메뉴 건너뛰기




Volumn 40, Issue 11, 2012, Pages 2081-2089

ATP serves as an endogenous inhibitor of UDP-glucuronosyltransferase (UGT): A new insight into the latency of UGT

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; ALAMETHICIN; CETOMACROGOL; GEFITINIB; GLUCURONOSYLTRANSFERASE; GLUCURONOSYLTRANSFERASE 1A9; HYMECROMONE;

EID: 84867690602     PISSN: 00909556     EISSN: 1521009X     Source Type: Journal    
DOI: 10.1124/dmd.112.046862     Document Type: Article
Times cited : (17)

References (45)
  • 1
    • 0027216642 scopus 로고
    • Latency is the major determinant of UDP-glucuronosyltransferase activity in isolated hepatocytes
    • DOI 10.1016/0014-5793(93)80983-2
    • Bánhegyi G, Garzó T, Fulceri R, Benedetti A, and Mandl J (1993) Latency is the major determinant of UDP-glucuronosyltransferase activity in isolated hepatocytes. FEBS Lett 328:149-152. (Pubitemid 23234783)
    • (1993) FEBS Letters , vol.328 , Issue.1-2 , pp. 149-152
    • Banhegyi, G.1    Garzo, T.2    Fulceri, R.3    Benedetti, A.4    Mandl, J.5
  • 3
    • 0023189255 scopus 로고
    • The role of conjugation reactions in detoxication
    • DOI 10.1007/BF00296941
    • Bock KW, Lilienblum W, Fischer G, Schirmer G, and Bock-Henning BS (1987) The role of conjugation reactions in detoxication. Arch Toxicol 60:22-29. (Pubitemid 17081678)
    • (1987) Archives of Toxicology , vol.60 , Issue.1-3 , pp. 22-29
    • Bock, K.W.1    Lilienblum, W.2    Fischer, G.3
  • 5
    • 0026665249 scopus 로고
    • Translocation of ATP into the lumen of rough endoplasmic reticulum-derived vesicles and its binding to luminal proteins including BiP (GRP 78) and GRP 94
    • Clairmont CA, De Maio A, and Hirschberg CB (1992) Translocation of ATP into the lumen of rough endoplasmic reticulum-derived vesicles and its binding to luminal proteins including BiP (GRP 78) and GRP 94. J Biol Chem 267:3983-3990.
    • (1992) J Biol Chem , vol.267 , pp. 3983-3990
    • Clairmont, C.A.1    De Maio, A.2    Hirschberg, C.B.3
  • 7
    • 0028291264 scopus 로고
    • The levels of endoplasmic reticulum proteins and ATP affect folding and secretion of selective proteins
    • DOI 10.1006/biol.1994.1016
    • Dorner AJ and Kaufman RJ (1994) The levels of endoplasmic reticulum proteins and ATP affect folding and secretion of selective proteins. Biologicals 22:103-112. (Pubitemid 24224591)
    • (1994) Biologicals , vol.22 , Issue.2 , pp. 103-112
    • Dorner, A.J.1    Kaufman, R.J.2
  • 9
    • 78651083117 scopus 로고    scopus 로고
    • The small-molecular tyrosine kinase inhibitor nilotinib is a potent noncompetitive inhibitor of the SN-38 glucuronidation by human UGT1A1
    • Fujita K, Sugiyama M, Akiyama Y, Ando Y, and Sasaki Y (2011) The small-molecular tyrosine kinase inhibitor nilotinib is a potent noncompetitive inhibitor of the SN-38 glucuronidation by human UGT1A1. Cancer Chemother Pharmacol 67:237-241.
    • (2011) Cancer Chemother Pharmacol , vol.67 , pp. 237-241
    • Fujita, K.1    Sugiyama, M.2    Akiyama, Y.3    Ando, Y.4    Sasaki, Y.5
  • 10
    • 69949169707 scopus 로고    scopus 로고
    • In silico and in vitro approaches to elucidate the thermal stability of human UDP-glucuronosyltransferase (UGT)1A9
    • Fujiwara R, Nakajima M, Yamamoto T, Nagao H, and Yokoi T (2009) In silico and in vitro approaches to elucidate the thermal stability of human UDP-glucuronosyltransferase (UGT)1A9. Drug Metab Pharmacokinet 24:235-244.
    • (2009) Drug Metab Pharmacokinet , vol.24 , pp. 235-244
    • Fujiwara, R.1    Nakajima, M.2    Yamamoto, T.3    Nagao, H.4    Yokoi, T.5
  • 11
    • 0030068075 scopus 로고    scopus 로고
    • ATP binding and hydrolysis by the multifunctional protein disulfide isomerase
    • DOI 10.1074/jbc.271.5.2663
    • Guthapfel R, Guéguen P, and Quéméneur E (1996) ATP binding and hydrolysis by the multifunctional protein disulfide isomerase. J Biol Chem 271:2663-2666. (Pubitemid 26047880)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.5 , pp. 2663-2666
    • Guthapfel, R.1    Gueguen, P.2    Quenaeneur, E.3
  • 12
    • 0031717105 scopus 로고    scopus 로고
    • The AMP-activated/SNF1 protein kinase subfamily: Metabolic sensors of the eukaryotic cell?
    • DOI 10.1146/annurev.biochem.67.1.821
    • Hardie DG, Carling D, and Carlson M (1998) The AMP-activated/SNF1 protein kinase subfamily: metabolic sensors of the eukaryotic cell? Ann Rev Biochem 67:821-855. (Pubitemid 28411146)
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 821-855
    • Hardie, D.G.1    Carling, D.2    Carlson, M.3
  • 13
    • 0035542970 scopus 로고    scopus 로고
    • AMP-activated protein kinase: The energy charge hypothesis revisited
    • Hardie DG and Hawley SA (2001) AMP-activated protein kinase: the energy charge hypothesis revisited. Bioessays 23:1112-1119.
    • (2001) Bioessays , vol.23 , pp. 1112-1119
    • Hardie, D.G.1    Hawley, S.A.2
  • 14
    • 0035076242 scopus 로고    scopus 로고
    • Determination of UDP-glucuronosyltransferase UGT1A6 activity in human and rat liver microsomes by HPLC with UV detection
    • DOI 10.1016/S0731-7085(00)00491-X, PII S073170850000491X
    • Hanioka N, Jinno H, Tanaka-Kagawa T, Nishimura T, and Ando M (2001) Detection of UDP-glucuronosyltransferase UGT1A6 activity in human and rat liver microsomes by HPLC with UV detection. J Pharm Biomed Anal 25:65-75. (Pubitemid 32234400)
    • (2001) Journal of Pharmaceutical and Biomedical Analysis , vol.25 , Issue.1 , pp. 65-75
    • Hanioka, N.1    Jinno, H.2    Tanaka-Kagawa, T.3    Nishimura, T.4    Ando, M.5
  • 15
    • 0023763078 scopus 로고
    • A membrane transporter mediates access of uridine 5'-diphosphoglucuronic acid from the cytosol into the endoplasmic reticulum of rat hepatocytes: Implications for glucuronidation reactions
    • DOI 10.1016/0304-4165(88)90004-9
    • Hauser SC, Ziurys JC, and Gollan JL (1988) A membrane transporter mediates access of uridine 5′-diphosphoglucuronic acid from the cytosol into the endoplasmic reticulum of rat hepatocytes: implications for glucuronidation reactions. Biochim Biophys Acta 967:149-157. (Pubitemid 18265670)
    • (1988) Biochimica et Biophysica Acta - General Subjects , vol.967 , Issue.2 , pp. 149-157
    • Hauser, S.C.1    Ziurys, J.C.2    Gollan, J.L.3
  • 16
    • 18844388999 scopus 로고    scopus 로고
    • Minireview: Hexose-6-phosphate dehydrogenase and redox control of 11β-hydroxysteroid dehydrogenase type 1 activity
    • DOI 10.1210/en.2005-0117
    • Hewitt KN, Walker EA, and Stewart PM (2005) Minireview: hexose-6-phosphate dehydrogenase and redox control of 11β-hydroxysteroid dehydrogenase type 1 activity. Endocrinology 146:2539-2543. (Pubitemid 40695555)
    • (2005) Endocrinology , vol.146 , Issue.6 , pp. 2539-2543
    • Hewitt, K.N.1    Walker, E.A.2    Stewart, P.M.3
  • 17
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • Kelley LA and Sternberg MJ (2009) Protein structure prediction on the Web: a case study using the Phyre server. Nat Protoc 4:363-371.
    • (2009) Nat Protoc , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 18
    • 0029866372 scopus 로고    scopus 로고
    • Identification of the ATP transporter of rat liver rough endoplasmic reticulum via photoaffinity labeling and partial purification
    • Kim SH, Shin SJ, and Park JS (1996) Identification of the ATP transporter of rat liver rough endoplasmic reticulum via photoaffinity labeling and partial purification. Biochemistry 35:5418-5425.
    • (1996) Biochemistry , vol.35 , pp. 5418-5425
    • Kim, S.H.1    Shin, S.J.2    Park, J.S.3
  • 19
    • 34250172749 scopus 로고    scopus 로고
    • Crystal Structure of Medicago truncatula UGT85H2 - Insights into the Structural Basis of a Multifunctional (Iso)flavonoid Glycosyltransferase
    • DOI 10.1016/j.jmb.2007.05.036, PII S0022283607006729
    • Li L, Modolo LV, Escamilla-Trevino LL, Achnine L, Dixon RA, and Wang X (2007) Crystal structure of Medicago truncatula UGT85H2-insights into the structural basis of a multifunctional (iso)flavonoid glycosyltransferase. J Mol Biol 370:951-963. (Pubitemid 46899073)
    • (2007) Journal of Molecular Biology , vol.370 , Issue.5 , pp. 951-963
    • Li, L.1    Modolo, L.V.2    Escamilla-Trevino, L.L.3    Achnine, L.4    Dixon, R.A.5    Wang, X.6
  • 20
    • 73149090339 scopus 로고    scopus 로고
    • Comparison of the drug-drug interactions potential of erlotinib and gefitinib via inhibition of UDP-glucuronosyltransferases
    • Liu Y, Ramírez J, House L, and Ratain MJ (2010) Comparison of the drug-drug interactions potential of erlotinib and gefitinib via inhibition of UDP-glucuronosyltransferases. Drug Metab Dispos 38:32-39.
    • (2010) Drug Metab Dispos , vol.38 , pp. 32-39
    • Liu, Y.1    Ramírez, J.2    House, L.3    Ratain, M.J.4
  • 24
    • 70149104455 scopus 로고    scopus 로고
    • Crystal structures of glycosyltransferase UGT78G1 reveal the molecular basis for glycosylation and deglycosylation of (iso)flavonoids
    • Modolo LV, Li L, Pan H, Blount JW, Dixon RA, and Wang X (2009) Crystal structures of glycosyltransferase UGT78G1 reveal the molecular basis for glycosylation and deglycosylation of (iso)flavonoids. J Mol Biol 392:1292-1302.
    • (2009) J Mol Biol , vol.392 , pp. 1292-1302
    • Modolo, L.V.1    Li, L.2    Pan, H.3    Blount, J.W.4    Dixon, R.A.5    Wang, X.6
  • 25
    • 2442440054 scopus 로고    scopus 로고
    • Crystal Structure of Vancosaminyltransferase GtfD from the Vancomycin Biosynthetic Pathway: Interactions with Acceptor and Nucleotide Ligands
    • DOI 10.1021/bi036130c
    • Mulichak AM, Lu W, Losey HC, Walsh CT, and Garavito RM (2004) Crystal structure of vancosaminyltransferase GtfD from the vancomycin biosynthetic pathway: interactions with acceptor and nucleotide ligands. Biochemistry 43:5170-5180. (Pubitemid 38620908)
    • (2004) Biochemistry , vol.43 , Issue.18 , pp. 5170-5180
    • Mulichak, A.M.1    Lu, W.2    Losey, H.C.3    Walsh, C.T.4    Garavito, R.M.5
  • 26
    • 34548359330 scopus 로고    scopus 로고
    • Variety of nucleotide sugar transporters with respect to the interaction with nucleoside mono- and diphosphates
    • DOI 10.1074/jbc.M611358200
    • Muraoka M, Miki T, Ishida N, Hara T, and Kawakita M (2007) Variety of nucleotide sugar transporters with respect to the interaction with nucleoside mono- and diphosphates. J Biol Chem 282:24615-24622. (Pubitemid 47347531)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.34 , pp. 24615-24622
    • Muraoka, M.1    Miki, T.2    Ishida, N.3    Hara, T.4    Kawakita, M.5
  • 27
    • 34848893895 scopus 로고    scopus 로고
    • Inhibitory effects of adenine nucleotides and related substances on UDP-glucuronosyltransferase: Structure-effect relationships and evidence for an allosteric mechanism
    • DOI 10.1016/j.bbagen.2007.07.011, PII S0304416507001614
    • Nishimura Y, Maeda S, Ikushiro S, Mackenzie PI, Ishii Y, and Yamada H (2007) Inhibitory effects of adenine nucleotides and related substances on UDP-glucuronosyltransferase: structure-effect relationships and evidence for an allosteric mechanism. Biochim Biophys Acta 1770:1557-1566. (Pubitemid 47503557)
    • (2007) Biochimica et Biophysica Acta - General Subjects , vol.1770 , Issue.11 , pp. 1557-1566
    • Nishimura, Y.1    Maeda, S.2    Ikushiro, S.-i.3    Mackenzie, P.I.4    Ishii, Y.5    Yamada, H.6
  • 28
    • 0034465184 scopus 로고    scopus 로고
    • An automatic homology modeling method consisting of database searches and simulated annealing
    • Ogata K and Umeyama H (2000) An automatic homology modeling method consisting of database searches and simulated annealing. J Mol Graph Model 18:258-272, 305-306.
    • (2000) J Mol Graph Model , vol.18
    • Ogata, K.1    Umeyama, H.2
  • 30
    • 0030027365 scopus 로고    scopus 로고
    • Purification of a phenobarbital-inducible UDP-glucuronosyltransferase isoform from dog liver which catalyzes morphine and testosterone glucuronidation
    • DOI 10.1006/abbi.1996.0020
    • Oguri K, Kurogi A, Yamabe K, Tanaka M, Yoshisue K, Ishii Y, and Yoshimura H (1996) Purification of a phenobarbital-inducible UDP-glucuronosyltransferase isoform from dog liver which catalyzes morphine and testosterone glucuronidation. Arch Biochem Biophys 325:159-166. (Pubitemid 26025986)
    • (1996) Archives of Biochemistry and Biophysics , vol.325 , Issue.2 , pp. 159-166
    • Oguri, K.1    Kurogi, A.2    Yamabe, K.-I.3    Tanaka, M.4    Yoshisue, K.5    Ishii, Y.6    Yoshimura, H.7
  • 31
    • 79955877359 scopus 로고    scopus 로고
    • Inhibition of paracetamol glucuronidation by tyrosine kinase inhibitors
    • Liu I, Ramírez J, and Ratain MJ (2011) Inhibition of paracetamol glucuronidation by tyrosine kinase inhibitors. Br J Clin Pharmacol 76:917-920.
    • (2011) Br J Clin Pharmacol , vol.76 , pp. 917-920
    • Liu, I.1    Ramírez, J.2    Ratain, M.J.3
  • 32
    • 0022897428 scopus 로고
    • Isolation and purification of rat liver morphine UDP- glucuronsyltransferase
    • Puig JF and Tephly TR (1986) Isolation and purification of rat liver morphine UDP-glucuronosyltransferase. Mol Pharmacol 30:558-565. (Pubitemid 17228899)
    • (1986) Molecular Pharmacology , vol.30 , Issue.6 , pp. 558-565
    • Puig, J.F.1    Tephly, T.R.2
  • 33
    • 0028141851 scopus 로고
    • A major phosphoprotein of the endoplasmic reticulum is protein disulfide isomerase
    • Quéméneur E, Guthapfel R, and Gueguen P (1994) A major phosphoprotein of the endoplasmic reticulum is protein disulfide isomerase. J Biol Chem 269:5485-5488. (Pubitemid 24242905)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.8 , pp. 5485-5488
    • Quemeneur, E.1    Guthapfel, R.2    Gueguen, P.3
  • 34
    • 30144443660 scopus 로고    scopus 로고
    • Structure of UDP-glucuronosyltransferases in membranes
    • DOI 10.1016/S0076-6879(05)00008-X, PII S007668790500008X, 8, Phase II Conjugation Enzymes and Transport Systems
    • Radominska-Pandya A, Ouzzine M, Fournel-Gigleux S, and Magdalou J (2005) Structure of UDP-glucuronosyltransferases in membranes. Methods Enzymol 400:116-147. (Pubitemid 43052419)
    • (2005) Methods in Enzymology , vol.400 , pp. 116-147
    • Radominska-Pandya, A.1    Ouzzine, M.2    Fournel-Gigleux, S.3    Magdalou, J.4
  • 35
    • 12144265135 scopus 로고    scopus 로고
    • A circadian clock and light/dark adaptation differentially regulate adenosine in the mammalian retina
    • DOI 10.1523/JNEUROSCI.3138-04.2005
    • Ribelayga C and Mangel SC (2005) A circadian clock and light/dark adaptation differentially regulate adenosine in the mammalian retina. J Neurosci 25:215-222. (Pubitemid 40110783)
    • (2005) Journal of Neuroscience , vol.25 , Issue.1 , pp. 215-222
    • Ribelayga, C.1    Mangel, S.C.2
  • 36
    • 0034534895 scopus 로고    scopus 로고
    • Roles of glucuronidation and UDP-glucuronosyltransferases in xenobiotic bioactivation reactions
    • Ritter JK (2000) Roles of glucuronidation and UDP- glucuronosyltransferases in xenobiotic bioactivation reactions. Chem Biol Interact 129:171-193.
    • (2000) Chem Biol Interact , vol.129 , pp. 171-193
    • Ritter, J.K.1
  • 37
    • 3042777537 scopus 로고    scopus 로고
    • Adenosine nucleotides and the regulation of GRP94-client protein interactions
    • DOI 10.1021/bi049539q
    • Rosser MF, Trotta BM, Marshall MR, Berwin B, and Nicchitta CV (2004) Adenosine nucleotides and the regulation of GRP94-client protein interactions. Biochemistry 43:8835-8845. (Pubitemid 38880054)
    • (2004) Biochemistry , vol.43 , Issue.27 , pp. 8835-8845
    • Rosser, M.F.N.1    Trotta, B.M.2    Marshall, M.R.3    Berwin, B.4    Nicchitta, C.V.5
  • 38
    • 0033858372 scopus 로고    scopus 로고
    • Extracellular ATP-mediated propagation of Ca(2+) waves. Focus on "mechanical strain-induced Ca(2+) waves are propagated via ATP release and purinergic receptor activation."
    • Schwiebert EM (2000) Extracellular ATP-mediated propagation of Ca(2+) waves. Focus on "mechanical strain-induced Ca(2+) waves are propagated via ATP release and purinergic receptor activation." Am J Physiol Cell Physiol 279:C281-C283.
    • (2000) Am J Physiol Cell Physiol , vol.279
    • Schwiebert, E.M.1
  • 39
    • 33645281589 scopus 로고    scopus 로고
    • Crystal structures of a multifunctional triterpene/flavonoid glycosyltransferase from Medicago truncatula
    • Shao H, He X, Achnine L, Blount JW, Dixon RA, and Wang X (2005) Crystal structures of a multifunctional triterpene/flavonoid glycosyltransferase from Medicago truncatula. Plant Cell 17:3141-3154.
    • (2005) Plant Cell , vol.17 , pp. 3141-3154
    • Shao, H.1    He, X.2    Achnine, L.3    Blount, J.W.4    Dixon, R.A.5    Wang, X.6
  • 40
    • 0024566868 scopus 로고
    • An investigation of the transverse topology of bilirubin UDP-glucuronosyltransferase in rat hepatic endoplasmic reticulum
    • Shepherd SR, Baird SJ, Hallinan T, and Burchell B (1989) An investigation of the transverse topology of bilirubin UDP-glucuronosyltransferase in rat hepatic endoplasmic reticulum. Biochem J 259:617-620. (Pubitemid 19111705)
    • (1989) Biochemical Journal , vol.259 , Issue.2 , pp. 617-620
    • Shepherd, S.R.P.1    Baird, S.J.2    Hallinan, T.3    Burchell, B.4
  • 41
    • 0016607004 scopus 로고
    • Regulation of pyruvate dehydrogenase in isolated rat liver mitochondria. Effects of octanoate, oxidation-reduction state, and adenosine triphosphate to adenosine diphosphate ratio
    • Taylor SI, Mukherjee C, and Jungas RL (1975) Regulation of pyruvate dehydrogenase in isolated rat liver mitochondria. Effects of octanoate, oxidation-reduction state, and adenosine triphosphate to adenosine diphosphate ratio. J Biol Chem 250:2028-2035.
    • (1975) J Biol Chem , vol.250 , pp. 2028-2035
    • Taylor, S.I.1    Mukherjee, C.2    Jungas, R.L.3
  • 42
    • 0034128936 scopus 로고    scopus 로고
    • Human UDP-glucuronosyltransferases: Metabolism, expression, and disease
    • DOI 10.1146/annurev.pharmtox.40.1.581
    • Tukey RH and Strassburg CP (2000) Human UDP-glucuronosyltransferases: metabolism, expression, and disease. Annu Rev Pharmacol Toxicol 40:581-616. (Pubitemid 30340694)
    • (2000) Annual Review of Pharmacology and Toxicology , vol.40 , pp. 581-616
    • Tukey, R.H.1    Strassburg, C.P.2
  • 43
    • 77954299402 scopus 로고    scopus 로고
    • 3DLigandSite: Predicting ligand-binding sites using similar structures
    • Wass MN, Kelley LA, and Sternberg MJ (2010) 3DLigandSite: predicting ligand-binding sites using similar structures. Nucleic Acids Res 38:W469-W473.
    • (2010) Nucleic Acids Res , vol.38
    • Wass, M.N.1    Kelley, L.A.2    Sternberg, M.J.3
  • 44
    • 0014664072 scopus 로고
    • Studies on the activation in vitro of glucuronyltransferase
    • Winsnes A (1969) Studies on the activation in vitro of glucuronyltransferase. Biochim Biophys Acta 191:279-291.
    • (1969) Biochim Biophys Acta , vol.191 , pp. 279-291
    • Winsnes, A.1
  • 45
    • 0031054687 scopus 로고    scopus 로고
    • Interaction of endoplasmic reticulum chaperone GRP94 with peptide substrates is adenine nucleotide-independent
    • DOI 10.1074/jbc.272.8.5152
    • Wearsch PA and Nicchitta CV (1997) Interaction of endoplasmic reticulum chaperone GRP94 with peptide substrates is adenine nucleotide-independent. J Biol Chem 272:5152-5156. (Pubitemid 27090072)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.8 , pp. 5152-5156
    • Wearsch, P.A.1    Nicchitta, C.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.