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Volumn 75, Issue 4, 2009, Pages 956-964

Interaction of cytochrome P450 3A4 and UDP-glucuronosyltransferase 2B7: Evidence for protein-protein association and possible involvement of CYP3A4 J-helix in the interaction

Author keywords

[No Author keywords available]

Indexed keywords

1 (3 DIMETHYLAMINOPROPYL) 3 ETHYLCARBODIIMIDE; ALANINE; ANTIBODY; CYTOCHROME P450 3A4; GLUCURONOSYLTRANSFERASE 2B7; GLUTATHIONE TRANSFERASE; HISTIDINE; HYBRID PROTEIN; LEUCINE; LYSINE; METHIONINE; TYROSINE;

EID: 63849272821     PISSN: 0026895X     EISSN: 15210111     Source Type: Journal    
DOI: 10.1124/mol.108.052001     Document Type: Article
Times cited : (46)

References (35)
  • 1
    • 0026088568 scopus 로고
    • Interactions among cytochromes P-450 in the endoplasmic reticulum. Detection of chemically cross-linked complexes with monoclonal antibodies
    • Alston K, Robinson RC, Park SS, Gelboin HV, and Friedman FK (1991) Interactions among cytochromes P-450 in the endoplasmic reticulum. Detection of chemically cross-linked complexes with monoclonal antibodies. J Biol Chem 266:735-739.
    • (1991) J Biol Chem , vol.266 , pp. 735-739
    • Alston, K.1    Robinson, R.C.2    Park, S.S.3    Gelboin, H.V.4    Friedman, F.K.5
  • 2
    • 0024412071 scopus 로고
    • Cytochrome P-450 hPCN3, a novel cytochrome P-450 IIIA gene product that is differentially expressed in adult human liver. cDNA and deduced amino acid sequence and distinct specificities of cDNA-expressed hPCN1 and hPCN3 for the metabolism of steroid hormones and cyclosporine
    • Aoyama T, Yamano S, Waxman DJ, Lapenson DP, Meyer UA, Fischer V, Tyndale R, Inaba T, Kalow W, and Gelboin HV (1989) Cytochrome P-450 hPCN3, a novel cytochrome P-450 IIIA gene product that is differentially expressed in adult human liver. cDNA and deduced amino acid sequence and distinct specificities of cDNA-expressed hPCN1 and hPCN3 for the metabolism of steroid hormones and cyclosporine. J Biol Chem 264:10388-10395.
    • (1989) J Biol Chem , vol.264 , pp. 10388-10395
    • Aoyama, T.1    Yamano, S.2    Waxman, D.J.3    Lapenson, D.P.4    Meyer, U.A.5    Fischer, V.6    Tyndale, R.7    Inaba, T.8    Kalow, W.9    Gelboin, H.V.10
  • 3
    • 0032483045 scopus 로고    scopus 로고
    • Required buried alpha-helical structure in the bilirubin UDP-glucuronosyltransferase, UGT1A1, contains a non-replaceable phenylalanine
    • Ciotti M, Cho JW, George J, and Owens IS (1998) Required buried alpha-helical structure in the bilirubin UDP-glucuronosyltransferase, UGT1A1, contains a non-replaceable phenylalanine. Biochemistry 37:11018-11025.
    • (1998) Biochemistry , vol.37 , pp. 11018-11025
    • Ciotti, M.1    Cho, J.W.2    George, J.3    Owens, I.S.4
  • 4
    • 0034723195 scopus 로고    scopus 로고
    • Engineering microsomal cytochrome P450 2C5 to be a soluble, monomeric enzyme. Mutations that alter aggregation, phospholipid dependence of catalysis, and membrane binding
    • Cosme J and Johnson EF (2000) Engineering microsomal cytochrome P450 2C5 to be a soluble, monomeric enzyme. Mutations that alter aggregation, phospholipid dependence of catalysis, and membrane binding. J Biol Chem 275:2545-2553.
    • (2000) J Biol Chem , vol.275 , pp. 2545-2553
    • Cosme, J.1    Johnson, E.F.2
  • 5
    • 31344443943 scopus 로고    scopus 로고
    • Significance of the minor cytochrome P450 3A isoforms
    • Daly AK (2006) Significance of the minor cytochrome P450 3A isoforms. Clin Phar-macokinet 45:13-31.
    • (2006) Clin Phar-macokinet , vol.45 , pp. 13-31
    • Daly, A.K.1
  • 6
    • 27144459868 scopus 로고    scopus 로고
    • Kinetics of dithionite-dependent reduction of cytochrome P450 3A4: Heterogeneity of the enzyme caused by its oligomerization
    • Davydov DR, Fernando H, Baas BJ, Sligar SG, and Halpert JR (2005) Kinetics of dithionite-dependent reduction of cytochrome P450 3A4: heterogeneity of the enzyme caused by its oligomerization. Biochemistry 44:13902-13913.
    • (2005) Biochemistry , vol.44 , pp. 13902-13913
    • Davydov, D.R.1    Fernando, H.2    Baas, B.J.3    Sligar, S.G.4    Halpert, J.R.5
  • 8
    • 11244283497 scopus 로고    scopus 로고
    • Co-immunoprecipitation of UDP-glucuronosyltransferase (UGT) isoforms and cytochrome P450 3A4
    • Fremont JJ, Wang RW, and King CD (2005) Co-immunoprecipitation of UDP-glucuronosyltransferase (UGT) isoforms and cytochrome P450 3A4. Mol Pharmacol 67:260-262.
    • (2005) Mol Pharmacol , vol.67 , pp. 260-262
    • Fremont, J.J.1    Wang, R.W.2    King, C.D.3
  • 9
    • 0029820670 scopus 로고    scopus 로고
    • Constitutive expression of hepatic cytochrome P450 genes
    • Gonzalez FJ and Lee YH (1996) Constitutive expression of hepatic cytochrome P450 genes. FASEB J 10:1112-1117.
    • (1996) FASEB J , vol.10 , pp. 1112-1117
    • Gonzalez, F.J.1    Lee, Y.H.2
  • 10
    • 0026542989 scopus 로고
    • Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences
    • Gotoh O (1992) Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences. J Biol Chem 267:83-90.
    • (1992) J Biol Chem , vol.267 , pp. 83-90
    • Gotoh, O.1
  • 11
    • 0024593072 scopus 로고
    • Characterization of human microsomal cytochrome P-450 enzymes
    • Guengerich FP (1989) Characterization of human microsomal cytochrome P-450 enzymes. Annu Rev Pharmacol Toxicol 29:241-264.
    • (1989) Annu Rev Pharmacol Toxicol , vol.29 , pp. 241-264
    • Guengerich, F.P.1
  • 12
    • 22144442645 scopus 로고    scopus 로고
    • Functional protein-protein interaction of drug metabolizing enzymes
    • Ishii Y, Takeda S, Yamada H, and Oguri K (2005) Functional protein-protein interaction of drug metabolizing enzymes. Front Biosci 10:887-895.
    • (2005) Front Biosci , vol.10 , pp. 887-895
    • Ishii, Y.1    Takeda, S.2    Yamada, H.3    Oguri, K.4
  • 13
    • 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
  • 14
    • 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
  • 15
    • 0344844370 scopus 로고    scopus 로고
    • The 2002 Bernard B. Brodie Award lecture: Deciphering substrate recognition by drug-metabolizing cytochromes P450
    • Johnson EF (2003) The 2002 Bernard B. Brodie Award lecture: deciphering substrate recognition by drug-metabolizing cytochromes P450. Drug Metab Dispos 31:1532-1540.
    • (2003) Drug Metab Dispos , vol.31 , pp. 1532-1540
    • Johnson, E.F.1
  • 16
    • 0346333300 scopus 로고    scopus 로고
    • Membrane properties induced by anionic phospholipids and hosphatidylethanolamine are critical for the membrane binding and catalytic activity of human cytochrome P450 3A4
    • Kim KH, Ahn T, and Yun CH (2003) Membrane properties induced by anionic phospholipids and hosphatidylethanolamine are critical for the membrane binding and catalytic activity of human cytochrome P450 3A4. Biochemistry 42:15377-5387.
    • (2003) Biochemistry , vol.42 , pp. 15377-15387
    • Kim, K.H.1    Ahn, T.2    Yun, C.H.3
  • 17
    • 0021678736 scopus 로고
    • Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose
    • Kyhse-Andersen J (1984) Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose. J Biochem Biophys Methods 10:203-209.
    • (1984) J Biochem Biophys Methods , vol.10 , pp. 203-209
    • Kyhse-Andersen, J.1
  • 18
    • 0017637023 scopus 로고
    • Cleavage at aspartyl-prolyl bonds
    • Landon M (1977) Cleavage at aspartyl-prolyl bonds. Methods Enzymol 47:145-149.
    • (1977) Methods Enzymol , vol.47 , pp. 145-149
    • Landon, M.1
  • 19
    • 0029956992 scopus 로고    scopus 로고
    • Mutational analysis of the car-boxy-terminal region of UDP-glucuronosyltransferase 2B1
    • Meech R, Yogalingam G, and Mackenzie PI (1996) Mutational analysis of the car-boxy-terminal region of UDP-glucuronosyltransferase 2B1. DNA Cell Biol 15:489-494.
    • (1996) DNA Cell Biol , vol.15 , pp. 489-494
    • Meech, R.1    Yogalingam, G.2    Mackenzie, P.I.3
  • 20
    • 0037470515 scopus 로고    scopus 로고
    • Oda Y, Hosokawa N, Wada I, and Nagata K (2003) EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin. Science 299:13941397.
    • Oda Y, Hosokawa N, Wada I, and Nagata K (2003) EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin. Science 299:13941397.
  • 21
    • 29944434772 scopus 로고    scopus 로고
    • Selective suppressions of human CYP3A forms, CYP3A5 and CYP3A7, by troglitazone in HepG2 cells
    • Ogino M, Nagata K, and Yamazoe Y (2002) Selective suppressions of human CYP3A forms, CYP3A5 and CYP3A7, by troglitazone in HepG2 cells. Drug Metab Phar-macokinet 17:42-46.
    • (2002) Drug Metab Phar-macokinet , vol.17 , pp. 42-46
    • Ogino, M.1    Nagata, K.2    Yamazoe, Y.3
  • 25
    • 0033615624 scopus 로고    scopus 로고
    • An internal signal sequence mediates the targeting and retention of the human UDP-glucuronosyl-transferase 1A6 to the endoplasmic reticulum
    • Ouzzine M, Magdalou J, Burchell B, and Fournel-Gigleux S (1999) An internal signal sequence mediates the targeting and retention of the human UDP-glucuronosyl-transferase 1A6 to the endoplasmic reticulum. J Biol Chem 274:31401-31409.
    • (1999) J Biol Chem , vol.274 , pp. 31401-31409
    • Ouzzine, M.1    Magdalou, J.2    Burchell, B.3    Fournel-Gigleux, S.4
  • 26
    • 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
  • 27
    • 14944354806 scopus 로고    scopus 로고
    • Modulation of UDP-glucuronosyltransferase function by cyto-chrome P450: Evidence for the alteration of UGT2B7-catalyzed glucuronidation of morphine by CYP3A4
    • Takeda S, Ishii Y, Iwanaga M, Mackenzie PI, Nagata K, Yamazoe Y, Oguri K, and Yamada H (2005a) Modulation of UDP-glucuronosyltransferase function by cyto-chrome P450: evidence for the alteration of UGT2B7-catalyzed glucuronidation of morphine by CYP3A4. Mol Pharmacol 67:665-672.
    • (2005) Mol Pharmacol , vol.67 , pp. 665-672
    • Takeda, S.1    Ishii, Y.2    Iwanaga, M.3    Mackenzie, P.I.4    Nagata, K.5    Yamazoe, Y.6    Oguri, K.7    Yamada, H.8
  • 28
    • 26444523430 scopus 로고    scopus 로고
    • Modulation of UDP-glucuronosyltransferase 2B7 function by cytochrome P450s in vitro: Differential effects of CYP1A2, CYP2C9 and CYP3A4
    • Takeda S, Ishii Y, Mackenzie PI, Nagata K, Yamazoe Y, Oguri K, and Yamada H (2005b) Modulation of UDP-glucuronosyltransferase 2B7 function by cytochrome P450s in vitro: differential effects of CYP1A2, CYP2C9 and CYP3A4. Biol Pharm Bull 28:2026-2027.
    • (2005) Biol Pharm Bull , vol.28 , pp. 2026-2027
    • Takeda, S.1    Ishii, Y.2    Mackenzie, P.I.3    Nagata, K.4    Yamazoe, Y.5    Oguri, K.6    Yamada, H.7
  • 29
    • 0034647835 scopus 로고    scopus 로고
    • Interaction between cytochrome P450 and other drug-metabolizing enzymes: Evidence for an association of CYP1A1 with microsomal epoxide hydrolase and UDP-glucurono-syltransferase
    • Taura KI, Yamada H, Hagino Y, Ishii Y, Mori MA, and Oguri K (2000) Interaction between cytochrome P450 and other drug-metabolizing enzymes: evidence for an association of CYP1A1 with microsomal epoxide hydrolase and UDP-glucurono-syltransferase. Biochem Biophys Res Commun 273:1048-1052.
    • (2000) Biochem Biophys Res Commun , vol.273 , pp. 1048-1052
    • Taura, K.I.1    Yamada, H.2    Hagino, Y.3    Ishii, Y.4    Mori, M.A.5    Oguri, K.6
  • 30
    • 1942532106 scopus 로고    scopus 로고
    • Cytochrome P450 1A1 (CYP1A1) inhibitor alpha-naphthoflavone interferes with UDP-glucuronosyltransferase (UGT) activity in intact but not in permeabilized hepatic microsomes from 3-methylcholanthrene-treated rats: Possible involvement of UGT-P450 interactions
    • Taura K, Naito E, Ishii Y, Mori MA, Oguri K, and Yamada H (2004) Cytochrome P450 1A1 (CYP1A1) inhibitor alpha-naphthoflavone interferes with UDP-glucuronosyltransferase (UGT) activity in intact but not in permeabilized hepatic microsomes from 3-methylcholanthrene-treated rats: possible involvement of UGT-P450 interactions. Biol Pharm Bull 27:56-60.
    • (2004) Biol Pharm Bull , vol.27 , pp. 56-60
    • Taura, K.1    Naito, E.2    Ishii, Y.3    Mori, M.A.4    Oguri, K.5    Yamada, H.6
  • 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
    • 0026718792 scopus 로고
    • The cytochrome P450 2B4-NADPH cytochrome P450 reductase electron transfer complex is not formed by charge-pairing
    • Voznesensky AI and Schenkman JB (1992) The cytochrome P450 2B4-NADPH cytochrome P450 reductase electron transfer complex is not formed by charge-pairing. J Biol Chem 267:14669-14676.
    • (1992) J Biol Chem , vol.267 , pp. 14669-14676
    • Voznesensky, A.I.1    Schenkman, J.B.2
  • 33
    • 0033970047 scopus 로고    scopus 로고
    • Mammalian microsomal cytochrome P450 monooxygenase: Structural adaptations for membrane binding and functional diversity
    • Williams PA, Cosme J, Sridhar V, Johnson EF, and McRee DE (2000) Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity. Mol Cell 5:121-131.
    • (2000) Mol Cell , vol.5 , pp. 121-131
    • Williams, P.A.1    Cosme, J.2    Sridhar, V.3    Johnson, E.F.4    McRee, D.E.5
  • 35
    • 4644301430 scopus 로고    scopus 로고
    • The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05-A resolution
    • Yano JK, Wester MR, Schoch GA, Griffin KJ, Stout CD, and Johnson EF (2004) The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05-A resolution. J Biol Chem 279:38091- 38094.
    • (2004) J Biol Chem , vol.279 , pp. 38091-38094
    • Yano, J.K.1    Wester, M.R.2    Schoch, G.A.3    Griffin, K.J.4    Stout, C.D.5    Johnson, E.F.6


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