sugatani, J.1    Kojima, H.2    Ueda, A.3    Kakizaki, S.4    Yoshinari, K.5    Gong, Q.H.6    Owens, I.S.7    Negishi, M.8    Sueyoshi, T.9
  • 53
    • 1042287037 scopus 로고    scopus 로고
    • The induction of human UDP-glucuronosyltransferase 1A1 mediated through a distal enhancer module by flavonoids and xenobiotics
    • Sugatani, J., Yamakawa, K., Tonda, E., Nishitani, S., Yoshinari, K., Degawa, M., Abe, I., Noguchi, H. and Miwa, M.: The induction of human UDP-glucuronosyltransferase 1A1 mediated through a distal enhancer module by flavonoids and xenobiotics. Biochem. Pharmacol., 67: 989-1000 (2004).
    • (2004) Biochem. Pharmacol , vol.67 , pp. 989-1000
    • Sugatani, J.1    Yamakawa, K.2    Tonda, E.3    Nishitani, S.4    Yoshinari, K.5    Degawa, M.6    Abe, I.7    Noguchi, H.8    Miwa, M.9
  • 54
    • 30144438495 scopus 로고    scopus 로고
    • Regulation of the human UGT1A1 gene by nuclear receptors CAR, PXR and GR
    • In: Sies, H. and Packer, L, Philadelphia, Elsevier
    • Sugatani, J., Sueyoshi, T., Negishi, M. and Miwa, M.: Regulation of the human UGT1A1 gene by nuclear receptors CAR, PXR and GR. In: Sies, H. and Packer, L. (eds), Conjugation Enzymes. Methods in Enzymology, Philadelphia, Elsevier, 2005, pp. 92-104.
    • (2005) Conjugation Enzymes. Methods In Enzymology , pp. 92-104
    • Sugatani, J.1    Sueyoshi, T.2    Negishi, M.3    Miwa, M.4
  • 55
    • 84856181093 scopus 로고    scopus 로고
    • Constitutive activity and ligand-dependent activation of the nuclear receptor CAR-insights from molecular dynamics simulations
    • Windshügel, B. and Poso, A.: Constitutive activity and ligand-dependent activation of the nuclear receptor CAR-insights from molecular dynamics simulations. J. Mol. Recognit., 24: 875-882 (2011).
    • (2011) J. Mol. Recognit , vol.24 , pp. 875-882
    • Windshügel, B.1    Poso, A.2
  • 56
    • 84861198882 scopus 로고    scopus 로고
    • FXR and PXR: Potential therapeutic targets in cholestasis
    • Jonker, J. W., Liddle, C. and Downes, M.: FXR and PXR: Potential therapeutic targets in cholestasis. J. Steroid Biochem. Mol. Biol., 130: 147-158 (2012).
    • (2012) J. Steroid Biochem. Mol. Biol , vol.130 , pp. 147-158
    • Jonker, J.W.1    Liddle, C.2    Downes, M.3
  • 57
    • 33847024555 scopus 로고    scopus 로고
    • CAR and PXR: The xenobiotic-sensing receptors
    • Timsit, Y. E. and Negishi, M.: CAR and PXR: The xenobiotic-sensing receptors. Steroids, 72: 231-246 (2007).
    • (2007) Steroids , vol.72 , pp. 231-246
    • Timsit, Y.E.1    Negishi, M.2
  • 58
    • 74549178738 scopus 로고    scopus 로고
    • The regulation of UDP-glucuronosyltransferase genes by tissue-specific and ligand-activated transcription factors
    • Mackenzie, P. I., Hu, D. G. and Gardner-Stephen, D. A.: The regulation of UDP-glucuronosyltransferase genes by tissue-specific and ligand-activated transcription factors. Drug Metab. Rev., 42: 99-109 (2010).
    • (2010) Drug Metab. Rev , vol.42 , pp. 99-109
    • Mackenzie, P.I.1    Hu, D.G.2    Gardner-Stephen, D.A.3
  • 59
    • 79957603666 scopus 로고    scopus 로고
    • From differential induction of UDP-glucuronosyltransfer-ases in rat liver to characterization of responsible ligand-activated transcription factors, and their multilevel crosstalk in humans
    • Bock, K. W.: From differential induction of UDP-glucuronosyltransfer-ases in rat liver to characterization of responsible ligand-activated transcription factors, and their multilevel crosstalk in humans. Biochem. Pharmacol., 82: 9-16 (2011).
    • (2011) Biochem. Pharmacol , vol.82 , pp. 9-16
    • Bock, K.W.1
  • 60
    • 84866067633 scopus 로고    scopus 로고
    • Human UDP-glucuronosyltransferases: Feedback loops between substrates and ligands of their transcription factors
    • Bock, K. W.: Human UDP-glucuronosyltransferases: Feedback loops between substrates and ligands of their transcription factors. Biochem. Pharmacol., 84: 1000-1006 (2012).
    • (2012) Biochem Pharmacol , vol.84 , pp. 1000-1006
    • Bock, K.W.1
  • 61
    • 0043168030 scopus 로고    scopus 로고
    • Coactivator binding promotes the specific interaction between ligand and the pregnane X receptor
    • Watkins, R. E., Davis-Searles, P. R., Lambert, M. H. and Redinbo, M. R.: Coactivator binding promotes the specific interaction between ligand and the pregnane X receptor. J. Mol. Biol., 331: 815-828 (2003).
    • (2003) J. Mol. Biol , vol.331 , pp. 815-828
    • Watkins, R.E.1    Davis-Searles, P.R.2    Lambert, M.H.3    Redinbo, M.R.4
  • 62
    • 0035076197 scopus 로고    scopus 로고
    • The peptide near the C terminus regulates receptor CAR nuclear trans-location induced by xenochemicals in mouse liver
    • Zelko, I., Sueyoshi, T., Kawamoto, T., Moore, R. and Negishi, M.: The peptide near the C terminus regulates receptor CAR nuclear trans-location induced by xenochemicals in mouse liver. Mol. Cell. Biol., 21: 2838-2846 (2001).
    • (2001) Mol. Cell. Biol , vol.21 , pp. 2838-2846
    • Zelko, I.1    Sueyoshi, T.2    Kawamoto, T.3    Moore, R.4    Negishi, M.5
  • 63
    • 0037135532 scopus 로고    scopus 로고
    • Glucocorticoid receptor-interacting protein 1 mediates ligand-independent nuclear translocation and activation of constitutive androstane receptor in vivo
    • Min, G., Kemper, J. K. and Kemper, B.: Glucocorticoid receptor-interacting protein 1 mediates ligand-independent nuclear translocation and activation of constitutive androstane receptor in vivo. J. Biol. Chem., 277: 26356-26363 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 26356-26363
    • Min, G.1    Kemper, J.K.2    Kemper, B.3
  • 64
    • 0042236405 scopus 로고    scopus 로고
    • Identification of the nuclear receptor CAR:HSP90 complex in mouse liver and recruitment of protein phosphatase 2A in response to phenobarbital
    • Yoshinari, K., Kobayashi, K., Moore, R., Kawamoto, T. and Negishi, M.: Identification of the nuclear receptor CAR:HSP90 complex in mouse liver and recruitment of protein phosphatase 2A in response to phenobarbital. FEBS Lett., 548: 17-20 (2003).
    • (2003) FEBS Lett , vol.548 , pp. 17-20
    • Yoshinari, K.1    Kobayashi, K.2    Moore, R.3    Kawamoto, T.4    Negishi, M.5
  • 65
    • 0142210183 scopus 로고    scopus 로고
    • Cytoplasmic accumulation of the nuclear receptor CAR by a tetratricopeptide repeat protein in HepG2 cells
    • Kobayashi, K., Sueyoshi, T., Inoue, K., Moore, R. and Negishi, M.: Cytoplasmic accumulation of the nuclear receptor CAR by a tetratricopeptide repeat protein in HepG2 cells. Mol. Pharmacol., 64: 1069-1075 (2003).
    • (2003) Mol Pharmacol , vol.64 , pp. 1069-1075
    • Kobayashi, K.1    Sueyoshi, T.2    Inoue, K.3    Moore, R.4    Negishi, M.5
  • 66
    • 8344219885 scopus 로고    scopus 로고
    • Cytoplasmic localization of pregnane X receptor and ligand-dependent nuclear translocation in mouse liver
    • Squires, E. J., Sueyoshi, T. and Negishi, M.: Cytoplasmic localization of pregnane X receptor and ligand-dependent nuclear translocation in mouse liver. J. Biol. Chem., 279: 49307-49314 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 49307-49314
    • Squires, E.J.1    Sueyoshi, T.2    Negishi, M.3
  • 67
    • 66449126809 scopus 로고    scopus 로고
    • Nuclear translocation of adenoviral-enhanced yellow fluorescent protein-tagged-human constitutive androstane receptor (hCAR): A novel tool for screening hCAR activators in human primary hepatocytes
    • Li, H., Chen, T., Cottrell, J. and Wang, H.: Nuclear translocation of adenoviral-enhanced yellow fluorescent protein-tagged-human constitutive androstane receptor (hCAR): A novel tool for screening hCAR activators in human primary hepatocytes. Drug Metab. Dispos., 37: 1098-1106 (2009).
    • (2009) Drug Metab. Dispos , vol.37 , pp. 1098-1106
    • Li, H.1    Chen, T.2    Cottrell, J.3    Wang, H.4
  • 68
    • 34247505536 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase is an endogenous signal retaining the nuclear constitutive active/ androstane receptor (CAR) in the cytoplasm of mouse primary hepatocytes
    • Koike, C., Moore, R. and Negishi, M.: Extracellular signal-regulated kinase is an endogenous signal retaining the nuclear constitutive active/ androstane receptor (CAR) in the cytoplasm of mouse primary hepatocytes. Mol. Pharmacol., 71: 1217-1221 (2007).
    • (2007) Mol. Pharmacol , vol.71 , pp. 1217-1221
    • Koike, C.1    Moore, R.2    Negishi, M.3
  • 69
    • 80053895720 scopus 로고    scopus 로고
    • Active ERK1/2 protein interacts with the phosphorylated nuclear constitutive active/androstane receptor (CAR; NR1I3), repressing dephosphorylation and sequestering CAR in the cytoplasm
    • Osabe, M. and Negishi, M.: Active ERK1/2 protein interacts with the phosphorylated nuclear constitutive active/androstane receptor (CAR; NR1I3), repressing dephosphorylation and sequestering CAR in the cytoplasm. J. Biol. Chem., 286: 35763-35769 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 35763-35769
    • Osabe, M.1    Negishi, M.2
  • 70
    • 33645109954 scopus 로고    scopus 로고
    • Serine 202 regulates the nuclear translocation of constitutive active/androstane receptor
    • Hosseinpour, F., Moore, R., Negishi, M. and Sueyoshi, T.: Serine 202 regulates the nuclear translocation of constitutive active/androstane receptor. Mol. Pharmacol., 69: 1095-1102 (2006).
    • (2006) Mol Pharmacol , vol.69 , pp. 1095-1102
    • Hosseinpour, F.1    Moore, R.2    Negishi, M.3    Sueyoshi, T.4
  • 71
    • 0035310906 scopus 로고    scopus 로고
    • Xenobiotic induction of cytochrome P450 2B1 (CYP2B1) is mediated by the orphan nuclear receptor constitutive androstane receptor (CAR) and requires steroid co-activator 1 (SRC-1) and the transcription factor Sp1
    • Muangmoonchai, R., Smirlis, D., Wong, S.-C., Edwards, M., Phillips, I. R. and Shephard, E. A.: Xenobiotic induction of cytochrome P450 2B1 (CYP2B1) is mediated by the orphan nuclear receptor constitutive androstane receptor (CAR) and requires steroid co-activator 1 (SRC-1) and the transcription factor Sp1. Biochem. J., 355: 71-78 (2001).
    • (2001) Biochem. J , vol.355 , pp. 71-78
    • Muangmoonchai, R.1    Smirlis, D.2    Wong, S.-C.3    Edwards, M.4    Phillips, I.R.5    Shephard, E.A.6
  • 72
    • 41149143719 scopus 로고    scopus 로고
    • PPP1R16A, the membrane subunit of protein phosphatase 1b, signals nuclear translocation of the nuclear receptor constitutive active/ androstane receptor
    • Sueyoshi, T., Moore, R., Sugatani, J., Matsumura, Y. and Negishi, M.: PPP1R16A, the membrane subunit of protein phosphatase 1b, signals nuclear translocation of the nuclear receptor constitutive active/ androstane receptor. Mol. Pharmacol., 73: 1113-1121 (2008).
    • (2008) Mol. Pharmacol , vol.73 , pp. 1113-1121
    • Sueyoshi, T.1    Moore, R.2    Sugatani, J.3    Matsumura, Y.4    Negishi, M.5
  • 73
    • 71749090253 scopus 로고    scopus 로고
    • Dephosphorylation of threonine 38 is required for nuclear translocation and activation of human xenobiotic receptor CAR (NR1I3)
    • Mutoh, S., Osabe, M., Inoue, K., Moore, R., Pedersen, L., Perera, L., Rebolloso, Y., Sueyoshi, T. and Negishi, M.: Dephosphorylation of threonine 38 is required for nuclear translocation and activation of human xenobiotic receptor CAR (NR1I3). J. Biol. Chem., 284: 34785-34792 (2009).
    • (2009) J. Biol. Chem , vol.284 , pp. 34785-34792
    • Mutoh, S.1    Osabe, M.2    Inoue, K.3    Moore, R.4    Pedersen, L.5    Perera, L.6    Rebolloso, Y.7    Sueyoshi, T.8    Negishi, M.9
  • 74
    • 74549170027 scopus 로고    scopus 로고
    • Dependence on the microtubule network and 90-kDa heat shock protein of phenobarbital-induced nuclear translocation of the rat constitutive androstane receptor
    • Kanno, Y., Miyama, Y., Ando, M. and Inouye, Y.: Dependence on the microtubule network and 90-kDa heat shock protein of phenobarbital-induced nuclear translocation of the rat constitutive androstane receptor. Mol. Pharmacol., 77: 311-316 (2010).
    • (2010) Mol. Pharmacol , vol.77 , pp. 311-316
    • Kanno, Y.1    Miyama, Y.2    Ando, M.3    Inouye, Y.4
  • 75
    • 33845881481 scopus 로고    scopus 로고
    • Relative activation of human pregnane X receptor versus constitutive androstane receptor defines distinct classes of CYP2B6 and CYP3A4 inducers
    • Faucette, S. R., Zhang, T.-C., Moore, R., Sueyoshi, T., Omiecinki, C. J., LeCluyse, E. L., Negishi, M. and Wang, H.: Relative activation of human pregnane X receptor versus constitutive androstane receptor defines distinct classes of CYP2B6 and CYP3A4 inducers. J. Pharmacol. Exp. Ther., 320: 72-80 (2007).
    • (2007) J. Pharmacol. Exp. Ther , vol.320 , pp. 72-80
    • Faucette, S.R.1    Zhang, T.-C.2    Moore, R.3    Sueyoshi, T.4    Omiecinki, C.J.5    Lecluyse, E.L.6    Negishi, M.7    Wang, H.8
  • 76
    • 15644384598 scopus 로고    scopus 로고
    • AMP-activated protein kinase mediates phenobarbital induction of CYP2B gene expression in hepatocytes and a newly derived human hepatoma cell line
    • Rencurel, F., Stenhouse, A., Hawley, S. A., Friedberg, T., Hardie, D. G., Sutherland, C. and Wolf, C. R.: AMP-activated protein kinase mediates phenobarbital induction of CYP2B gene expression in hepatocytes and a newly derived human hepatoma cell line. J. Biol. Chem., 280: 4367-4373 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 4367-4373
    • Rencurel, F.1    Stenhouse, A.2    Hawley, S.A.3    Friedberg, T.4    Hardie, D.G.5    Sutherland, C.6    Wolf, C.R.7
  • 77
    • 33751088552 scopus 로고    scopus 로고
    • Stimulation of AMP-activated protein kinase is essential for the induction of drug metabolizing enzymes by phenobarbital in human and mouse liver
    • Rencurel, F., Foretz, M., Kaufmann, M. R., Stroka, D., Looser, R., Leclerc, I., Xavier, G. S., Rutter, G. A., Viollet, B. and Meyer, U. A.: Stimulation of AMP-activated protein kinase is essential for the induction of drug metabolizing enzymes by phenobarbital in human and mouse liver. Mol. Pharmacol., 70: 1925-1934 (2006).
    • (2006) Mol Pharmacol , vol.70 , pp. 1925-1934
    • Rencurel, F.1    Foretz, M.2    Kaufmann, M.R.3    Stroka, D.4    Looser, R.5    Leclerc, I.6    Xavier, G.S.7    Rutter, G.A.8    Viollet, B.9    Meyer, U.A.10
  • 78
    • 33846886331 scopus 로고    scopus 로고
    • A physiological role of AMP-activated protein kinase in phenobarbital-mediated constitutive androstane receptor activation and CYP2B induction
    • Shindo, S., Numazawa, S. and Yoshida, T.: A physiological role of AMP-activated protein kinase in phenobarbital-mediated constitutive androstane receptor activation and CYP2B induction. Biochem. J., 401: 735-741 (2007).
    • (2007) Biochem. J , vol.401 , pp. 735-741
    • Shindo, S.1    Numazawa, S.2    Yoshida, T.3
  • 79
    • 84864018529 scopus 로고    scopus 로고
    • MicroRNA-122 down-regulation is involved in phenobarbital-mediated activation of the constitutive androstane receptor
    • Shizu, R., Shindo, S., Yoshida, T. and Numazawa, S.: MicroRNA-122 down-regulation is involved in phenobarbital-mediated activation of the constitutive androstane receptor. PLoS ONE, 7: e41291 (2012).
    • (2012) PLoS ONE , vol.7
    • Shizu, R.1    Shindo, S.2    Yoshida, T.3    Numazawa, S.4
  • 80
    • 70349308415 scopus 로고    scopus 로고
    • A systematic analysis of predicted phosphorylation sites within the human pregnane X receptor protein
    • Lichti-Kaiser, K., Brobst, D., Xu, C. and Staudinger, J. L.: A systematic analysis of predicted phosphorylation sites within the human pregnane X receptor protein. J. Pharmacol. Exp. Ther., 331: 65-76 (2009).
    • (2009) J. Pharmacol. Exp. Ther , vol.331 , pp. 65-76
    • Lichti-Kaiser, K.1    Brobst, D.2    Xu, C.3    Staudinger, J.L.4
  • 81
    • 63849272898 scopus 로고    scopus 로고
    • A phosphomimetic mutation at threonine-57 abolishes transactivation activity and alters nuclear localization pattern of human pregnane X receptor
    • Pondugula, S. R., Brimer-Cline, C., Wu, J., Schuetz, E. G., Tyagi, R. K. and Chen, T.: A phosphomimetic mutation at threonine-57 abolishes transactivation activity and alters nuclear localization pattern of human pregnane X receptor. Drug Metab. Dispos., 37: 719-730 (2009).
    • (2009) Drug Metab. Dispos , vol.37 , pp. 719-730
    • Pondugula, S.R.1    Brimer-Cline, C.2    Wu, J.3    Schuetz, E.G.4    Tyagi, R.K.5    Chen, T.6
  • 82
    • 79957729535 scopus 로고    scopus 로고
    • Post-translational modification of pregnane x receptor
    • Staudinger, J. L., Xu, C., Biswas, A. and Mani, S.: Post-translational modification of pregnane x receptor. Pharmacol. Res., 64: 4-10 (2011).
    • (2011) Pharmacol. Res , vol.64 , pp. 4-10
    • Staudinger, J.L.1    Xu, C.2    Biswas, A.3    Mani, S.4
  • 83
    • 84866465020 scopus 로고    scopus 로고
    • Regulation of pregnane X receptor (PXR) function and UGT1A1 gene expression by post-translational modification of PXR protein
    • Sugatani, J., Uchida, T., Kurosawa, M., Yamaguchi, M., Yamazaki, Y., Ikari, A. and Miwa, M.: Regulation of pregnane X receptor (PXR) function and UGT1A1 gene expression by post-translational modification of PXR protein. Drug Metab. Dispos., 40: 2031-2040 (2012).
    • (2012) Drug Metab. Dispos , vol.40 , pp. 2031-2040
    • Sugatani, J.1    Uchida, T.2    Kurosawa, M.3    Yamaguchi, M.4    Yamazaki, Y.5    Ikari, A.6    Miwa, M.7
  • 84
    • 13844253850 scopus 로고    scopus 로고
    • Repression of PXR-mediated induction of hepatic CYP3A gene expression by protein kinase C
    • Ding, X. and Staudinger, J. L.: Repression of PXR-mediated induction of hepatic CYP3A gene expression by protein kinase C. Biochem. Pharmacol., 69: 867-873 (2005).
    • (2005) Biochem. Pharmacol , vol.69 , pp. 867-873
    • Ding, X.1    Staudinger, J.L.2
  • 85
    • 65449122400 scopus 로고    scopus 로고
    • Cyclc AMP-dependent protein kinase signaling modulates pregnane x receptor activity in a species-specific manner
    • Lichti-Kaiser, K., Xu, C. and Staudinger, J. L.: Cyclc AMP-dependent protein kinase signaling modulates pregnane x receptor activity in a species-specific manner. J. Biol. Chem., 284: 6639-6649 (2009).
    • (2009) J. Biol. Chem , vol.284 , pp. 6639-6649
    • Lichti-Kaiser, K.1    Xu, C.2    Staudinger, J.L.3
  • 86
    • 73149115997 scopus 로고    scopus 로고
    • Induction of UGT1A1 and CYP2B6 by an antimitogenic factor in HepG2 cells is mediated through suppression of cyclin-dependent kinase 2 activity: Cell-cycle dependent expression
    • Sugatani, J., Osabe, M., Kurosawa, M., Kitamura, N., Ikari, A. and Miwa, M.: Induction of UGT1A1 and CYP2B6 by an antimitogenic factor in HepG2 cells is mediated through suppression of cyclin-dependent kinase 2 activity: Cell-cycle dependent expression. Drug Metab. Dispos., 38: 177-186 (2010).
    • (2010) Drug Metab. Dispos , vol.38 , pp. 177-186
    • Sugatani, J.1    Osabe, M.2    Kurosawa, M.3    Kitamura, N.4    Ikari, A.5    Miwa, M.6
  • 87
    • 57649198455 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 2 negatively regulates human pregnane X receptor-mediated CYP3A4 gene expression in HepG2 liver carcinoma cells
    • Lin, W., Wu, J., Dong, H., Bouck, D., Zeng, F.-Y. and Chen, T.: Cyclin-dependent kinase 2 negatively regulates human pregnane X receptor-mediated CYP3A4 gene expression in HepG2 liver carcinoma cells. J. Biol. Chem., 283: 30650-30657 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 30650-30657
    • Lin, W.1    Wu, J.2    Dong, H.3    Bouck, D.4    Zeng, F.-Y.5    Chen, T.6
  • 89
    • 0027184569 scopus 로고
    • PAS is a dimerization domain common to Drosophila Period and several transcription factors
    • Huang, Z. J., Edery, I. and Rosbash, M.: PAS is a dimerization domain common to Drosophila Period and several transcription factors. Nature, 364: 259-262 (1993).
    • (1993) Nature , vol.364 , pp. 259-262
    • Huang, Z.J.1    Edery, I.2    Rosbash, M.3
  • 90
    • 0029017976 scopus 로고
    • Protein-protein interaction via PAS domains: Role of the PAS domain in positive and negative regulation of the bHLH/PAS dioxin receptor-Arnt transcription factor complex
    • Lindebro, M. C., Poellinger, L. and Whitelaw, M. L.: Protein-protein interaction via PAS domains: role of the PAS domain in positive and negative regulation of the bHLH/PAS dioxin receptor-Arnt transcription factor complex. EMBO J., 14: 3528-3539 (1995).
    • (1995) EMBO J , vol.14 , pp. 3528-3539
    • Lindebro, M.C.1    Poellinger, L.2    Whitelaw, M.L.3
  • 91
    • 79952074453 scopus 로고    scopus 로고
    • Xenobiotic metabolism, disposition, and regulation by receptors: From biochemical phenomenon to predictors of major toxicities
    • Omiecinski, C. J., Heuvel, J. P. V., Perdew, G. H. and Peters, J. M.: Xenobiotic metabolism, disposition, and regulation by receptors: From biochemical phenomenon to predictors of major toxicities. Toxicol. Sci., 120: S49-S75 (2011).
    • (2011) Toxicol. Sci , vol.120
    • Omiecinski, C.J.1    Heuvel, J.P.V.2    Perdew, G.H.3    Peters, J.M.4
  • 92
    • 0141704410 scopus 로고    scopus 로고
    • Defining the role for XAP2 in stabilization of the dioxin receptor
    • Lees, M. J., Peet, D. J. and Whitelaw, M. L.: Defining the role for XAP2 in stabilization of the dioxin receptor. J. Biol. Chem., 278: 35878-35888 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 35878-35888
    • Lees, M.J.1    Peet, D.J.2    Whitelaw, M.L.3
  • 93
    • 77949911622 scopus 로고    scopus 로고
    • Activation of xenobiotic receptors: Driving into the nucleus
    • Li, H. and Wang, H.: Activation of xenobiotic receptors: driving into the nucleus. Expert Opin. Drug Metab. Toxicol., 6: 409-426 (2010).
    • (2010) Expert Opin. Drug Metab Toxicol , vol.6 , pp. 409-426
    • Li, H.1    Wang, H.2
  • 94
    • 0038236664 scopus 로고    scopus 로고
    • Involvement of the xenobotic response element (XRE) in Ah-receptor mediated induction of human UDP-glucuronosyltransferase 1A1
    • Yueh, M.-F., Huang, Y.-H., Chen, S., Nguyen, N. and Tukey, R. H.: Involvement of the xenobotic response element (XRE) in Ah-receptor mediated induction of human UDP-glucuronosyltransferase 1A1. J. Biol. Chem., 278: 15001-15006 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 15001-15006
    • Yueh, M.-F.1    Huang, Y.-H.2    Chen, S.3    Nguyen, N.4    Tukey, R.H.5
  • 95
    • 38949097735 scopus 로고    scopus 로고
    • The search for endogenous activators of the aryl hydrocarbon receptor
    • Nguyen, L. P. and Bradfield, C. A.: The search for endogenous activators of the aryl hydrocarbon receptor. Chem. Res. Toxicol., 21: 102-116 (2008).
    • (2008) Chem. Res. Toxicol , vol.21 , pp. 102-116
    • Nguyen, L.P.1    Bradfield, C.A.2
  • 96
    • 57349122123 scopus 로고    scopus 로고
    • 12(R)-Hydroxy-5(Z),8(Z),10(E),14(Z)-eicosatetraenoic acid [12(R)-HETE], an arach-idonic acid derivative, is an activator of the aryl hydrocarbon receptor
    • Chiaro, C. R., Patel, R. D. and Perdew, G. H.: 12(R)-Hydroxy-5(Z),8(Z),10(E),14(Z)-eicosatetraenoic acid [12(R)-HETE], an arach-idonic acid derivative, is an activator of the aryl hydrocarbon receptor. Mol. Pharmacol., 74: 1649-1656 (2008).
    • (2008) Mol. Pharmacol , vol.74 , pp. 1649-1656
    • Chiaro, C.R.1    Patel, R.D.2    Perdew, G.H.3
  • 97
    • 77952569598 scopus 로고    scopus 로고
    • Molecular mechanism of the physiological functions of the aryl hydrocarbon (dioxin) receptor, a multifunctional regulator that senses and responds to environmental stimuli
    • Fujii-Kuriyama, Y. and Kawajiri, K.: Molecular mechanism of the physiological functions of the aryl hydrocarbon (dioxin) receptor, a multifunctional regulator that senses and responds to environmental stimuli. Proc. Jpn. Acad. Ser. B, 86: 40-53 (2010).
    • (2010) Proc. Jpn. Acad. Ser. B , vol.86 , pp. 40-53
    • Fujii-Kuriyama, Y.1    Kawajiri, K.2
  • 98
    • 34247869082 scopus 로고    scopus 로고
    • Nrf2-Keap1 signaling pathway regulates human UGT1A1 expression in vitro and in transgenic UGT1 mice
    • Yueh, M.-F. and Tukey, R. H.: Nrf2-Keap1 signaling pathway regulates human UGT1A1 expression in vitro and in transgenic UGT1 mice. J. Biol. Chem., 282: 8749-8758 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 8749-8758
    • Yueh, M.-F.1    Tukey, R.H.2
  • 99
    • 2342511435 scopus 로고    scopus 로고
    • Small Maf proteins serve as transcriptional cofactors for keratinocyte differentiation in the Keap1-Nrf2 regulatory pathway
    • Motohashi, H., Katsuoka, F., Engel, J. D. and Yamamoto, M.: Small Maf proteins serve as transcriptional cofactors for keratinocyte differentiation in the Keap1-Nrf2 regulatory pathway. Proc. Natl. Acad. Sci. USA, 101: 6379-6384 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6379-6384
    • Motohashi, H.1    Katsuoka, F.2    Engel, J.D.3    Yamamoto, M.4
  • 100
    • 5144232811 scopus 로고    scopus 로고
    • Chemoprevention through the Keap1-Nrf2 signaling pathway by phase 2 enzyme inducers
    • Kwak, M.-K., Wakabayashi, N. and Kensler, T. W.: Chemoprevention through the Keap1-Nrf2 signaling pathway by phase 2 enzyme inducers. Mutat. Res., 555: 133-148 (2004).
    • (2004) Mutat Res , vol.555 , pp. 133-148
    • Kwak, M.-K.1    Wakabayashi, N.2    Kensler, T.W.3
  • 102
    • 20144385916 scopus 로고    scopus 로고
    • Transcriptional regulation of NF-E2 p45-related factor (NRF2) expression by the aryl hydrocarbon receptor-xenobiotic response element signaling pathway
    • Miao, W., Hu, L., Serivens, P. J. and Batist, G.: Transcriptional regulation of NF-E2 p45-related factor (NRF2) expression by the aryl hydrocarbon receptor-xenobiotic response element signaling pathway. J. Biol. Chem., 280: 20340-20348 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 20340-20348
    • Miao, W.1    Hu, L.2    Serivens, P.J.3    Batist, G.4
  • 104
    • 0032831896 scopus 로고    scopus 로고
    • Antioxidant response elementmediated 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) induction of human NAD(P)H;quinone oxidoreductase 1 gene expression
    • Radjendirane, V. and Jaiswal, A. K.: Antioxidant response elementmediated 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) induction of human NAD(P)H;quinone oxidoreductase 1 gene expression. Biochem. Pharmacol., 58: 1649-1655 (1999).
    • (1999) Biochem. Pharmacol , vol.58 , pp. 1649-1655
    • Radjendirane, V.1    Jaiswal, A.K.2
  • 105
    • 77949901726 scopus 로고    scopus 로고
    • Interaction between oxidative stress sensor Nrf2 and xenobiotic-activated aryl hydrocarbon receptor in the regulation of the human phase II detoxifying UDP-glucuronosyltransferase 1A10
    • Kalthoff, S., Ehmer, U., Freiberg, N., Manns, M. P. and Strassburg, C. P.: Interaction between oxidative stress sensor Nrf2 and xenobiotic-activated aryl hydrocarbon receptor in the regulation of the human phase II detoxifying UDP-glucuronosyltransferase 1A10. J. Biol. Chem., 285: 5993-6002 (2010).
    • (2010) J. Biol. Chem , vol.285 , pp. 5993-6002
    • Kalthoff, S.1    Ehmer, U.2    Freiberg, N.3    Manns, M.P.4    Strassburg, C.P.5
  • 106
    • 0028922238 scopus 로고
    • Drug-responsive and tissue-specific alternative expression of multiple first exons in rat UDP-glucuronosyltransferase family 1 (UGT1) gene complex
    • Emi, Y., Ikushiro, S. and Iyanagi, T.: Drug-responsive and tissue-specific alternative expression of multiple first exons in rat UDP-glucuronosyltransferase family 1 (UGT1) gene complex. J. Biochem., 117: 392-399 (1995).
    • (1995) J. Biochem , vol.117 , pp. 392-399
    • Emi, Y.1    Ikushiro, S.2    Iyanagi, T.3
  • 107
    • 0036079698 scopus 로고    scopus 로고
    • In vitro induction of bilirubin conjugation in primary rat hepatocyte culture
    • Jemnitz, K., Lengyel, G. and Vereczkey, L.: In vitro induction of bilirubin conjugation in primary rat hepatocyte culture. Biochem. Biophys. Res. Commun., 291: 29-33 (2002).
    • (2002) Biochem. Biophys. Res. Commun , vol.291 , pp. 29-33
    • Jemnitz, K.1    Lengyel, G.2    Vereczkey, L.3
  • 108
    • 0022981876 scopus 로고
    • In vivo protein-DNA interaction in a glucocorticoid response element require the presence of the hormone
    • Becker, P. B., Glose, B., Schmid, W., Strahle, U. and Schutz, G.: In vivo protein-DNA interaction in a glucocorticoid response element require the presence of the hormone. Nature, 324: 686-688 (1986).
    • (1986) Nature , vol.324 , pp. 686-688
    • Becker, P.B.1    Glose, B.2    Schmid, W.3    Strahle, U.4    Schutz, G.5
  • 109
    • 0029943273 scopus 로고    scopus 로고
    • Visualization of glucocorticoid receptor translocation and intranuclear organization in living cells with a green fluorescent protein chimera
    • Htun, H., Barsony, J., Renyi, I., Gould, D. L. and Hager, G. L.: Visualization of glucocorticoid receptor translocation and intranuclear organization in living cells with a green fluorescent protein chimera. Proc. Natl. Acad. Sci. USA, 93: 4845-4850 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4845-4850
    • Htun, H.1    Barsony, J.2    Renyi, I.3    Gould, D.L.4    Hager, G.L.5
  • 111
    • 38749132313 scopus 로고    scopus 로고
    • Expression of hepatic UDP-glucuronosyltransferase 1A1 and 1A6 correlated with increased expression of the nuclear constitutive androstane receptor and peroxisome proliferator-activated receptor α in male rats fed a high-fat and high-sucrose diet
    • Osabe, M., Sugatani, J., Fukuyama, T., Ikushiro, S., Ikari, A. and Miwa, M.: Expression of hepatic UDP-glucuronosyltransferase 1A1 and 1A6 correlated with increased expression of the nuclear constitutive androstane receptor and peroxisome proliferator-activated receptor α in male rats fed a high-fat and high-sucrose diet. Drug Metab. Dispos., 36: 294-302 (2008).
    • (2008) Drug Metab. Dispos , vol.36 , pp. 294-302
    • Osabe, M.1    Sugatani, J.2    Fukuyama, T.3    Ikushiro, S.4    Ikari, A.5    Miwa, M.6
  • 112
    • 33847421803 scopus 로고    scopus 로고
    • Expression of the human UGT1 locus in transgenic mice by 4-chloro-6-(2,3-xylidino)-2-pyrimidinylth-ioacetic acid (WY-14643) and implications on drug metabolism through peroxisome proliferators-activated receptor α activation
    • Senekeo-Effenberger, K., Chen, S., Brace-Sinnokrak, E., Bonzo, J. A., Yueh, M.-F., Argikar, U., Kaeding, J., Trottier, J., Remmei, R. P., Ritter, J. K., Barbier, O. and Tukey, R. H.: Expression of the human UGT1 locus in transgenic mice by 4-chloro-6-(2,3-xylidino)-2-pyrimidinylth-ioacetic acid (WY-14643) and implications on drug metabolism through peroxisome proliferators-activated receptor α activation. Drug Metab. Dispos., 35: 419-427 (2007).
    • (2007) Drug Metab. Dispos , vol.35 , pp. 419-427
    • Senekeo-Effenberger, K.1    Chen, S.2    Brace-Sinnokrak, E.3    Bonzo, J.A.4    Yueh, M.-F.5    Argikar, U.6    Kaeding, J.7    Trottier, J.8    Remmei, R.P.9    Ritter, J.K.10    Barbier, O.11    Tukey, R.H.12
  • 113
    • 0034713444 scopus 로고    scopus 로고
    • Roles of PPARs in health and disease
    • Kersten, S., Desvergne, B. and Wahli, W.: Roles of PPARs in health and disease. Nature, 405: 421-424 (2000).
    • (2000) Nature , vol.405 , pp. 421-424
    • Kersten, S.1    Desvergne, B.2    Wahli, W.3
  • 114
    • 34250731775 scopus 로고    scopus 로고
    • Cytochrome P450 eicosanoids are activators of peroxisome proliferator-activated receptor α
    • Ng, V. Y., Huang, Y., Reddy, L. M., Falck, J. R., Lin, E. T. and Kroetz, D. L.: Cytochrome P450 eicosanoids are activators of peroxisome proliferator-activated receptor α. Drug Metab. Dispos., 35: 1126-1134 (2007).
    • (2007) Drug Metab. Dispos , vol.35 , pp. 1126-1134
    • Ng, V.Y.1    Huang, Y.2    Reddy, L.M.3    Falck, J.R.4    Lin, E.T.5    Kroetz, D.L.6
  • 115
    • 45849117263 scopus 로고    scopus 로고
    • Transcriptional regulation of human UGT1A1 gene expression through distal and proximal promoter motifs: Implication of defects in the UGT1A1 gene promoter
    • Sugatani, J., Mizushima, K., Osabe, M., Yamakawa, K., Kakizaki, S., Takagi, H., Mori, M., Ikari, A. and Miwa, M.: Transcriptional regulation of human UGT1A1 gene expression through distal and proximal promoter motifs: implication of defects in the UGT1A1 gene promoter. Naunyn Schmiedebergs Arch. Pharmacol., 377(4-6): 597-605 (2008).
    • (2008) Naunyn Schmiedebergs Arch. Pharmacol , vol.377 , Issue.4-6 , pp. 597-605
    • Sugatani, J.1    Mizushima, K.2    Osabe, M.3    Yamakawa, K.4    Kakizaki, S.5    Takagi, H.6    Mori, M.7    Ikari, A.8    Miwa, M.9
  • 116
    • 77649322609 scopus 로고    scopus 로고
    • Regulation of UGT1A1 and HNF1 transcription factor gene expression by DNA methylation in colon cancer cells
    • Bélanger, A.-S., Tojcic, J., Harvey, M. and Guillemette, C.: Regulation of UGT1A1 and HNF1 transcription factor gene expression by DNA methylation in colon cancer cells. BMC Mol. Biol., 11: 9 (2010).
    • (2010) BMC Mol. Biol , vol.11 , pp. 9
    • Bélanger, A.-S.1    Tojcic, J.2    Harvey, M.3    Guillemette, C.4
  • 117
    • 34848824067 scopus 로고    scopus 로고
    • Role of human hepatocyte nuclear factor 4α in the expression of drug-metabolizing enzymes and transporters in human hepatocytes assessed by use of small interfering RNA
    • Kamiyama, Y., Matsubara, T., Yoshinari, K., Nagata, K., Kamimura, H. and Yamazoe, Y.: Role of human hepatocyte nuclear factor 4α in the expression of drug-metabolizing enzymes and transporters in human hepatocytes assessed by use of small interfering RNA. Drug Metab. Pharmacokinet., 22: 287-298 (2007).
    • (2007) Drug Metab. Pharmacokinet , vol.22 , pp. 287-298
    • Kamiyama, Y.1    Matsubara, T.2    Yoshinari, K.3    Nagata, K.4    Kamimura, H.5    Yamazoe, Y.6
  • 118
    • 38449087463 scopus 로고    scopus 로고
    • Hepatocyte nuclear factor 1 alpha and 4 alpha are factors involved in interindividual variability in the expression of UGT1A6 and UGT1A9 but not UGT1A1, UGT1A3, and UGT1A4 mRNA in human livers
    • Aueviriyavit, S., Furihata, T., Morimoto, K., Kobayashi, K. and Chiba, K.: Hepatocyte nuclear factor 1 alpha and 4 alpha are factors involved in interindividual variability in the expression of UGT1A6 and UGT1A9 but not UGT1A1, UGT1A3, and UGT1A4 mRNA in human livers. Drug Metab. Pharmacokinet., 22: 391-398 (2007).
    • (2007) Drug Metab. Pharmacokinet , vol.22 , pp. 391-398
    • Aueviriyavit, S.1    Furihata, T.2    Morimoto, K.3    Kobayashi, K.4    Chiba, K.5
  • 119
    • 33748750262 scopus 로고    scopus 로고
    • Regulation of constitutive androstane receptor and its target genes by fasting, cAMP, hepatocyte nuclear factor α, and the coactivator peroxisome proliferator-activated receptor g coactivator-1α
    • Ding, X., Lichti, K., Kim, I., Gonzalez, F. J. and Staudinger, J. L.: Regulation of constitutive androstane receptor and its target genes by fasting, cAMP, hepatocyte nuclear factor α, and the coactivator peroxisome proliferator-activated receptor g coactivator-1α J. Biol. Chem., 281(36): 26540-26551 (2006).
    • (2006) J. Biol. Chem , vol.281 , Issue.36 , pp. 26540-26551
    • Ding, X.1    Lichti, K.2    Kim, I.3    Gonzalez, F.J.4    Staudinger, J.L.5
  • 121
    • 79958815033 scopus 로고    scopus 로고
    • Garlic extract diallyl sulfide (DAS) activates nuclear receptor CAR to induce the Sult1e1 gene in mouse liver
    • Sueyoshi, T., Green, W. D., Vinal, K., Woodrum, T. S., Moore, R. and Negishi, M.: Garlic extract diallyl sulfide (DAS) activates nuclear receptor CAR to induce the Sult1e1 gene in mouse liver. PLoS ONE, 6: e21229 (2011).
    • (2011) PLoS ONE , vol.6
    • Sueyoshi, T.1    Green, W.D.2    Vinal, K.3    Woodrum, T.S.4    Moore, R.5    Negishi, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.