메뉴 건너뛰기




Volumn 38, Issue 10, 2010, Pages 1785-1789

Alternatively spliced products of the UGT1A gene interact with the enzymatically active proteins to inhibit glucuronosyltransferase activity in vitro

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC G 418; BLASTICIDIN S; DRUG METABOLIZING ENZYME; GLUCURONOSYLTRANSFERASE; GLUCURONOSYLTRANSFERASE 1A1; GLUCURONOSYLTRANSFERASE 1A10; GLUCURONOSYLTRANSFERASE 1A3; GLUCURONOSYLTRANSFERASE 1A4; GLUCURONOSYLTRANSFERASE 1A6; GLUCURONOSYLTRANSFERASE 1A7; GLUCURONOSYLTRANSFERASE 1A8; GLUCURONOSYLTRANSFERASE 1A9; GLYCOSYLTRANSFERASE; ISOPROTEIN; PROTEIN; TRANSFERASE; UDP GLUCURONOSYLTRANFERASE A1; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE GLUCURONIC ACID;

EID: 77957173109     PISSN: 00909556     EISSN: 1521009X     Source Type: Journal    
DOI: 10.1124/dmd.110.034835     Document Type: Article
Times cited : (22)

References (28)
  • 1
    • 77950501858 scopus 로고    scopus 로고
    • Modulation of the human glucuronosyltransferase UGT1A pathway by splice isoform polypeptides is mediated through protein-protein interactions
    • Bellemare J, Rouleau M, Harvey M, and Guillemette C (2010) Modulation of the human glucuronosyltransferase UGT1A pathway by splice isoform polypeptides is mediated through protein-protein interactions. J Biol Chem 285:3600-3607.
    • (2010) J Biol Chem , vol.285 , pp. 3600-3607
    • Bellemare, J.1    Rouleau, M.2    Harvey, M.3    Guillemette, C.4
  • 2
    • 77957140215 scopus 로고    scopus 로고
    • Alternative-splicing forms of the major phase II conjugating UGT1A gene negatively regulate glucuronidation in human carcinoma cell lines
    • doi:10.1038/tpj.2009.64
    • Bellemare J, Rouleau M, Harvey M, Tetu B, and Guillemette C (2009) Alternative-splicing forms of the major phase II conjugating UGT1A gene negatively regulate glucuronidation in human carcinoma cell lines. Pharmacogenomics J doi:10.1038/tpj.2009.64.
    • (2009) Pharmacogenomics J
    • Bellemare, J.1    Rouleau, M.2    Harvey, M.3    Tetu, B.4    Guillemette, C.5
  • 3
    • 3242695875 scopus 로고    scopus 로고
    • The main role of UGT1A9 in the hepatic metabolism of mycophenolic acid and the effects of naturally occurring variants
    • Bernard O and Guillemette C (2004) The main role of UGT1A9 in the hepatic metabolism of mycophenolic acid and the effects of naturally occurring variants. Drug Metab Dispos 32:775-778.
    • (2004) Drug Metab Dispos , vol.32 , pp. 775-778
    • Bernard, O.1    Guillemette, C.2
  • 4
    • 63149156351 scopus 로고    scopus 로고
    • Topological aspects of oligomeric UDP-glucuronosyltransferases in endoplasmic reticulum membranes: Advances and open questions
    • Bock KW and Köhle C (2009) Topological aspects of oligomeric UDP-glucuronosyltransferases in endoplasmic reticulum membranes: advances and open questions. Biochem Pharmacol 77:1458-1465.
    • (2009) Biochem Pharmacol , vol.77 , pp. 1458-1465
    • Bock, K.W.1    Köhle, C.2
  • 5
    • 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
  • 6
    • 38849197491 scopus 로고    scopus 로고
    • The UDP-glucuronosyltransferases as oligomeric enzymes
    • Finel M and Kurkela M (2008) The UDP-glucuronosyltransferases as oligomeric enzymes. Curr Drug Metab 9:70-76.
    • (2008) Curr Drug Metab , vol.9 , pp. 70-76
    • Finel, M.1    Kurkela, M.2
  • 8
    • 34548097015 scopus 로고    scopus 로고
    • Interactions between human UGT1A1, UGT1A4, and UGT1A6 affect their enzymatic activities
    • Fujiwara R, Nakajima M, Yamanaka H, Katoh M, and Yokoi T (2007a) Interactions between human UGT1A1, UGT1A4, and UGT1A6 affect their enzymatic activities. Drug Metab Dispos 35:1781-1787.
    • (2007) Drug Metab Dispos , vol.35 , pp. 1781-1787
    • Fujiwara, R.1    Nakajima, M.2    Yamanaka, H.3    Katoh, M.4    Yokoi, T.5
  • 10
    • 0036765309 scopus 로고    scopus 로고
    • Common human UGT1A polymorphisms and the altered metabolism of irinotecan active metabolite 7-ethyl-10-hydroxycamptothecin (SN-38)
    • Gagné JF, Montminy V, Belanger P, Journault K, Gaucher G, and Guillemette C (2002) Common human UGT1A polymorphisms and the altered metabolism of irinotecan active metabolite 7-ethyl-10-hydroxycamptothecin (SN-38). Mol Pharmacol 62:608-617.
    • (2002) Mol Pharmacol , vol.62 , pp. 608-617
    • Gagné, J.F.1    Montminy, V.2    Belanger, P.3    Journault, K.4    Gaucher, G.5    Guillemette, C.6
  • 11
    • 0035834673 scopus 로고    scopus 로고
    • Homodimerization of human bilirubin-uridine-diphosphoglucuronate glucuronosyltransferase-1 (UGT1A1) and its functional implications
    • Ghosh SS, Sappal BS, Kalpana GV, Lee SW, Chowdhury JR, and Chowdhury NR (2001) Homodimerization of human bilirubin-uridine-diphosphoglucuronate glucuronosyltransferase-1 (UGT1A1) and its functional implications. J Biol Chem 276:42108-42115.
    • (2001) J Biol Chem , vol.276 , pp. 42108-42115
    • Ghosh, S.S.1    Sappal, B.S.2    Kalpana, G.V.3    Lee, S.W.4    Chowdhury, J.R.5    Chowdhury, N.R.6
  • 12
    • 38449095074 scopus 로고    scopus 로고
    • Genetic diversity at the UGT1 locus is amplified by a novel 3′ alternative splicing mechanism leading to nine additional UGT1A proteins that act as regulators of glucuronidation activity
    • DOI 10.1097/FPC.0b013e3282f1f118, PII 0121301120071200000008
    • Girard H, Lévesque E, Bellemare J, Journault K, Caillier B, and Guillemette C (2007) Genetic diversity at the UGT1 locus is amplified by a novel 3′ alternative splicing mechanism leading to nine additional UGT1A proteins that act as regulators of glucuronidation activity. Pharmacogenet Genomics 17:1077-1089. (Pubitemid 351339492)
    • (2007) Pharmacogenetics and Genomics , vol.17 , Issue.12 , pp. 1077-1089
    • Girard, H.1    Levesque, E.2    Bellemare, J.3    Journault, K.4    Caillier, B.5    Guillemette, C.6
  • 14
    • 0031010059 scopus 로고    scopus 로고
    • Protein-protein interactions between UDP-glucuronosyltransferase isozymes in rat hepatic microsomes
    • DOI 10.1021/bi9702344
    • Ikushiro S, Emi Y, and Iyanagi T (1997) Protein-protein interactions between UDP-glucuronosyltransferase isozymes in rat hepatic microsomes. Biochemistry 36:7154-7161. (Pubitemid 27258131)
    • (1997) Biochemistry , vol.36 , Issue.23 , pp. 7154-7161
    • Ikushiro, S.-I.1    Emi, Y.2    Iyanagi, T.3
  • 15
    • 38449093974 scopus 로고    scopus 로고
    • Protein-protein interactions between rat hepatic cytochromes P450 (P450s) and UDP-glucuronosyltransferases (UGTs): Evidence for the functionally active UGT in P450-UGT complex
    • Ishii Y, Iwanaga M, Nishimura Y, Takeda S, Ikushiro S, Nagata K, Yamazoe Y, Mackenzie PI, and Yamada H (2007) Protein-protein interactions between rat hepatic cytochromes P450 (P450s) and UDP-glucuronosyltransferases (UGTs): evidence for the functionally active UGT in P450-UGT complex. Drug Metab Pharmacokinet 22:367-376.
    • (2007) Drug Metab Pharmacokinet , vol.22 , pp. 367-376
    • Ishii, Y.1    Iwanaga, M.2    Nishimura, Y.3    Takeda, S.4    Ikushiro, S.5    Nagata, K.6    Yamazoe, Y.7    Mackenzie, P.I.8    Yamada, H.9
  • 16
    • 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. (Pubitemid 33027439)
    • (2001) Molecular Pharmacology , vol.60 , Issue.5 , 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    Oguri, K.11
  • 17
    • 74549143382 scopus 로고    scopus 로고
    • Modulation of UDP-glucuronosyltransferase activity by protein-protein association
    • Ishii Y, Takeda S, and Yamada H (2010) Modulation of UDP- glucuronosyltransferase activity by protein-protein association. Drug Metab Rev 42:140-153.
    • (2010) Drug Metab Rev , vol.42 , pp. 140-153
    • Ishii, Y.1    Takeda, S.2    Yamada, H.3
  • 18
    • 40849096162 scopus 로고    scopus 로고
    • Cloning, expression, and functional characterization of relaxin receptor (leucine-rich repeat-containing G protein-coupled receptor 7) splice variants from human fetal membranes
    • DOI 10.1210/en.2007-1348
    • Kern A, Hubbard D, Amano A, and Bryant-Greenwood GD (2008) Cloning, expression, and functional characterization of relaxin receptor (leucine-rich repeat-containing g protein-coupled receptor 7) splice variants from human fetal membranes. Endocrinology 149:1277-1294. (Pubitemid 351397972)
    • (2008) Endocrinology , vol.149 , Issue.3 , pp. 1277-1294
    • Kern, A.1    Hubbard, D.2    Amano, A.3    Bryant-Greenwood, G.D.4
  • 19
    • 0037423299 scopus 로고    scopus 로고
    • Expression and characterization of recombinant human UDP- glucuronosyltransferases (UGTs). UGT1A9 is more resistant to detergent inhibition than other UGTs and was purified as an active dimeric enzyme
    • Kurkela M, García-Horsman JA, Luukkanen L, Mörsky 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 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    García-Horsman, J.A.2    Luukkanen, L.3    Mörsky, S.4    Taskinen, J.5    Baumann, M.6    Kostiainen, R.7    Hirvonen, J.8    Finel, M.9
  • 20
    • 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
    • DOI 10.1016/j.bcp.2004.08.019, PII S0006295204005969
    • 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. (Pubitemid 39535117)
    • (2004) Biochemical Pharmacology , vol.68 , Issue.12 , pp. 2443-2450
    • Kurkela, M.1    Hirvonen, J.2    Kostiainen, R.3    Finel, M.4
  • 21
    • 33847043537 scopus 로고    scopus 로고
    • Interactions with other human UDP-glucuronosyltransferases attenuate the consequences of the Y485D mutation on the activity and substrate affinity of UGT1A6
    • Kurkela M, Patana AS, Mackenzie PI, Court MH, Tate CG, Hirvonen J, Goldman A, and Finel M (2007) Interactions with other human UDP- glucuronosyltransferases attenuate the consequences of the Y485D mutation on the activity and substrate affinity of UGT1A6. Pharmacogenet Genomics 17:115-126.
    • (2007) Pharmacogenet Genomics , vol.17 , pp. 115-126
    • Kurkela, M.1    Patana, A.S.2    Mackenzie, P.I.3    Court, M.H.4    Tate, C.G.5    Hirvonen, J.6    Goldman, A.7    Finel, M.8
  • 22
    • 33846442350 scopus 로고    scopus 로고
    • Regulation of the UGT1A1 bilirubin-conjugating pathway: Role of a new splicing event at the UGT1A locus
    • DOI 10.1002/hep.21464
    • Lévesque E, Girard H, Journault K, Lépine J, and Guillemette C (2007) Regulation of the UGT1A1 bilirubin-conjugating pathway: role of a new splicing event at the UGT1A locus. Hepatology 45:128-138. (Pubitemid 46144372)
    • (2007) Hepatology , vol.45 , Issue.1 , pp. 128-138
    • Levesque, E.1    Girard, H.2    Journault, K.3    Lepine, J.4    Guillemette, C.5
  • 23
    • 0030846868 scopus 로고    scopus 로고
    • UDP-glucuronosyltransferase, the role of the amino terminus in dimerization
    • DOI 10.1074/jbc.272.43.26913
    • Meech R and Mackenzie PI (1997) UDP-glucuronosyltransferase, the role of the amino terminus in dimerization. J Biol Chem 272:26913-26917. (Pubitemid 27452641)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.43 , pp. 26913-26917
    • Meech, R.1    Mackenzie, P.I.2
  • 24
    • 34548055967 scopus 로고    scopus 로고
    • Stereoselective glucuronidation of 5-(4′-hydroxyphenyl)-5- phenylhydantoin by human UDP-glucuronosyltransferase (UGT) 1A1, UGT1A9, and UGT2B15: Effects of UGT-UGT interactions
    • Nakajima M, Yamanaka H, Fujiwara R, Katoh M, and Yokoi T (2007) Stereoselective glucuronidation of 5-(4′-hydroxyphenyl)-5-phenylhydantoin by human UDP-glucuronosyltransferase (UGT) 1A1, UGT1A9, and UGT2B15: effects of UGT-UGT interactions. Drug Metab Dispos 35:1679-1686.
    • (2007) Drug Metab Dispos , vol.35 , pp. 1679-1686
    • Nakajima, M.1    Yamanaka, H.2    Fujiwara, R.3    Katoh, M.4    Yokoi, T.5
  • 25
    • 33947527347 scopus 로고    scopus 로고
    • Oligomerization of the UDP-glucuronosyltransferase 1A proteins: Homo- And heterodimerization analysis by fluorescence resonance energy transfer and co-immunoprecipitation
    • DOI 10.1074/jbc.M609417200
    • Operaña TN and Tukey RH (2007) Oligomerization of the UDP-glucuronosyltransferase 1A proteins: homo- and heterodimerization analysis by fluorescence resonance energy transfer and co-immunoprecipitation. J Biol Chem 282:4821-4829. (Pubitemid 47100945)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.7 , pp. 4821-4829
    • Operana, T.N.1    Tukey, R.H.2
  • 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
    • 0035834703 scopus 로고    scopus 로고
    • The Drosophila nitric-oxide synthase gene (dNOS) encodes a family of proteins that can modulate NOS activity by acting as dominant negative regulators
    • Stasiv Y, Regulski M, Kuzin B, Tully T, and Enikolopov G (2001) The Drosophila nitric-oxide synthase gene (dNOS) encodes a family of proteins that can modulate NOS activity by acting as dominant negative regulators. J Biol Chem 276:42241-42251.
    • (2001) J Biol Chem , vol.276 , pp. 42241-42251
    • Stasiv, Y.1    Regulski, M.2    Kuzin, B.3    Tully, T.4    Enikolopov, G.5
  • 28
    • 0034770465 scopus 로고    scopus 로고
    • Human drug metabolism and the cytochromes P450: Application and relevance of in vitro models
    • DOI 10.1177/00912700122012724
    • Venkatakrishnan K, Von Moltke LL, and Greenblatt DJ (2001) Human drug metabolism and the cytochromes P450: application and relevance of in vitro models. J Clin Pharmacol 41:1149-1179. (Pubitemid 32983216)
    • (2001) Journal of Clinical Pharmacology , vol.41 , Issue.11 , pp. 1149-1179
    • Venkatakrishnan, K.1    Von Moltke, L.L.2    Greenblatt, D.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.