메뉴 건너뛰기




Volumn 34, Issue 10, 2006, Pages 1703-1712

Characterization of the rhesus monkey CYP3A64 enzyme: Species comparisons of CYP3A substrate specificity and kinetics using baculovirus-expressed recombinant enzymes

Author keywords

[No Author keywords available]

Indexed keywords

7 BENZOXY 4 TRIFLUORMETHYLCOUMARIN; COUMARIN; CYTOCHROME P450; CYTOCHROME P450 3A; CYTOCHROME P450 3A1; CYTOCHROME P450 3A12; CYTOCHROME P450 3A2; CYTOCHROME P450 3A26; CYTOCHROME P450 3A4; CYTOCHROME P450 3A5; CYTOCHROME P450 3A6; CYTOCHROME P450 3A64; CYTOCHROME P450 3A8; KETOCONAZOLE; MIDAZOLAM; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 10 1 1; NIFEDIPINE; RECOMBINANT ENZYME; TESTOSTERONE; UNCLASSIFIED DRUG;

EID: 33747846229     PISSN: 00909556     EISSN: 1521009X     Source Type: Journal    
DOI: 10.1124/dmd.106.009977     Document Type: Article
Times cited : (54)

References (43)
  • 1
    • 0028106482 scopus 로고
    • Cytochrome P450 specificities of alkoxyresorufin O-dealkylation in human and rat liver
    • Burke MD, Thompson S, Weaver RJ, Wolf CR, and Mayer RT (1994) Cytochrome P450 specificities of alkoxyresorufin O-dealkylation in human and rat liver. Biochem Pharmacol 48:923-936.
    • (1994) Biochem Pharmacol , vol.48 , pp. 923-936
    • Burke, M.D.1    Thompson, S.2    Weaver, R.J.3    Wolf, C.R.4    Mayer, R.T.5
  • 2
    • 0032866401 scopus 로고    scopus 로고
    • The use of heterologously expressed drug metabolizing enzymes-state of the art and prospects for the future
    • Crespi CL and Miller VP (1999) The use of heterologously expressed drug metabolizing enzymes-state of the art and prospects for the future. Pharmacol Ther 84:121-131.
    • (1999) Pharmacol Ther , vol.84 , pp. 121-131
    • Crespi, C.L.1    Miller, V.P.2
  • 3
    • 0035197548 scopus 로고    scopus 로고
    • Identification of variants of CYP3A4 and characterization of their abilities to metabolize testosterone and chlorpyrifos
    • Dai D, Tang J, Rose R, Hodgson E, Bienstock RJ, Mohrenweiser HW, and Goldstein JA (2001) Identification of variants of CYP3A4 and characterization of their abilities to metabolize testosterone and chlorpyrifos. J Pharmacol Exp Ther 299:825-831.
    • (2001) J Pharmacol Exp Ther , vol.299 , pp. 825-831
    • Dai, D.1    Tang, J.2    Rose, R.3    Hodgson, E.4    Bienstock, R.J.5    Mohrenweiser, H.W.6    Goldstein, J.A.7
  • 4
    • 0035964178 scopus 로고    scopus 로고
    • Phenylalanine and tryptophan scanning mutagenesis of CYP3A4 substrate recognition site residues and effect on substrate oxidation and cooperativity
    • Domanski TL, He YA, Khan KK, Roussel F, Wang Q, and Halpert JR (2001) Phenylalanine and tryptophan scanning mutagenesis of CYP3A4 substrate recognition site residues and effect on substrate oxidation and cooperativity. Biochemistry 40:10150-10160.
    • (2001) Biochemistry , vol.40 , pp. 10150-10160
    • Domanski, T.L.1    He, Y.A.2    Khan, K.K.3    Roussel, F.4    Wang, Q.5    Halpert, J.R.6
  • 5
    • 0029790347 scopus 로고    scopus 로고
    • Inhibition and kinetics of cytochrome P4503A activity in microsomes from rat, human, and cDNA-expressed human cytochrome P450
    • Ghosal A, Satoh H, Thomas PE, Bush E, and Moore D (1996) Inhibition and kinetics of cytochrome P4503A activity in microsomes from rat, human, and cDNA-expressed human cytochrome P450. Drug Metab Dispos 24:940-947.
    • (1996) Drug Metab Dispos , vol.24 , pp. 940-947
    • Ghosal, A.1    Satoh, H.2    Thomas, P.E.3    Bush, E.4    Moore, D.5
  • 7
    • 0028234586 scopus 로고
    • Regioselective biotransformation of midazolam by members of the human cytochrome P450 3A (CYP3A) subfamily
    • Gorski JC, Hall SD, Jones DR, VandenBranden M, and Wrighton SA (1994) Regioselective biotransformation of midazolam by members of the human cytochrome P450 3A (CYP3A) subfamily. Biochem Pharmacol 47:1643-1653.
    • (1994) Biochem Pharmacol , vol.47 , pp. 1643-1653
    • Gorski, J.C.1    Hall, S.D.2    Jones, D.R.3    VandenBranden, M.4    Wrighton, S.A.5
  • 11
    • 0036178095 scopus 로고    scopus 로고
    • Midazolam oxidation by cytochrome P450 3A4 and active-site mutants: An evaluation of multiple binding sites and of the metabolic pathway that leads to enzyme inactivation
    • Khan KK, He YQ, Domanski TL, and Halpert JR (2002) Midazolam oxidation by cytochrome P450 3A4 and active-site mutants: an evaluation of multiple binding sites and of the metabolic pathway that leads to enzyme inactivation. Mol Pharmacol 61:495-506.
    • (2002) Mol Pharmacol , vol.61 , pp. 495-506
    • Khan, K.K.1    He, Y.Q.2    Domanski, T.L.3    Halpert, J.R.4
  • 12
    • 0027050579 scopus 로고
    • Molecular cloning of monkey liver cytochrome P-450 cDNAs: Similarity of the primary sequences to human cytochromes P-450
    • Komori M, Kikuchi O, Sakuma T, Funaki J, Kitada M, and Kamataki T (1992) Molecular cloning of monkey liver cytochrome P-450 cDNAs: similarity of the primary sequences to human cytochromes P-450. Biochim Biophys Acta 1171:141-146.
    • (1992) Biochim Biophys Acta , vol.1171 , pp. 141-146
    • Komori, M.1    Kikuchi, O.2    Sakuma, T.3    Funaki, J.4    Kitada, M.5    Kamataki, T.6
  • 13
    • 0000574406 scopus 로고    scopus 로고
    • Evaluation of atypical cytochrome P450 kinetics with two-substrate models: Evidence that multiple substrates can simultaneously bind to cytochrome P450 active sites
    • Korzekwa KR, Krishnamachary N, Shou M, Ogai A, Parise RA, Rettie AE, Gonzalez FJ, and Tracy TS (1998) Evaluation of atypical cytochrome P450 kinetics with two-substrate models: evidence that multiple substrates can simultaneously bind to cytochrome P450 active sites. Biochemistry 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    Tracy, T.S.8
  • 14
    • 0024373348 scopus 로고
    • Oxidation of midazolam and triazolam by human liver cytochrome P450IIIA4
    • Kronbach T, Mathys D, Umeno M, Gonzalez FJ, and Meyer UA (1989) Oxidation of midazolam and triazolam by human liver cytochrome P450IIIA4. Mol Pharmacol 36:89-96.
    • (1989) Mol Pharmacol , vol.36 , pp. 89-96
    • Kronbach, T.1    Mathys, D.2    Umeno, M.3    Gonzalez, F.J.4    Meyer, U.A.5
  • 15
    • 0036363648 scopus 로고    scopus 로고
    • Monkey hepatic microsomal alcohol oxygenase: Purification and characterization of a cytochrome P450 enzyme catalyzing the stereoselective oxidation of 7alpha- and 7beta-hydroxydelta8-tetrahydrocannabinol to 7-oxo-delta8-tetrahydrocannabinol
    • Matsunaga T, Iwawaki Y, Komura A, Watanabe K, Kageyama T, and Yamamoto I (2002) Monkey hepatic microsomal alcohol oxygenase: purification and characterization of a cytochrome P450 enzyme catalyzing the stereoselective oxidation of 7alpha- and 7beta-hydroxydelta8-tetrahydrocannabinol to 7-oxo-delta8-tetrahydrocannabinol. Biol Pharm Bull 25:42-47.
    • (2002) Biol Pharm Bull , vol.25 , pp. 42-47
    • Matsunaga, T.1    Iwawaki, Y.2    Komura, A.3    Watanabe, K.4    Kageyama, T.5    Yamamoto, I.6
  • 17
    • 0036285162 scopus 로고    scopus 로고
    • Evaluation of approach to predict the contribution of multiple cytochrome P450s in drug metabolism using relative activity factor: Effects of the differences in expression levels of NADPH-cytochrome P450 reductase and cytochrome b(5) in the expression system and the differences in the marker activities
    • Nakajima M, Tane K, Nakamura S, Shimada N, Yamazaki H, and Yokoi T (2002) Evaluation of approach to predict the contribution of multiple cytochrome P450s in drug metabolism using relative activity factor: effects of the differences in expression levels of NADPH-cytochrome P450 reductase and cytochrome b(5) in the expression system and the differences in the marker activities. J Pharm Sci 91:952-963.
    • (2002) J Pharm Sci , vol.91 , pp. 952-963
    • Nakajima, M.1    Tane, K.2    Nakamura, S.3    Shimada, N.4    Yamazaki, H.5    Yokoi, T.6
  • 18
    • 0027246658 scopus 로고
    • Purification and characterization of two forms of hepatic microsomal cytochrome P450 from untreated cynomolgus monkeys
    • Ohmori S, Horie T, Guengerich FP, Kiuchi M, and Kitada M (1993) Purification and characterization of two forms of hepatic microsomal cytochrome P450 from untreated cynomolgus monkeys. Arch Biochem Biophys 305:405-413.
    • (1993) Arch Biochem Biophys , vol.305 , pp. 405-413
    • Ohmori, S.1    Horie, T.2    Guengerich, F.P.3    Kiuchi, M.4    Kitada, M.5
  • 19
    • 0024386612 scopus 로고
    • Purification of cytochrome P-450 from polychlorinated biphenyl-treated crab-eating monkeys: High homology to a form of human cytochrome P-450
    • Ohta K, Kitada M, Hashizume T, Komori M, Ohi H, and Kamataki T (1989) Purification of cytochrome P-450 from polychlorinated biphenyl-treated crab-eating monkeys: high homology to a form of human cytochrome P-450. Biochim Biophys Acta 996:142-145.
    • (1989) Biochim Biophys Acta , vol.996 , pp. 142-145
    • Ohta, K.1    Kitada, M.2    Hashizume, T.3    Komori, M.4    Ohi, H.5    Kamataki, T.6
  • 20
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura T and Sato R (1964) The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. J Biol Chem 239:2370-2378.
    • (1964) J Biol Chem , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 21
    • 0037974573 scopus 로고    scopus 로고
    • In vitro metabolism of midazolam, triazolam, nifedipine, and testosterone by human liver microsomes and recombinant cytochromes P450: Role of CYP3A4 and CYP3A5
    • Patki KC, Von Moltke LL, and Greenblatt DJ (2003) In vitro metabolism of midazolam, triazolam, nifedipine, and testosterone by human liver microsomes and recombinant cytochromes P450: role of CYP3A4 and CYP3A5. Drug Metab Dispos 31:938-944.
    • (2003) Drug Metab Dispos , vol.31 , pp. 938-944
    • Patki, K.C.1    Von Moltke, L.L.2    Greenblatt, D.J.3
  • 22
    • 0032849211 scopus 로고    scopus 로고
    • Purification and characterization of the hepatic CYP2C and 3A isozymes from phenobarbitone pretreated rhesus monkey
    • Ramana KV and Kohli KK (1999) Purification and characterization of the hepatic CYP2C and 3A isozymes from phenobarbitone pretreated rhesus monkey. Mol Cell Biochem 198:79-88.
    • (1999) Mol Cell Biochem , vol.198 , pp. 79-88
    • Ramana, K.V.1    Kohli, K.K.2
  • 23
    • 0035699920 scopus 로고    scopus 로고
    • Triazolam substrate inhibition: Evidence of competition for heme-bound reactive oxygen within the CYP3A4 active site
    • Schrag ML and Wienkers LC (2001) Triazolam substrate inhibition: evidence of competition for heme-bound reactive oxygen within the CYP3A4 active site. Adv Exp Med Biol 500:347-350.
    • (2001) Adv Exp Med Biol , vol.500 , pp. 347-350
    • Schrag, M.L.1    Wienkers, L.C.2
  • 25
    • 0028838715 scopus 로고
    • Comparisons of phase I and phase II in vitro hepatic enzyme activities of human, dog, rhesus monkey, and cynomolgus monkey
    • Sharer JE, Shipley LA, Vandenbranden MR, Binkley SN, and Wrighton SA (1995) Comparisons of phase I and phase II in vitro hepatic enzyme activities of human, dog, rhesus monkey, and cynomolgus monkey. Drug Metab Dispos 23:1231-1241.
    • (1995) Drug Metab Dispos , vol.23 , pp. 1231-1241
    • Sharer, J.E.1    Shipley, L.A.2    Vandenbranden, M.R.3    Binkley, S.N.4    Wrighton, S.A.5
  • 26
    • 0028237729 scopus 로고
    • Interindividual variations in human liver cytochrome P-450 enzymes involved in the oxidation of drugs, carcinogens and toxic chemicals: Studies with liver microsomes of 30 Japanese and 30 Caucasians
    • Shimada T, Yamazaki H, Mimura M, Inui Y, and Guengerich F (1994) Interindividual variations in human liver cytochrome P-450 enzymes involved in the oxidation of drugs, carcinogens and toxic chemicals: studies with liver microsomes of 30 Japanese and 30 Caucasians. J Pharmacol Exp Ther 270:414-423.
    • (1994) J Pharmacol Exp Ther , vol.270 , pp. 414-423
    • Shimada, T.1    Yamazaki, H.2    Mimura, M.3    Inui, Y.4    Guengerich, F.5
  • 27
    • 0033564235 scopus 로고    scopus 로고
    • Sigmoidal kinetic model for two co-operative substrate-binding sites in a cytochrome P450 3A4 active site: An example of the metabolism of diazepam and its derivatives
    • Shou M, Mei Q, Ettore MW Jr, Dai R, Baillie TA, and Rushmore TH (1999) Sigmoidal kinetic model for two co-operative substrate-binding sites in a cytochrome P450 3A4 active site: an example of the metabolism of diazepam and its derivatives. Biochem J 340 (Pt 3):845-853.
    • (1999) Biochem J , vol.340 , Issue.3 PART , pp. 845-853
    • Shou, M.1    Mei, Q.2    Ettore Jr., M.W.3    Dai, R.4    Baillie, T.A.5    Rushmore, T.H.6
  • 29
    • 0027379798 scopus 로고
    • Comparison of human and rhesus monkey in vitro phase I and phase II hepatic drug metabolism activities
    • Stevens JC, Shipley LA, Cashman JR, Vandenbranden M, and Wrighton SA (1993) Comparison of human and rhesus monkey in vitro phase I and phase II hepatic drug metabolism activities. Drug Metab Dispos 21:753-760.
    • (1993) Drug Metab Dispos , vol.21 , pp. 753-760
    • Stevens, J.C.1    Shipley, L.A.2    Cashman, J.R.3    Vandenbranden, M.4    Wrighton, S.A.5
  • 30
  • 31
    • 0035987896 scopus 로고    scopus 로고
    • Cytochrome P450 fluorometric substrates: Identification of isoform-selective probes for rat CYP2D2 and human CYP3A4
    • Stresser DM, Turner SD, Blanchard AP, Miller VP, and Crespi CL (2002) Cytochrome P450 fluorometric substrates: identification of isoform-selective probes for rat CYP2D2 and human CYP3A4. Drug Metab Dispos 30:845-852.
    • (2002) Drug Metab Dispos , vol.30 , pp. 845-852
    • Stresser, D.M.1    Turner, S.D.2    Blanchard, A.P.3    Miller, V.P.4    Crespi, C.L.5
  • 32
    • 0031748173 scopus 로고    scopus 로고
    • In vitro and in vivo drug interactions involving human CYP3A
    • Thummel KE and Wilkinson GR (1998) In vitro and in vivo drug interactions involving human CYP3A. Annu Rev Pharmacol Toxicol 38:389-430.
    • (1998) Annu Rev Pharmacol Toxicol , vol.38 , pp. 389-430
    • Thummel, K.E.1    Wilkinson, G.R.2
  • 33
    • 0031028518 scopus 로고    scopus 로고
    • Cooperativity in oxidations catalyzed by cytochrome P450 3A4
    • Ueng YF, Kuwabara T, Chun YJ, and Guengerich FP (1997) Cooperativity in oxidations catalyzed by cytochrome P450 3A4. Biochemistry 36:370-381.
    • (1997) Biochemistry , vol.36 , pp. 370-381
    • Ueng, Y.F.1    Kuwabara, T.2    Chun, Y.J.3    Guengerich, F.P.4
  • 34
    • 0018220868 scopus 로고
    • Identification of the high and low potential flavins of liver microsomal NADPH-cytochrome P-450 reductase
    • Vermilion JL and Coon MJ (1978) Identification of the high and low potential flavins of liver microsomal NADPH-cytochrome P-450 reductase. J Biol Chem 253:8812-8819.
    • (1978) J Biol Chem , vol.253 , pp. 8812-8819
    • Vermilion, J.L.1    Coon, M.J.2
  • 35
    • 2442690439 scopus 로고    scopus 로고
    • Validated assays for human cytochrome P450 activities
    • Walsky RL and Obach RS (2004) Validated assays for human cytochrome P450 activities. Drug Metab Dispos 32:647-660.
    • (2004) Drug Metab Dispos , vol.32 , pp. 647-660
    • Walsky, R.L.1    Obach, R.S.2
  • 36
    • 0034093628 scopus 로고    scopus 로고
    • Human cytochrome P-450 3A4: In vitro drug-drug interaction patterns are substrate-dependent
    • Wang RW, Newton DJ, Liu N, Atkins WM, and Lu AY (2000) Human cytochrome P-450 3A4: in vitro drug-drug interaction patterns are substrate-dependent. Drug Metab Dispos 28:360-366.
    • (2000) Drug Metab Dispos , vol.28 , pp. 360-366
    • Wang, R.W.1    Newton, D.J.2    Liu, N.3    Atkins, W.M.4    Lu, A.Y.5
  • 38
    • 0026750647 scopus 로고
    • The human hepatic cytochromes P450 involved in drug metabolism
    • Wrighton SA and Stevens JC (1992) The human hepatic cytochromes P450 involved in drug metabolism. Crit Rev Toxicol 22:1-21.
    • (1992) Crit Rev Toxicol , vol.22 , pp. 1-21
    • Wrighton, S.A.1    Stevens, J.C.2
  • 41
    • 0036447583 scopus 로고    scopus 로고
    • Roles of NADPH-P450 reductase and apo- And holo-cytochrome b5 on xenobiotic oxidations catalyzed by 12 recombinant human cytochrome P450s expressed in membranes of Escherichia coli
    • Yamazaki H, Nakamura M, Komatsu T, Ohyama K, Hatanaka N, Asahi S, Shimada N, Guengerich FP, Shimada T, Nakajima M, et al. (2002) Roles of NADPH-P450 reductase and apo- and holo-cytochrome b5 on xenobiotic oxidations catalyzed by 12 recombinant human cytochrome P450s expressed in membranes of Escherichia coli. Protein Expr Purif 24:329-337.
    • (2002) Protein Expr Purif , vol.24 , pp. 329-337
    • Yamazaki, H.1    Nakamura, M.2    Komatsu, T.3    Ohyama, K.4    Hatanaka, N.5    Asahi, S.6    Shimada, N.7    Guengerich, F.P.8    Shimada, T.9    Nakajima, M.10
  • 42
    • 0029671251 scopus 로고    scopus 로고
    • Roles of cytochrome b5 in the oxidation of testosterone and nifedipine by recombinant cytochrome P450 3A4 and by human liver microsomes
    • Yamazaki H, Nakano M, Imai Y, Ueng YF, Guengerich FP, and Shimada T (1996) Roles of cytochrome b5 in the oxidation of testosterone and nifedipine by recombinant cytochrome P450 3A4 and by human liver microsomes. Arch Biochem Biophys 325:174-182.
    • (1996) Arch Biochem Biophys , vol.325 , pp. 174-182
    • Yamazaki, H.1    Nakano, M.2    Imai, Y.3    Ueng, Y.F.4    Guengerich, F.P.5    Shimada, T.6
  • 43
    • 0036893593 scopus 로고    scopus 로고
    • Evaluation of cytochrome P450 probe substrates commonly used by the pharmaceutical industry to study in vitro drug interactions
    • Yuan R, Madani S, Wei XX, Reynolds K, and Huang SM (2002) Evaluation of cytochrome P450 probe substrates commonly used by the pharmaceutical industry to study in vitro drug interactions. Drug Metab Dispos 30:1311-1319.
    • (2002) Drug Metab Dispos , vol.30 , pp. 1311-1319
    • Yuan, R.1    Madani, S.2    Wei, X.X.3    Reynolds, K.4    Huang, S.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.