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Volumn 35, Issue 5, 2007, Pages 747-757

Effects of coexpression of UGT1A9 on enzymatic activities of human UGT1A isoforms

Author keywords

[No Author keywords available]

Indexed keywords

DETERGENT; ESTRADIOL; ESTRADIOL O GLUCURONIDE; GLUCURONOSYLTRANSFERASE 1A1; GLUCURONOSYLTRANSFERASE 1A4; GLUCURONOSYLTRANSFERASE 1A6; GLUCURONOSYLTRANSFERASE 1A9; IMIPRAMINE; IMIPRAMINE N GLUCURONIDE; PROPOFOL; PROPOFOL O GLUCURONIDE; SEROTONIN; SEROTONIN O GLUCURONIDE; TRITON X 100; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE GLUCURONIC ACID;

EID: 34247379533     PISSN: 00909556     EISSN: 1521009X     Source Type: Journal    
DOI: 10.1124/dmd.106.014191     Document Type: Article
Times cited : (67)

References (33)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 2
    • 0026505255 scopus 로고
    • Sequence of exons and the flanking regions of human bilirubin-UDP-glucuronosyltransferase gene complex and identification of a genetic mutation in a patient with Crigler-Najjar syndrome, type I
    • Bosma PJ, Chowdhury NR, Goldhoorn BG, Hofker MH, Oude Elferink RP, Jansen PL, and Chowdhury JR (1992) Sequence of exons and the flanking regions of human bilirubin-UDP-glucuronosyltransferase gene complex and identification of a genetic mutation in a patient with Crigler-Najjar syndrome, type I. Hepatology 15:941-947.
    • (1992) Hepatology , vol.15 , pp. 941-947
    • Bosma, P.J.1    Chowdhury, N.R.2    Goldhoorn, B.G.3    Hofker, M.H.4    Oude Elferink, R.P.5    Jansen, P.L.6    Chowdhury, J.R.7
  • 3
    • 0008451644 scopus 로고
    • Acceptor substrates of UDP glucuronosyltransferase and their assay
    • Dutton GJ ed pp, CRC Press, Boca Raton, FL
    • Dutton GJ (1980) Acceptor substrates of UDP glucuronosyltransferase and their assay, in Glucuronidation of Drugs and Other Compounds (Dutton GJ ed) pp 69-78, CRC Press, Boca Raton, FL.
    • (1980) Glucuronidation of Drugs and Other Compounds , pp. 69-78
    • Dutton, G.J.1
  • 6
    • 0028116221 scopus 로고
    • Radiation inactivation analysis of microsomal UDP-glucuronosyltransferases catalysing mono- and diglucuronide formation of 3,6-dihydroxybenzo(a)pyrene and 3,6-dihydroxychrysene
    • Gschaidmeier H and Bock KW (1994) Radiation inactivation analysis of microsomal UDP-glucuronosyltransferases catalysing mono- and diglucuronide formation of 3,6-dihydroxybenzo(a)pyrene and 3,6-dihydroxychrysene. Biochem Pharmacol 48:1545-1549.
    • (1994) Biochem Pharmacol , vol.48 , pp. 1545-1549
    • Gschaidmeier, H.1    Bock, K.W.2
  • 7
    • 0031661763 scopus 로고    scopus 로고
    • +-glucuronidation, a common pathway in human metabolism of drugs with a tertiary amine group
    • +-glucuronidation, a common pathway in human metabolism of drugs with a tertiary amine group. Drug Metab Dispos 26:830-837.
    • (1998) Drug Metab Dispos , vol.26 , pp. 830-837
    • Hawes, E.M.1
  • 8
    • 0037417869 scopus 로고    scopus 로고
    • Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases
    • Hu Y, Chen L, Ha S, Gross B, Falcone B, Walker D, Mokhtarzadeh M, and Walker S (2003) Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases. Proc Natl Acad Sci USA 100:845-849.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 845-849
    • Hu, Y.1    Chen, L.2    Ha, S.3    Gross, B.4    Falcone, B.5    Walker, D.6    Mokhtarzadeh, M.7    Walker, S.8
  • 9
    • 33645995117 scopus 로고    scopus 로고
    • Monospecific antipeptide antibodies against human hepatic UDP-glucuronosyltransferase 1A subfamily (UGT1A) isoforms
    • Ikushiro S, Emi Y, Kato Y, Yamada S, and Sakaki T (2006) Monospecific antipeptide antibodies against human hepatic UDP-glucuronosyltransferase 1A subfamily (UGT1A) isoforms. Drug Metab Pharmacokinet 21:70-74.
    • (2006) Drug Metab Pharmacokinet , vol.21 , pp. 70-74
    • Ikushiro, S.1    Emi, Y.2    Kato, Y.3    Yamada, S.4    Sakaki, T.5
  • 10
    • 0031010059 scopus 로고    scopus 로고
    • Protein-protein interactions between UDP-glucuronosyltransferase isozymes in rat hepatic microsomes
    • Ikushiro S, Emi Y, and Iyanagi T (1997) Protein-protein interactions between UDP-glucuronosyltransferase isozymes in rat hepatic microsomes. Biochemistry 36:7154-7161.
    • (1997) Biochemistry , vol.36 , pp. 7154-7161
    • Ikushiro, S.1    Emi, Y.2    Iyanagi, T.3
  • 11
    • 0034752769 scopus 로고    scopus 로고
    • Simultaneous expression of guinea pig UDP-glucuronosyltransferase 2B21 and 2B22 in COS-7 cells enhances UDP-glucuronosyltransferase 2B21-catalyzed morphine-6-glucuronide formation
    • Ishii Y, Miyoshi A, Watanabe R, Tsuruda K, Tsuda M, Yamaguchi-Nagamatsu Y, Yoshisue K, Tanaka M, Maji D, Ohgiya S, et al. (2001) Simultaneous expression of guinea pig UDP-glucuronosyltransferase 2B21 and 2B22 in COS-7 cells enhances UDP-glucuronosyltransferase 2B21-catalyzed morphine-6-glucuronide formation. Mol Pharmacol 60:1040-1048.
    • (2001) Mol Pharmacol , vol.60 , pp. 1040-1048
    • Ishii, Y.1    Miyoshi, A.2    Watanabe, R.3    Tsuruda, K.4    Tsuda, M.5    Yamaguchi-Nagamatsu, Y.6    Yoshisue, K.7    Tanaka, M.8    Maji, D.9    Ohgiya, S.10
  • 12
    • 0038685671 scopus 로고    scopus 로고
    • Validation of serotonin (5-hydroxtryptamine) as an in vitro substrate probe for human UDP-glucuronosyltransferase (UGT) 1A6
    • Krishnaswamy S, Duan SX, Von Moltke LL, Greenblatt DJ, and Court MH (2003) Validation of serotonin (5-hydroxtryptamine) as an in vitro substrate probe for human UDP-glucuronosyltransferase (UGT) 1A6. Drug Metab Dispos 31:133-139.
    • (2003) Drug Metab Dispos , vol.31 , pp. 133-139
    • Krishnaswamy, S.1    Duan, S.X.2    Von Moltke, L.L.3    Greenblatt, D.J.4    Court, M.H.5
  • 13
    • 0037423299 scopus 로고    scopus 로고
    • Expression and characterization of recombinant human UDP-glucuronosyltransferases (UGTs): UGT1A9 is more resistant to detergent inhibition than the other UGTs and was purified as an active dimeric enzyme
    • Kurkela M, Garcia-Horsman JA, Luukkanen L, Morsky S, Taskinen J, Baumann M, Kostiainen R, Hirvonen J, and Finel M (2003) Expression and characterization of recombinant human UDP-glucuronosyltransferases (UGTs): UGT1A9 is more resistant to detergent inhibition than the other UGTs and was purified as an active dimeric enzyme. J Biol Chem 278:3536-3544.
    • (2003) J Biol Chem , vol.278 , pp. 3536-3544
    • Kurkela, M.1    Garcia-Horsman, J.A.2    Luukkanen, L.3    Morsky, S.4    Taskinen, J.5    Baumann, M.6    Kostiainen, R.7    Hirvonen, J.8    Finel, M.9
  • 14
    • 8844283291 scopus 로고    scopus 로고
    • The interactions between the N-terminal and C-terminal domains of the human UDP- glucuronosyltransferases are partly isoform-specific and may involve both monomers
    • Kurkela M, Hirvonen J, Kostiainen R, and Finel M (2004) The interactions between the N-terminal and C-terminal domains of the human UDP- glucuronosyltransferases are partly isoform-specific and may involve both monomers. Biochem Pharmacol 68:2443-2450.
    • (2004) Biochem Pharmacol , vol.68 , pp. 2443-2450
    • Kurkela, M.1    Hirvonen, J.2    Kostiainen, R.3    Finel, M.4
  • 15
    • 6344248683 scopus 로고    scopus 로고
    • Specificity and regioselectivity of the conjugation of estradiol, estrone, and their catecholestrogen and methoxyestrogen metabolites by human uridine diphosphoglucuronosyltransferases expressed in endometrium
    • Lepine J, Bernard O, Plante M, Tetu B, Pelletier G, Labrie F, Belanger A, and Guillemette C (2004) Specificity and regioselectivity of the conjugation of estradiol, estrone, and their catecholestrogen and methoxyestrogen metabolites by human uridine diphosphoglucuronosyltransferases expressed in endometrium. J Clin Endocrinol Metab 89:5222-5232.
    • (2004) J Clin Endocrinol Metab , vol.89 , pp. 5222-5232
    • Lepine, J.1    Bernard, O.2    Plante, M.3    Tetu, B.4    Pelletier, G.5    Labrie, F.6    Belanger, A.7    Guillemette, C.8
  • 16
    • 0030895678 scopus 로고    scopus 로고
    • Characterization of 1-hydroxypyrene as a novel marker substrate of 3-methylcholanthrene-inducible phenol UDP-glucuronosyltransferase(s)
    • Luukkanen L, Elovaara E, Lautala P, Taskinen J, and Vainio H (1997) Characterization of 1-hydroxypyrene as a novel marker substrate of 3-methylcholanthrene-inducible phenol UDP-glucuronosyltransferase(s). Pharmacol Toxicol 80:152-158.
    • (1997) Pharmacol Toxicol , vol.80 , pp. 152-158
    • Luukkanen, L.1    Elovaara, E.2    Lautala, P.3    Taskinen, J.4    Vainio, H.5
  • 17
    • 0025236448 scopus 로고
    • Expression of chimeric cDNAs in cell culture defines a region of UDP glucuronosyltransferase involved in substrate selection
    • Mackenzie PI (1990) Expression of chimeric cDNAs in cell culture defines a region of UDP glucuronosyltransferase involved in substrate selection. J Biol Chem 265:3432-3435.
    • (1990) J Biol Chem , vol.265 , pp. 3432-3435
    • Mackenzie, P.I.1
  • 19
    • 4243182634 scopus 로고    scopus 로고
    • Human UDP-glucuronosyltransferase 1A1 is the primary enzyme responsible for the N-glucuronidation of N-hydroxy-PhIP in vitro
    • Malfatti MA, and Felton JS (2004) Human UDP-glucuronosyltransferase 1A1 is the primary enzyme responsible for the N-glucuronidation of N-hydroxy-PhIP in vitro. Chem Res Toxicol 17:1137-1144.
    • (2004) Chem Res Toxicol , vol.17 , pp. 1137-1144
    • Malfatti, M.A.1    Felton, J.S.2
  • 20
    • 0020287243 scopus 로고
    • Isolation and characterization of rat liver microsomal UDP-glucuronosyltransferase activity toward chenodeoxycholic acid and testosterone as a single form of enzyme
    • Matern H, Matern S, and Gerok W (1982) Isolation and characterization of rat liver microsomal UDP-glucuronosyltransferase activity toward chenodeoxycholic acid and testosterone as a single form of enzyme. J Biol Chem 257:7422-7429.
    • (1982) J Biol Chem , vol.257 , pp. 7422-7429
    • Matern, H.1    Matern, S.2    Gerok, W.3
  • 21
    • 0041422391 scopus 로고    scopus 로고
    • Structure of the TDP-epi-vancosaminyltransferase GtfA from the chloroeremomycin biosynthetic pathway
    • Mulichak AM, Losey HC, Lu W, Wawrzak Z, Walsh CT, and Garavito RM (2003) Structure of the TDP-epi-vancosaminyltransferase GtfA from the chloroeremomycin biosynthetic pathway. Proc Natl Acad Sci USA 100:9238-9243.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 9238-9243
    • Mulichak, A.M.1    Losey, H.C.2    Lu, W.3    Wawrzak, Z.4    Walsh, C.T.5    Garavito, R.M.6
  • 22
    • 0036266825 scopus 로고    scopus 로고
    • Imipramine N-glucuronidation in human liver microsomes: Biphasic kinetics and characterization of UDP-glucuronosyltransferase isoforms
    • Nakajima M, Tanaka E, Kobayashi T, Ohashi N, Kume T, and Yokoi T (2002) Imipramine N-glucuronidation in human liver microsomes: biphasic kinetics and characterization of UDP-glucuronosyltransferase isoforms. Drug Metab Dispos 30:636-642.
    • (2002) Drug Metab Dispos , vol.30 , pp. 636-642
    • Nakajima, M.1    Tanaka, E.2    Kobayashi, T.3    Ohashi, N.4    Kume, T.5    Yokoi, T.6
  • 23
    • 0021133988 scopus 로고
    • The molecular weights of UDP-glucuronyltransferase determined with radiation-inactivation analysis. a molecular model of bilirubin UDPglucuronyltransferase
    • Peters WH, Jansen PL, and Nauta H (1984) The molecular weights of UDP-glucuronyltransferase determined with radiation-inactivation analysis. a molecular model of bilirubin UDPglucuronyltransferase. J Biol Chem 259:11701-11705.
    • (1984) J Biol Chem , vol.259 , pp. 11701-11705
    • Peters, W.H.1    Jansen, P.L.2    Nauta, H.3
  • 24
    • 33646234012 scopus 로고    scopus 로고
    • Biosynthesis of imipramine glucuronide and characterization of imipramine glucuronidation catalyzed by recombinant UGT1A4
    • Qian MR and Zeng S (2006) Biosynthesis of imipramine glucuronide and characterization of imipramine glucuronidation catalyzed by recombinant UGT1A4. Acta Pharmacol Sin 27:623-628.
    • (2006) Acta Pharmacol Sin , vol.27 , pp. 623-628
    • Qian, M.R.1    Zeng, S.2
  • 25
    • 0033783035 scopus 로고    scopus 로고
    • O-Glucuronidation of the lung carcinogen 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanol (NNAL) by human UDP-glucuronosyltransferases 2B7 and 1A9
    • Ren Q, Murphy SE, Zheng Z, and Lazarus P (2000) O-Glucuronidation of the lung carcinogen 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanol (NNAL) by human UDP-glucuronosyltransferases 2B7 and 1A9. Drug Metab Dispos 28:1352-1360.
    • (2000) Drug Metab Dispos , vol.28 , pp. 1352-1360
    • Ren, Q.1    Murphy, S.E.2    Zheng, Z.3    Lazarus, P.4
  • 26
    • 0026701911 scopus 로고
    • A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini
    • Ritter JK, Chen F, Sheen YY, Tran HM, Kimura S, Yeatman MT, and Owens IS (1992) A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini. J Biol Chem 267:3257-3261.
    • (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
  • 27
    • 0028283149 scopus 로고
    • Thermal inactivation of tryptophan synthase. Stabilization by protein-protein interaction and protein-ligand interaction
    • Ruvinov SB and Miles EW (1994) Thermal inactivation of tryptophan synthase. Stabilization by protein-protein interaction and protein-ligand interaction. J Biol Chem 269:11703-11706.
    • (1994) J Biol Chem , vol.269 , pp. 11703-11706
    • Ruvinov, S.B.1    Miles, E.W.2
  • 28
    • 0042768143 scopus 로고    scopus 로고
    • Glucuronidation of propofol and its analogs by human and rat liver microsomes
    • Shimizu M, Matsumoto Y, Tatsuno M, and Fukuoka M (2003) Glucuronidation of propofol and its analogs by human and rat liver microsomes. Biol Pharm Bull 26:216-219.
    • (2003) Biol Pharm Bull , vol.26 , pp. 216-219
    • Shimizu, M.1    Matsumoto, Y.2    Tatsuno, M.3    Fukuoka, M.4
  • 29
    • 0038532316 scopus 로고    scopus 로고
    • The effect of incubation conditions on the enzyme kinetics of UDP-glucuronosyltransferases
    • Soars MG, Ring BJ, and Wrighton SA (2003) The effect of incubation conditions on the enzyme kinetics of UDP-glucuronosyltransferases. Drug Metab Dispos 31:762-767.
    • (2003) Drug Metab Dispos , vol.31 , pp. 762-767
    • Soars, M.G.1    Ring, B.J.2    Wrighton, S.A.3
  • 30
  • 31
    • 0034128936 scopus 로고    scopus 로고
    • Human UDP-glucuronosyltransferases: Metabolism, expression and disease
    • Tukey RH and Strassburg CP (2000) Human UDP-glucuronosyltransferases: metabolism, expression and disease. Annu Rev Pharmacol Toxicol 40:581-616.
    • (2000) Annu Rev Pharmacol Toxicol , vol.40 , pp. 581-616
    • Tukey, R.H.1    Strassburg, C.P.2
  • 32
    • 1842536833 scopus 로고    scopus 로고
    • Human UDP-glucuronosyltransferases, isoform selectivity and kinetics of 4-methylumbelliferone and 1-naphthol glucuronidation, effects of organic solvents, and inhibition by diclofenac and probenecid
    • Uchaipichat V, Mackenzie PI, Guo XH, Gardner-Stephen D, Galetin A, Houston JB, and Miners JO (2004) Human UDP-glucuronosyltransferases, isoform selectivity and kinetics of 4-methylumbelliferone and 1-naphthol glucuronidation, effects of organic solvents, and inhibition by diclofenac and probenecid. Drug Metab Dispos 32:413-423.
    • (2004) Drug Metab Dispos , vol.32 , pp. 413-423
    • Uchaipichat, V.1    Mackenzie, P.I.2    Guo, X.H.3    Gardner-Stephen, D.4    Galetin, A.5    Houston, J.B.6    Miners, J.O.7
  • 33
    • 33344473930 scopus 로고    scopus 로고
    • Selectivity of substrate (trifluoperazine) and inhibitor (amitriptyline, androsterone, canrenoic acid, hecogenin, phenylbutazone, quinidine, quinine, and sulfinpyrazone) "probes" for human UDP-glucuronosyltransferases
    • Uchaipichat V, Mackenzie PI, Elliot DJ, and Miners JO (2006) Selectivity of substrate (trifluoperazine) and inhibitor (amitriptyline, androsterone, canrenoic acid, hecogenin, phenylbutazone, quinidine, quinine, and sulfinpyrazone) "probes" for human UDP-glucuronosyltransferases. Drug Metab Dispos 34:449-456.
    • (2006) Drug Metab Dispos , vol.34 , pp. 449-456
    • Uchaipichat, V.1    Mackenzie, P.I.2    Elliot, D.J.3    Miners, J.O.4


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