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Volumn 289, Issue 2, 1999, Pages 661-667

Competition between cytochrome P-450 isozymes for NADPH-cytochrome P- 450 oxidoreductase affects drug metabolism

Author keywords

[No Author keywords available]

Indexed keywords

7 ETHOXYRESORUFIN O DEALKYLASE; BUFURALOL; BUFURALOL 1' HYDROXYLASE; COUMARIN 7 HYDROXYLASE; CYTOCHROME P450; CYTOCHROME P450 3A4; CYTOCHROME P450 ISOENZYME; DEBRISOQUINE 4 HYDROXYLASE; DRUG METABOLIZING ENZYME; LIVER ENZYME; NADPH CYTOCHROME P450 OXIDOREDUCTASE; TESTOSTERONE; UNCLASSIFIED DRUG;

EID: 0032954374     PISSN: 00223565     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Conference Paper
Times cited : (40)

References (32)
  • 1
    • 0024565227 scopus 로고
    • Cytochrome P450 LM2 reduction: Substrate effects on the rate of reductase-LM2 association
    • Backes WL and Eyer CS (1989) Cytochrome P450 LM2 reduction: Substrate effects on the rate of reductase-LM2 association. J Biol Chem 264:6252-6259.
    • (1989) J Biol Chem , vol.264 , pp. 6252-6259
    • Backes, W.L.1    Eyer, C.S.2
  • 2
    • 0025994649 scopus 로고
    • Expression and enzymatic activity of recombinant cytochrome P450 17α-hydroxylase in Escherichia coli
    • Barnes HJ, Arlotto MF and Waterman MR (1991) Expression and enzymatic activity of recombinant cytochrome P450 17α-hydroxylase in Escherichia coli. Proc Natl Acad Sci USA 88:5597-5601.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5597-5601
    • Barnes, H.J.1    Arlotto, M.F.2    Waterman, M.R.3
  • 3
    • 0030592712 scopus 로고    scopus 로고
    • Coexpression of a human P450 (CYP3A4) and P450 reductase generates a highly functional monooxygenase system in Escherichia coli
    • Blake JAR, Pritchard M, Ding S, Smith GCM, Burchell B, Wolf CR and Friedberg T (1996) Coexpression of a human P450 (CYP3A4) and P450 reductase generates a highly functional monooxygenase system in Escherichia coli. FEBS Lett 397:210-214.
    • (1996) FEBS Lett , vol.397 , pp. 210-214
    • Blake, J.A.R.1    Pritchard, M.2    Ding, S.3    Smith, G.C.M.4    Burchell, B.5    Wolf, C.R.6    Friedberg, T.7
  • 5
    • 0016754798 scopus 로고
    • Inherent specificities of purified cytochromes P-450 and P-448 toward biphenyl hydroxylation and ethoxyresorufin deethylation
    • Burke MD and Mayer RT (1975) Inherent specificities of purified cytochromes P-450 and P-448 toward biphenyl hydroxylation and ethoxyresorufin deethylation. Drug Metab Dispos 3:245-253.
    • (1975) Drug Metab Dispos , vol.3 , pp. 245-253
    • Burke, M.D.1    Mayer, R.T.2
  • 6
    • 0028943584 scopus 로고
    • Substrate dependent competition of different P450 isozymes for limiting NADPH-cytochrome P450 reductase
    • Cawley GF, Batie CJ and Backes WL (1995) Substrate dependent competition of different P450 isozymes for limiting NADPH-cytochrome P450 reductase. Biochemistry 34:1244-1247.
    • (1995) Biochemistry , vol.34 , pp. 1244-1247
    • Cawley, G.F.1    Batie, C.J.2    Backes, W.L.3
  • 7
    • 0031574146 scopus 로고    scopus 로고
    • High levels of recombinant CYP3A4 expression in Chinese hamster ovary cells are modulated by coexpressed human P450 reductase and by hemin supplementation
    • Ding S, Yao D, Burchell B, Wolf CR and Friedberg T (1997) High levels of recombinant CYP3A4 expression in Chinese hamster ovary cells are modulated by coexpressed human P450 reductase and by hemin supplementation. Arch Biochem Biophys 348:403-410.
    • (1997) Arch Biochem Biophys , vol.348 , pp. 403-410
    • Ding, S.1    Yao, D.2    Burchell, B.3    Wolf, C.R.4    Friedberg, T.5
  • 8
    • 0027404804 scopus 로고
    • Fluidity of the microsomal membrane and cytochrome P450 reduction kinetics of pig liver microsomes as a consequence of organic solvent impact
    • Engelke M, Bergmann U and Diehl HA (1993) Fluidity of the microsomal membrane and cytochrome P450 reduction kinetics of pig liver microsomes as a consequence of organic solvent impact. Xenobiotica 23:71-78.
    • (1993) Xenobiotica , vol.23 , pp. 71-78
    • Engelke, M.1    Bergmann, U.2    Diehl, H.A.3
  • 10
    • 0030588661 scopus 로고    scopus 로고
    • Recombinant-DNA technology as an investigative tool in drug-metabolism research
    • Friedberg T and Wolf CR (1996) Recombinant-DNA technology as an investigative tool in drug-metabolism research. Adv Drug Deliv Rev 22:187-213.
    • (1996) Adv Drug Deliv Rev , vol.22 , pp. 187-213
    • Friedberg, T.1    Wolf, C.R.2
  • 11
    • 0027223881 scopus 로고
    • Expression of modified human cytochrome-P450 3A4 in Escherichia-coli and purification and reconstitution of the enzyme
    • Gillam EMJ, Baba T, Kim BR, Ohmori S and Guengerich FP (1993) Expression of modified human cytochrome-P450 3A4 in Escherichia-coli and purification and reconstitution of the enzyme. Arch Biochem Biophys 305:123-131.
    • (1993) Arch Biochem Biophys , vol.305 , pp. 123-131
    • Gillam, E.M.J.1    Baba, T.2    Kim, B.R.3    Ohmori, S.4    Guengerich, F.P.5
  • 12
    • 0026651273 scopus 로고
    • Human cytochromes P450: Problems and prospects
    • Gonzalez FJ (1992) Human cytochromes P450: Problems and prospects. Trends Pharmacol Sci 12:346-352.
    • (1992) Trends Pharmacol Sci , vol.12 , pp. 346-352
    • Gonzalez, F.J.1
  • 13
    • 0030781147 scopus 로고    scopus 로고
    • Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase: Rapid reduction in the absence of substrate and variations among cytochrome P450 systems
    • Guengerich FP and Johnson WW (1997) Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase: Rapid reduction in the absence of substrate and variations among cytochrome P450 systems. Biochemistry 36:14741-14750.
    • (1997) Biochemistry , vol.36 , pp. 14741-14750
    • Guengerich, F.P.1    Johnson, W.W.2
  • 14
    • 0018728084 scopus 로고
    • The effects of incorporation into microsomes of purified NADPH-cytochrome c (P-450) reductase on drug oxidations
    • Kitada M, Kitagawa H and Kamataki T (1979) The effects of incorporation into microsomes of purified NADPH-cytochrome c (P-450) reductase on drug oxidations. Biochem Pharmacol 28:2670-2673.
    • (1979) Biochem Pharmacol , vol.28 , pp. 2670-2673
    • Kitada, M.1    Kitagawa, H.2    Kamataki, T.3
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.1
  • 16
    • 0029012009 scopus 로고
    • CYP3A4 expressed by insect cells infected with a recombinant baculovirus containing both CYP3A4 and human NADPH-cytochrome P450 reductase is catalytically similar to human liver microsomal CYP3A4
    • Lee CA, Kadwell SH, Kost TA and Serabjit-Singh CJ (1995) CYP3A4 expressed by insect cells infected with a recombinant baculovirus containing both CYP3A4 and human NADPH-cytochrome P450 reductase is catalytically similar to human liver microsomal CYP3A4. Arch Biochem Biophys 319:157-167.
    • (1995) Arch Biochem Biophys , vol.319 , pp. 157-167
    • Lee, C.A.1    Kadwell, S.H.2    Kost, T.A.3    Serabjit-Singh, C.J.4
  • 17
    • 0025939628 scopus 로고
    • Identification and characterization of an NADPH-cytochrome P450 reductase derived peptide involved in binding to cytochrome P450
    • Nadler SG and Strobel HW (1991) Identification and characterization of an NADPH-cytochrome P450 reductase derived peptide involved in binding to cytochrome P450. Arch Biochem Biophys 290:277-284.
    • (1991) Arch Biochem Biophys , vol.290 , pp. 277-284
    • Nadler, S.G.1    Strobel, H.W.2
  • 20
    • 0002030427 scopus 로고
    • Enzyme induction in the cytochrome P450 system
    • Kalow W ed Pergamon Press, New York
    • Okey AB (1992) Enzyme induction in the cytochrome P450 system, in Pharmacogenetics of Drug Metabolism (Kalow W ed) pp 549-608, Pergamon Press, New York.
    • (1992) Pharmacogenetics of Drug Metabolism , pp. 549-608
    • Okey, A.B.1
  • 21
    • 78651165715 scopus 로고
    • The carbon monoxide binding pigment of liver microsomes
    • Omura T and Sato R (1964) The carbon monoxide binding pigment of liver microsomes. J Biol Chem 239:2370-2378.
    • (1964) J Biol Chem , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 22
    • 0018801361 scopus 로고
    • Kinetics of reduction of cytochrome P-450LM4 in a reconstituted liver microsomal enzyme system
    • Oprian DD, Vatsis KP and Coon MJ (1979) Kinetics of reduction of cytochrome P-450LM4 in a reconstituted liver microsomal enzyme system. J Biol Chem 254: 8895-8902.
    • (1979) J Biol Chem , vol.254 , pp. 8895-8902
    • Oprian, D.D.1    Vatsis, Kp.2    Coon, M.J.3
  • 23
    • 0000106986 scopus 로고    scopus 로고
    • Biotransformation of xenobiotics
    • Klaassen CD, Amdur MO and Doull JD eds McGraw-Hill, New York
    • Parkinson A (1996) Biotransformation of xenobiotics, in Casarett and Doull's Toxicology: The Basic Science of Poisons (Klaassen CD, Amdur MO and Doull JD eds) pp 113-186, McGraw-Hill, New York.
    • (1996) Casarett and Doull's Toxicology: The Basic Science of Poisons , pp. 113-186
    • Parkinson, A.1
  • 24
    • 0017112947 scopus 로고
    • Temperature dependence of cytochrome P-450 reduction. A model for NADPH-cytochrome P-450 reductase:Cytochrome P-450 interaction
    • Peterson JA, Ebel RE, O'Keeffe DH, Matsubara T and Estabrook RW (1976) Temperature dependence of cytochrome P-450 reduction. A model for NADPH-cytochrome P-450 reductase:cytochrome P-450 interaction. J Biol Chem 251:4010-4016.
    • (1976) J Biol Chem , vol.251 , pp. 4010-4016
    • Peterson, J.A.1    Ebel, R.E.2    O'Keeffe, D.H.3    Matsubara, T.4    Estabrook, R.W.5
  • 25
    • 0025784027 scopus 로고
    • Cytochrome P450: Multiplicity of isoformes, substrates, and catalytic and regulatory mechanisms
    • Porter TD and Coon MJ (1991) Cytochrome P450: Multiplicity of isoformes, substrates, and catalytic and regulatory mechanisms. J Biol Chem 266:13469-13472.
    • (1991) J Biol Chem , vol.266 , pp. 13469-13472
    • Porter, T.D.1    Coon, M.J.2
  • 27
    • 0031572185 scopus 로고    scopus 로고
    • A general strategy for the expression of recombinant human cytochrome P450s in Escherichia coli using bacterial signal peptidea: Expression of CYP3A4, CYP2A6, and CYP2E1
    • Pritchard MP, Ossetian R, Li DN, Henderson CJ, Burchell B, Wolf CR and Friedberg T (1997) A general strategy for the expression of recombinant human cytochrome P450s in Escherichia coli using bacterial signal peptidea: Expression of CYP3A4, CYP2A6, and CYP2E1. Arch Biochem Biophys 345:342-354.
    • (1997) Arch Biochem Biophys , vol.345 , pp. 342-354
    • Pritchard, M.P.1    Ossetian, R.2    Li, D.N.3    Henderson, C.J.4    Burchell, B.5    Wolf, C.R.6    Friedberg, T.7
  • 28
    • 0017795019 scopus 로고
    • Purification and properties of NADPH-cytochrome P450 reductase
    • Strobel HW and Dignam JD (1978) Purification and properties of NADPH-cytochrome P450 reductase. Methods Enzymol 52:89-96.
    • (1978) Methods Enzymol , vol.52 , pp. 89-96
    • Strobel, H.W.1    Dignam, J.D.2
  • 29
    • 0031172743 scopus 로고    scopus 로고
    • Competitive interactions between cytochromes P450 2A6 and 2E1 for NADPH-cytochrome P450 oxidoreductase in the microsomal membranes produced by a baculovirus expression system
    • Tan Y, Patten CJ, Smith T and Yang CS (1997) Competitive interactions between cytochromes P450 2A6 and 2E1 for NADPH-cytochrome P450 oxidoreductase in the microsomal membranes produced by a baculovirus expression system. Arch Biochem Biophys 342:82-91.
    • (1997) Arch Biochem Biophys , vol.342 , pp. 82-91
    • Tan, Y.1    Patten, C.J.2    Smith, T.3    Yang, C.S.4
  • 30
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T and Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc Natl Acad Sci USA 76:4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 31
    • 0029021289 scopus 로고
    • Dynamic interactions of rabbit liver cytochromes P450IA2 and P450IIB4 with cytochrome b5 and NADPH-cytochrome P450 reductase in proteoliposomes
    • Yamada M, Ohta Y, Bachmanova GI, Nishimoto Y, Archakov AI and Kawato S (1995) Dynamic interactions of rabbit liver cytochromes P450IA2 and P450IIB4 with cytochrome b5 and NADPH-cytochrome P450 reductase in proteoliposomes. Biochemistry 34:10113-10119.
    • (1995) Biochemistry , vol.34 , pp. 10113-10119
    • Yamada, M.1    Ohta, Y.2    Bachmanova, G.I.3    Nishimoto, Y.4    Archakov, A.I.5    Kawato, S.6
  • 32
    • 0025841777 scopus 로고
    • Purification and characterization of human liver microsomal cytochrome P-450 2A6
    • Yun CH, Shimada T and Guengerich FP (1991) Purification and characterization of human liver microsomal cytochrome P-450 2A6. Mol Pharmacol 40:679-685.
    • (1991) Mol Pharmacol , vol.40 , pp. 679-685
    • Yun, Ch.1    Shimada, T.2    Guengerich, F.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.