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Volumn 1672, Issue 2, 2004, Pages 86-92

Functional co-expression of xenobiotic metabolizing enzymes, rat cytochrome P450 1A1 and UDP-glucuronosyltransferase 1A6, in yeast microsomes

Author keywords

7 ethoxycoumarin; 7EC; 7GC; AbA; Aureobasidin A; Co expression system; Cytochrome P450; Endoplasmic reticulum; ER; GAPDH; GlcUA; Glucuronic acid; Glucuronide of 7HC; P450; UDP glucuronosyltransferase; Xenobiotic; Yeast microsome

Indexed keywords

7 ETHOXYCOUMARIN; ALCOHOL DEHYDROGENASE; ALCOHOL DEHYDROGENASE I; COMPLEMENTARY DNA; CYTOCHROME P450; CYTOCHROME P450 1A1; FUNGAL ENZYME; GLUCURONIDE; GLUCURONOSYLTRANSFERASE; GLUCURONOSYLTRANSFERASE 1A6; PROTEINASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE; UMBELLIFERONE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE GLUCURONIC ACID; XENOBIOTIC AGENT;

EID: 1942446288     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2004.02.012     Document Type: Article
Times cited : (25)

References (34)
  • 1
    • 1942467974 scopus 로고    scopus 로고
    • Introduction to Drug Metabolism
    • United Kingdom: Nelson Thornes
    • Gibson G.G., Skett P. Introduction to Drug Metabolism. third ed. 2001;Nelson Thornes, United Kingdom.
    • (2001) Third Ed.
    • Gibson, G.G.1    Skett, P.2
  • 2
    • 0033616138 scopus 로고    scopus 로고
    • Forty years of cytochrome P450
    • Omura T. Forty years of cytochrome P450. Biochem. Biophys. Res. Commun. 266:1999;690-698.
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 690-698
    • Omura, T.1
  • 3
    • 0034092174 scopus 로고    scopus 로고
    • Human cytochrome P450 (CYP) genes: Recommendations for the nomenclature of alleles
    • Ingelman-Sundberg M., Daly A.K., Oscarson M., Nebert D.W. Human cytochrome P450 (CYP) genes: recommendations for the nomenclature of alleles. Pharmacogenetics. 10:2000;91-93.
    • (2000) Pharmacogenetics , vol.10 , pp. 91-93
    • Ingelman-Sundberg, M.1    Daly, A.K.2    Oscarson, M.3    Nebert, D.W.4
  • 5
    • 0015058837 scopus 로고
    • Hydroxylation and subsequent glucuronide conjugation of desmethylimipramine in rat liver microsomes
    • von Bahr C., Bertilsson L. Hydroxylation and subsequent glucuronide conjugation of desmethylimipramine in rat liver microsomes. Xenobiotica. 1:1971;205-212.
    • (1971) Xenobiotica , vol.1 , pp. 205-212
    • Von Bahr, C.1    Bertilsson, L.2
  • 6
    • 0023937729 scopus 로고
    • Competing pathways in drug metabolism: I. Effect of input concentration on the conjugation of gentisamide in the once-through in situ perfused rat liver preparation
    • Morris M.E., Yuen V., Tang B.K., Pang K.S. Competing pathways in drug metabolism: I. Effect of input concentration on the conjugation of gentisamide in the once-through in situ perfused rat liver preparation. J. Pharmacol. Exp. Ther. 245:1988;614-624.
    • (1988) J. Pharmacol. Exp. Ther. , vol.245 , pp. 614-624
    • Morris, M.E.1    Yuen, V.2    Tang, B.K.3    Pang, K.S.4
  • 7
    • 0029790412 scopus 로고    scopus 로고
    • Sequestered endoplasmic reticulum space for sequential metabolism of salicylamide: Coupling of hydroxylation and glucuronidation
    • Tirona R.G., Pang K.S. Sequestered endoplasmic reticulum space for sequential metabolism of salicylamide: coupling of hydroxylation and glucuronidation. Drug Metab. Dispos. 24:1996;821-833.
    • (1996) Drug Metab. Dispos. , vol.24 , pp. 821-833
    • Tirona, R.G.1    Pang, K.S.2
  • 8
    • 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-glucuronosyltransferase
    • Taura K., Yamada H., Hagino Y., Ishii Y., Mori M., Oguri K. Interaction between cytochrome P450 and other drug-metabolizing enzymes: evidence for an association of CYP1A1 with microsomal epoxide hydrolase and UDP- glucuronosyltransferase. Biochem. Biophys. Res. Commun. 273:2000;1048-1052.
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 1048-1052
    • Taura, K.1    Yamada, H.2    Hagino, Y.3    Ishii, Y.4    Mori, M.5    Oguri, K.6
  • 9
    • 0029559174 scopus 로고
    • Identification and analysis of drug-responsive expression of UDP-glucuronosyltransferase family 1 (UGT1) isozyme in rat hepatic microsomes using anti-peptide antibodies
    • Ikushiro S., Emi Y., Iyanagi T. Identification and analysis of drug-responsive expression of UDP-glucuronosyltransferase family 1 (UGT1) isozyme in rat hepatic microsomes using anti-peptide antibodies. Arch. Biochem. Biophys. 324:1995;267-272.
    • (1995) Arch. Biochem. Biophys. , vol.324 , pp. 267-272
    • Ikushiro, S.1    Emi, Y.2    Iyanagi, T.3
  • 10
    • 0026672248 scopus 로고
    • Organella-targeted expression of rat liver cytochrome P450c27 in yeast: Genetically engineered alteration of mitochondrial P450 into a microsomal form creates a novel functional electron transport chain
    • Sakaki T., Akiyoshi-Shibata M., Yabusaki Y., Ohkawa H. Organella-targeted expression of rat liver cytochrome P450c27 in yeast: genetically engineered alteration of mitochondrial P450 into a microsomal form creates a novel functional electron transport chain. J. Biol. Chem. 267:1992;16497-16502.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16497-16502
    • Sakaki, T.1    Akiyoshi-Shibata, M.2    Yabusaki, Y.3    Ohkawa, H.4
  • 11
    • 0037159194 scopus 로고    scopus 로고
    • Activation of glucuronidation through reduction of a disulfide bond in rat UDP-glucuronosyltransferase 1A6
    • Ikushiro S., Emi Y., Iyanagi T. Activation of glucuronidation through reduction of a disulfide bond in rat UDP-glucuronosyltransferase 1A6. Biochemistry. 41:2002;12813-12820.
    • (2002) Biochemistry , vol.41 , pp. 12813-12820
    • Ikushiro, S.1    Emi, Y.2    Iyanagi, T.3
  • 12
    • 0032549617 scopus 로고    scopus 로고
    • Transformation system for prototrophic industrial yeasts using the AUR1 gene as a dominant selection marker
    • Hashida-Okado T., Ogawa A., Kato I., Takesako K. Transformation system for prototrophic industrial yeasts using the AUR1 gene as a dominant selection marker. FEBS Lett. 425:1998;117-122.
    • (1998) FEBS Lett. , vol.425 , pp. 117-122
    • Hashida-Okado, T.1    Ogawa, A.2    Kato, I.3    Takesako, K.4
  • 13
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito H., Fukuda Y., Murata K., Kimura A. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:1983;163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 14
    • 0021880264 scopus 로고
    • Expression of rat liver cytochrome P-450MC cDNA in Saccharomyces cerevisiae
    • Oeda K., Sakaki T., Ohkawa H. Expression of rat liver cytochrome P-450MC cDNA in Saccharomyces cerevisiae. DNA. 4:1985;203-210.
    • (1985) DNA , vol.4 , pp. 203-210
    • Oeda, K.1    Sakaki, T.2    Ohkawa, H.3
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Lammli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1971;680-685.
    • (1971) Nature , vol.227 , pp. 680-685
    • Lammli, U.K.1
  • 17
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes: I. Evidence for its hemoprotein nature
    • Omura T., Sato R. The carbon monoxide-binding pigment of liver microsomes: I. Evidence for its hemoprotein nature. J. Biol. Chem. 239:1964;2370-2378.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 18
    • 0017088267 scopus 로고
    • Some properties of a detergent-solubilized NADPH-cytochrome c (cytochrome P-450) reductase purified by biospecific affinity chromatography
    • Yasukochi Y., Masters B.S. Some properties of a detergent-solubilized NADPH-cytochrome c (cytochrome P-450) reductase purified by biospecific affinity chromatography. J. Biol. Chem. 251:1976;5337-5344.
    • (1976) J. Biol. Chem. , vol.251 , pp. 5337-5344
    • Yasukochi, Y.1    Masters, B.S.2
  • 19
    • 0023019287 scopus 로고
    • Cloning and characterization of cDNA encoding 3-methylcholanthrene inducible rat mRNA for UDP-glucuronosyltransferase
    • Iyanagi T., Haniu M., Sogawa K., Fujii-Kuriyama Y., Watanabe S., Shively J.E., Anan K.F. Cloning and characterization of cDNA encoding 3-methylcholanthrene inducible rat mRNA for UDP-glucuronosyltransferase. J. Biol. Chem. 261:1986;15607-15614.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15607-15614
    • Iyanagi, T.1    Haniu, M.2    Sogawa, K.3    Fujii-Kuriyama, Y.4    Watanabe, S.5    Shively, J.E.6    Anan, K.F.7
  • 20
    • 0024566868 scopus 로고
    • An investigation of the transverse topology of bilirubin UDP-glucuronosyltransferase in rat hepatic endoplasmic reticulum
    • Shepherd S.R.P., Baird S.J., Hallinan T., Burchell B. An investigation of the transverse topology of bilirubin UDP-glucuronosyltransferase in rat hepatic endoplasmic reticulum. Biochem. J. 259:1989;617-620.
    • (1989) Biochem. J. , vol.259 , pp. 617-620
    • Shepherd, S.R.P.1    Baird, S.J.2    Hallinan, T.3    Burchell, B.4
  • 21
    • 0029956992 scopus 로고    scopus 로고
    • Mutational analysis of the carboxy-terminal region of UDP-glucuronosyltransferase 2B1
    • Meech R., Yogalingam G., Mackenzie P.I. Mutational analysis of the carboxy-terminal region of UDP-glucuronosyltransferase 2B1. DNA Cell Biol. 15:1996;489-494.
    • (1996) DNA Cell Biol. , vol.15 , pp. 489-494
    • Meech, R.1    Yogalingam, G.2    MacKenzie, P.I.3
  • 22
    • 0030879658 scopus 로고    scopus 로고
    • A critical amino acid residue, Asp446, in UDP-glucuronosyltransferase
    • Iwano H., Yokota H., Ohgiya S., Yotumoto N., Yuasa A. A critical amino acid residue, Asp446, in UDP-glucuronosyltransferase. Biochem. J. 325:1997;587-591.
    • (1997) Biochem. J. , vol.325 , pp. 587-591
    • Iwano, H.1    Yokota, H.2    Ohgiya, S.3    Yotumoto, N.4    Yuasa, A.5
  • 24
    • 0027339015 scopus 로고
    • Engineered yeast cells as model to study coupling between human xenobiotic metabolizing enzymes: Simulation of the two first steps of benzo[a]pyrene activation
    • Gautier J.-C., Urban P., Beaune P., Pompon D. Engineered yeast cells as model to study coupling between human xenobiotic metabolizing enzymes: simulation of the two first steps of benzo[a]pyrene activation. Eur. J. Biochem. 211:1993;63-72.
    • (1993) Eur. J. Biochem. , vol.211 , pp. 63-72
    • Gautier, J.-C.1    Urban, P.2    Beaune, P.3    Pompon, D.4
  • 25
    • 0029964690 scopus 로고    scopus 로고
    • Simulation of human benzo[a]pyrene metabolism deduced from the analysis of individual kinetic steps in recombinant yeast
    • Gautier J.-C., Urban P., Beaune P., Pompon D. Simulation of human benzo[a]pyrene metabolism deduced from the analysis of individual kinetic steps in recombinant yeast. Chem. Res. Toxicol. 9:1996;418-425.
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 418-425
    • Gautier, J.-C.1    Urban, P.2    Beaune, P.3    Pompon, D.4
  • 26
    • 0025240539 scopus 로고
    • Expression of UDP-glucuronosyltransferase cDNA in Saccharomyces cerevisiae as a membrane-bound and as a cytosolic form
    • Toghrol F., Kimura T., Owens I.S. Expression of UDP- glucuronosyltransferase cDNA in Saccharomyces cerevisiae as a membrane-bound and as a cytosolic form. Biochemistry. 29:1990;2349-2356.
    • (1990) Biochemistry , vol.29 , pp. 2349-2356
    • Toghrol, F.1    Kimura, T.2    Owens, I.S.3
  • 27
    • 0033615624 scopus 로고    scopus 로고
    • An internal signal sequence mediates the targeting and retention of the human UDP-glucuronosyltransferase 1A6 to the endoplasmic reticulum
    • Ouzzine M., Magdalou J., Burchell B., Fournel-Gigleux S. An internal signal sequence mediates the targeting and retention of the human UDP-glucuronosyltransferase 1A6 to the endoplasmic reticulum. J. Biol. Chem. 274:1999;31401-31409.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31401-31409
    • Ouzzine, M.1    Magdalou, J.2    Burchell, B.3    Fournel-Gigleux, S.4
  • 28
    • 0026088568 scopus 로고
    • Interactions among cytochromes P-450 in the endoplasmic reticulum: Detection of chemically cross-linked complexes with monoclonal antibodies
    • Alston K., Robinson R.C., Park S.S., Gelboin H.V., Friedman F.K. Interactions among cytochromes P-450 in the endoplasmic reticulum: detection of chemically cross-linked complexes with monoclonal antibodies. J. Biol. Chem. 266:1991;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
  • 29
    • 0026610271 scopus 로고
    • Adrenal P-450scc modulates activity of P-45011 β in liposomal and mitochondrial membranes: Implication of P-450scc in zone specificity of aldosterone biosynthesis in bovine adrenal
    • Ikushiro S., Kominami S., Takemori S. Adrenal P-450scc modulates activity of P-45011 β in liposomal and mitochondrial membranes: Implication of P-450scc in zone specificity of aldosterone biosynthesis in bovine adrenal. J. Biol. Chem. 267:1992;1464-1469.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1464-1469
    • Ikushiro, S.1    Kominami, S.2    Takemori, S.3
  • 30
    • 0031010059 scopus 로고    scopus 로고
    • Protein-protein interactions between UDP-glucuronosyltransferase isozymes in rat hepatic microsomes
    • Ikushiro S., Emi Y., Iyanagi T. Protein-protein interactions between UDP-glucuronosyltransferase isozymes in rat hepatic microsomes. Biochemistry. 36:1997;7154-7161.
    • (1997) Biochemistry , vol.36 , pp. 7154-7161
    • Ikushiro, S.1    Emi, Y.2    Iyanagi, T.3
  • 31
    • 0034752769 scopus 로고    scopus 로고
    • Simultaneous expression of guinea pig UDP-glucuronosyltransferase 2B21 and 2B22 in COS-7 cells enhances UDP-glucuronosyltransferase2B21-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., Oguri K. Simultaneous expression of guinea pig UDP-glucuronosyltransferase 2B21 and 2B22 in COS-7 cells enhances UDP-glucuronosyltransferase2B21-catalyzed morphine-6-glucuronide formation. Mol. Pharmacol. 60:2001;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    Oguri, K.11
  • 32
    • 0037408258 scopus 로고    scopus 로고
    • Organization of multiple cytochrome P450s with NADPH-cytochrome P450 reductase in membranes
    • Backes W.L., Kelley R.W. Organization of multiple cytochrome P450s with NADPH-cytochrome P450 reductase in membranes. Pharmacol. Ther. 98:2003;221-233.
    • (2003) Pharmacol. Ther. , vol.98 , pp. 221-233
    • Backes, W.L.1    Kelley, R.W.2
  • 33
    • 0026043538 scopus 로고
    • Rotation and interaction with epoxide hydrase of cytochrome P-450 in proteoliposomes
    • Etter H.U., Richter C., Ohta Y., Winterhalter K.H., Sasabe H., Kawato S. Rotation and interaction with epoxide hydrase of cytochrome P-450 in proteoliposomes. J. Biol. Chem. 266:1991;18600-18605.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18600-18605
    • Etter, H.U.1    Richter, C.2    Ohta, Y.3    Winterhalter, K.H.4    Sasabe, H.5    Kawato, S.6
  • 34
    • 1942532106 scopus 로고    scopus 로고
    • Cytochrome P450 1A1 (CYP1A1) inhibitor α-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 M., Oguri K., Yamada H. Cytochrome P450 1A1 (CYP1A1) inhibitor α-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. 27:2004;56-60.
    • (2004) Biol. Pharm. Bull. , vol.27 , pp. 56-60
    • Taura, K.1    Naito, E.2    Ishii, Y.3    Mori, M.4    Oguri, K.5    Yamada, H.6


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