메뉴 건너뛰기




Volumn 86, Issue , 2012, Pages 87-91

Drug-drug interactions and cooperative effects detected in electrochemically driven human cytochrome P450 3A4

Author keywords

Chronoamperometry; Cytochrome P450; Glassy carbon; Inhibition; Protein immobilization

Indexed keywords

ADVERSE DRUG REACTIONS; BIOELECTROCHEMISTRY; CATIONIC POLYELECTROLYTE; COOPERATIVE EFFECTS; COOPERATIVITY; CYTOCHROME P450; CYTOCHROME P450-3A4; DICLOFENAC; DRUG METABOLISMS; DRUG-DRUG INTERACTIONS; GLASSY CARBON ELECTRODES; HUMAN CYTOCHROME; IN-VITRO; POLY (DIALLYLDIMETHYLAMMONIUM CHLORIDE); PROTEIN IMMOBILIZATION;

EID: 84860270945     PISSN: 15675394     EISSN: 1878562X     Source Type: Journal    
DOI: 10.1016/j.bioelechem.2012.02.010     Document Type: Article
Times cited : (48)

References (32)
  • 3
    • 27644596457 scopus 로고    scopus 로고
    • Predicting in vivo drug interactions from in vitro drug discovery data
    • Wienkers L.C., Health T.G. Predicting in vivo drug interactions from in vitro drug discovery data. Nature Reviews. Drug Discovery 2005, 4:825-833.
    • (2005) Nature Reviews. Drug Discovery , vol.4 , pp. 825-833
    • Wienkers, L.C.1    Health, T.G.2
  • 4
    • 85146106485 scopus 로고    scopus 로고
    • In vitro approaches for studying the inhibition of drug-metabolizing enzymes and identifying the drug-metabolizing enzymes responsible for the metabolism of drugs (reaction phenotyping) with emphasis on cytochrome P450
    • Informa Healthcare, New York, A.D. Rodrigues (Ed.)
    • Ogilvie B.W., Usuki E., Yerino P., Parkinson A. In vitro approaches for studying the inhibition of drug-metabolizing enzymes and identifying the drug-metabolizing enzymes responsible for the metabolism of drugs (reaction phenotyping) with emphasis on cytochrome P450. Drug-Drug Interactions 2008, 231-358. Informa Healthcare, New York. A.D. Rodrigues (Ed.).
    • (2008) Drug-Drug Interactions , pp. 231-358
    • Ogilvie, B.W.1    Usuki, E.2    Yerino, P.3    Parkinson, A.4
  • 5
    • 13844308070 scopus 로고    scopus 로고
    • Non-Michaelis-Menten kinetics in cytochrome P450-catalysed reactions
    • Atkins W.M. Non-Michaelis-Menten kinetics in cytochrome P450-catalysed reactions. Annual Review of Pharmacology and Toxicology 2005, 45:291-310.
    • (2005) Annual Review of Pharmacology and Toxicology , vol.45 , pp. 291-310
    • Atkins, W.M.1
  • 6
    • 78650330724 scopus 로고    scopus 로고
    • Cytochromes P450: tayloring a class of enzymes for biosensing
    • RSC Publishing, London, J. Davis (Ed.)
    • Dodhia V.R., Gilardi G. Cytochromes P450: tayloring a class of enzymes for biosensing. Engineering the Bioelectronic Interface 2009, 154-193. RSC Publishing, London. J. Davis (Ed.).
    • (2009) Engineering the Bioelectronic Interface , pp. 154-193
    • Dodhia, V.R.1    Gilardi, G.2
  • 7
    • 78649449776 scopus 로고    scopus 로고
    • Breakthrough in P450 bioelectrochemistry and future perspectives
    • Sadeghi S.J., Fantuzzi A., Gilardi G. Breakthrough in P450 bioelectrochemistry and future perspectives. Biochimica et Biophysica Acta 2011, 1814:237-248.
    • (2011) Biochimica et Biophysica Acta , vol.1814 , pp. 237-248
    • Sadeghi, S.J.1    Fantuzzi, A.2    Gilardi, G.3
  • 8
    • 84892246340 scopus 로고    scopus 로고
    • Human cytochrome P450 enzymes
    • Kluwer Academic/Plenum Press, New York, P.R. Ortiz de Montellano (Ed.)
    • Guengerich F.P. Human cytochrome P450 enzymes. Cytochrome P450: Structure, Mechanism, and Biochemistry 2005, 377-530. Kluwer Academic/Plenum Press, New York. P.R. Ortiz de Montellano (Ed.).
    • (2005) Cytochrome P450: Structure, Mechanism, and Biochemistry , pp. 377-530
    • Guengerich, F.P.1
  • 9
    • 33748366369 scopus 로고    scopus 로고
    • Engineering human cytochrome P450 enzymes into catalytically self-sufficient chimeras using molecular Lego
    • Dodhia V.R., Fantuzzi A., Gilardi G. Engineering human cytochrome P450 enzymes into catalytically self-sufficient chimeras using molecular Lego. Journal of Biological Inorganic Chemistry 2006, 11:903-916.
    • (2006) Journal of Biological Inorganic Chemistry , vol.11 , pp. 903-916
    • Dodhia, V.R.1    Fantuzzi, A.2    Gilardi, G.3
  • 10
    • 77049138167 scopus 로고
    • The colourimetric estimation of formaldehyde by means of the Hantzsch reaction
    • Nash T. The colourimetric estimation of formaldehyde by means of the Hantzsch reaction. Biochemical Journal 1953, 55:416-421.
    • (1953) Biochemical Journal , vol.55 , pp. 416-421
    • Nash, T.1
  • 11
  • 12
    • 18744432274 scopus 로고    scopus 로고
    • Enzyme electrokinetics: using protein film voltammetry to investigate redox enzymes and their mechanisms
    • Léger C., Elliott S.J., Hoke K.R., Jeuken L.J.C., Jones A.K., Armstrong F.A. Enzyme electrokinetics: using protein film voltammetry to investigate redox enzymes and their mechanisms. Biochemistry 2003, 42:8653-8662.
    • (2003) Biochemistry , vol.42 , pp. 8653-8662
    • Léger, C.1    Elliott, S.J.2    Hoke, K.R.3    Jeuken, L.J.C.4    Jones, A.K.5    Armstrong, F.A.6
  • 14
    • 38849106780 scopus 로고    scopus 로고
    • Comparison of kinetic parameters for drug oxidation rates and substrate inhibition potential mediated by cytochrome P450 3A4 and 3A5
    • Niwa T., Murayama N., Emoto C., Yamazaki H. Comparison of kinetic parameters for drug oxidation rates and substrate inhibition potential mediated by cytochrome P450 3A4 and 3A5. Current Drug Metabolism 2008, 9:20-33.
    • (2008) Current Drug Metabolism , vol.9 , pp. 20-33
    • Niwa, T.1    Murayama, N.2    Emoto, C.3    Yamazaki, H.4
  • 15
    • 45249121177 scopus 로고    scopus 로고
    • Drugs behave as substrates, inhibitors and inducers of human cytochrome P450 3A4
    • Zhou S. Drugs behave as substrates, inhibitors and inducers of human cytochrome P450 3A4. Current Drug Metabolism 2008, 9:310-322.
    • (2008) Current Drug Metabolism , vol.9 , pp. 310-322
    • Zhou, S.1
  • 16
    • 0030470211 scopus 로고    scopus 로고
    • Immobilization of enzymes on lipid bilayers on a metal support allows study of the biophysical mechanisms of enzymatic reactions
    • Hianik T., Snejdárková M., Passechnik V.I., Rehák M., Babincová M. Immobilization of enzymes on lipid bilayers on a metal support allows study of the biophysical mechanisms of enzymatic reactions. Bioelectrochemistry and Bioenergetics 1996, 41:221-225.
    • (1996) Bioelectrochemistry and Bioenergetics , vol.41 , pp. 221-225
    • Hianik, T.1    Snejdárková, M.2    Passechnik, V.I.3    Rehák, M.4    Babincová, M.5
  • 17
    • 0031432829 scopus 로고    scopus 로고
    • In vitro analysis of the activity of the major human hepatic CYP enzyme (CYP3A4) using [N-methyl-C-14]-erythromycin
    • Riley R.J., Howbrook D. In vitro analysis of the activity of the major human hepatic CYP enzyme (CYP3A4) using [N-methyl-C-14]-erythromycin. Journal of Pharmacological and Toxicological Methods 1997, 38:189-193.
    • (1997) Journal of Pharmacological and Toxicological Methods , vol.38 , pp. 189-193
    • Riley, R.J.1    Howbrook, D.2
  • 19
    • 77953554845 scopus 로고    scopus 로고
    • Control of human cytochrome P450 2E1 electrocatalytic response as a result of unique orientation on gold electrodes
    • Mak L.H., Sadeghi S.J., Fantuzzi A., Gilardi G. Control of human cytochrome P450 2E1 electrocatalytic response as a result of unique orientation on gold electrodes. Analytical Chemistry 2010, 82:5357-5362.
    • (2010) Analytical Chemistry , vol.82 , pp. 5357-5362
    • Mak, L.H.1    Sadeghi, S.J.2    Fantuzzi, A.3    Gilardi, G.4
  • 20
    • 79954583659 scopus 로고    scopus 로고
    • Enzyme-based amperometric platform to determine the polymorphism response in drug metabolism by cytochromes P450
    • Panicco P., Dodhia V.R., Fantuzzi A., Gilardi G. Enzyme-based amperometric platform to determine the polymorphism response in drug metabolism by cytochromes P450. Analytical Chemistry 2011, 83:2179-2186.
    • (2011) Analytical Chemistry , vol.83 , pp. 2179-2186
    • Panicco, P.1    Dodhia, V.R.2    Fantuzzi, A.3    Gilardi, G.4
  • 21
    • 0036785511 scopus 로고    scopus 로고
    • Diclofenac-induced inactivation of CYP3A4 and its stimulation by quinidine
    • Masubuchi Y., Ose A., Horie T. Diclofenac-induced inactivation of CYP3A4 and its stimulation by quinidine. Drug Metabolism and Disposition 2002, 30:1143-1148.
    • (2002) Drug Metabolism and Disposition , vol.30 , pp. 1143-1148
    • Masubuchi, Y.1    Ose, A.2    Horie, T.3
  • 22
    • 9444257635 scopus 로고    scopus 로고
    • Identification and characterisation of potent CYP3A4 inhibitors in Schisandra fruit extract
    • Iwata H., Tezuka Y., Kadota S., Hiratsuka A., Watabe T. Identification and characterisation of potent CYP3A4 inhibitors in Schisandra fruit extract. Drug Metabolism and Disposition 2004, 32:1351-1358.
    • (2004) Drug Metabolism and Disposition , vol.32 , pp. 1351-1358
    • Iwata, H.1    Tezuka, Y.2    Kadota, S.3    Hiratsuka, A.4    Watabe, T.5
  • 23
    • 0028361593 scopus 로고
    • Inhibition of human CYP3A catalysed 1'-hydroxy midazolam formation by ketoconazole, nifedipine, erythromycin, cimetidine and nizatidine
    • Wrighton S.A., Ring B.J. Inhibition of human CYP3A catalysed 1'-hydroxy midazolam formation by ketoconazole, nifedipine, erythromycin, cimetidine and nizatidine. Pharmaceutical Research 1994, 11:921-924.
    • (1994) Pharmaceutical Research , vol.11 , pp. 921-924
    • Wrighton, S.A.1    Ring, B.J.2
  • 24
    • 0742287122 scopus 로고    scopus 로고
    • Drug-drug interactions evaluated by a highly active reconstituted native human cytochrome P450 3A4 and human NADPH-cytochrome P450 reductase system
    • Haehner T., Refaie M.O.I., Muller-Enoch D. Drug-drug interactions evaluated by a highly active reconstituted native human cytochrome P450 3A4 and human NADPH-cytochrome P450 reductase system. Arzneimittelforschung - Drug Research 2004, 54:78-83.
    • (2004) Arzneimittelforschung - Drug Research , vol.54 , pp. 78-83
    • Haehner, T.1    Refaie, M.O.I.2    Muller-Enoch, D.3
  • 25
    • 0032970480 scopus 로고    scopus 로고
    • Fully automated analysis of activities catalysed by the major human liver cytochrome P450 enzymes: assessment of human CYP inhibition potential
    • Moody G.C., Griffin S.J., Mather A.N., McGinnity D.F., Riley R.J. Fully automated analysis of activities catalysed by the major human liver cytochrome P450 enzymes: assessment of human CYP inhibition potential. Xenobiotica 1999, 29:53-75.
    • (1999) Xenobiotica , vol.29 , pp. 53-75
    • Moody, G.C.1    Griffin, S.J.2    Mather, A.N.3    McGinnity, D.F.4    Riley, R.J.5
  • 28
    • 0000574406 scopus 로고    scopus 로고
    • Evaluation of atypical cytochrome P450 kinetics with two-substrate models: evidence that multiple substrates can simultaneously bind to cytochromes P450 active sites
    • Korzekwa K.R., Krishnamachary N., Shou M., Ogai A., Parise R.A., Rettie A.E., Gonzalez F.J., Tracey T.S. Evaluation of atypical cytochrome P450 kinetics with two-substrate models: evidence that multiple substrates can simultaneously bind to cytochromes P450 active sites. Biochemistry 1998, 37:4137-4147.
    • (1998) Biochemistry , vol.37 , pp. 4137-4147
    • Korzekwa, K.R.1    Krishnamachary, N.2    Shou, M.3    Ogai, A.4    Parise, R.A.5    Rettie, A.E.6    Gonzalez, F.J.7    Tracey, T.S.8
  • 29
    • 0035910579 scopus 로고    scopus 로고
    • A kinetic model for the metabolic interaction of two substrates at the active site of cytochrome P450 3A4
    • Shou M., Dai R., Korzekwa K.R., Baillie T.A., Rushmore T.H. A kinetic model for the metabolic interaction of two substrates at the active site of cytochrome P450 3A4. Journal of Biological Chemistry 2001, 276:2256-2262.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 2256-2262
    • Shou, M.1    Dai, R.2    Korzekwa, K.R.3    Baillie, T.A.4    Rushmore, T.H.5
  • 30
    • 0035964178 scopus 로고    scopus 로고
    • Phenylalanine and tryptophan scanning mutagenesis of CYP3A4 substrate recognition site residues and effect on substrate oxidation and cooperativity
    • Domanski T.L., He Y.A., Khan K.K., Rousel F., Wang Q., Halpert J.R. Phenylalanine and tryptophan scanning mutagenesis of CYP3A4 substrate recognition site residues and effect on substrate oxidation and cooperativity. Biochemistry 2001, 40:10150-10160.
    • (2001) Biochemistry , vol.40 , pp. 10150-10160
    • Domanski, T.L.1    He, Y.A.2    Khan, K.K.3    Rousel, F.4    Wang, Q.5    Halpert, J.R.6
  • 31


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.