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Experimental approaches to evaluate activities of cytochromes P450 3A Cover

Experimental approaches to evaluate activities of cytochromes P450 3A

Open Access
|Nov 2010

References

  1. Andries, M. J., G. W. Lucier, J. Goldstein, and C. L. Thompson. (1990) Involvement of cytochrome P-450c in alpha-naphthoflavone metabolism by rat liver microsomes. Mol Pharmacol 37: 990-5.
  2. Aoyama, T., S. Yamano, D. J. Waxman, D. P. Lapenson, U. A. Meyer, V. Fischer, R. Tyndale, T. Inaba, W. Kalow, H. V. Gelboin, and et al. (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: 10388-95.10.1016/S0021-9258(18)81632-5
  3. Atkins, W. M. (2005) Non-Michaelis-Menten kinetics in cytochrome P450-catalyzed reactions. Annu Rev Pharmacol Toxicol 45: 291-310.10.1146/annurev.pharmtox.45.120403.100004
  4. Atkins, W. M., R. W. Wang, and A. Y. Lu. (2001) Allosteric behavior in cytochrome p450-dependent in vitro drug-drug interactions: a prospective based on conformational dynamics. Chem Res Toxicol 14: 338-47.10.1021/tx0002132
  5. Beaune, P. H., D. R. Umbenhauer, R. W. Bork, R. S. Lloyd, and F. P. Guengerich. (1986) Isolation and sequence determination of a cDNA clone related to human cytochrome P-450 nifedipine oxidase. Proc Natl Acad Sci U S A 83: 8064-8.10.1073/pnas.83.21.8064
  6. Burke, M. D., S. Thompson, C. R. Elcombe, J. Halpert, T. Haaparanta, and R. T. Mayer. (1985) Ethoxy-, pentoxy- and benzyloxyphenoxazones and homologues: a series of substrates to distinguish between different induced cytochromes P-450. Biochem Pharmacol 34: 3337-45.10.1016/0006-2952(85)90355-7
  7. Domanski, T. L., J. Liu, G. R. Harlow, and J. R. Halpert. (1998) Analysis of four residues within substrate recognition site 4 of human cytochrome P450 3A4: role in steroid hydroxylase activity and alpha-naphthoflavone stimulation. Arch Biochem Biophys 350: 223-32.10.1006/abbi.1997.0525
  8. Ekins, S., D. M. Stresser, and J. A. Williams. (2003) In vitro and pharmacophore insights into CYP3A enzymes. Trends Pharmacol Sci 24: 161-6.10.1016/S0165-6147(03)00049-X
  9. Galetin, A., S. E. Clarke, and J. B. Houston. (2002) Quinidine and haloperidol as modifiers of CYP3A4 activity: multisite kinetic model approach. Drug Metab Dispos 30: 1512-22.10.1124/dmd.30.12.151212433827
  10. Gonzalez, F. J., and H. V. Gelboin. (1992) Human cytochromes P450: evolution and cDNA-directed expression. Environ Health Perspect 98: 81-5.10.1289/ehp.92988115196181486867
  11. Guengerich, F. P. (1999) Cytochrome P-450 3A4: regulation and role in drug metabolism. Annu Rev Pharmacol Toxicol 39: 1-17.10.1146/annurev.pharmtox.39.1.110331074
  12. Guryev, O. L., A. A. Gilep, S. A. Usanov, and R. W. Estabrook. (2001) Interaction of apo-cytochrome b5 with cytochromes P4503A4 and P45017A: relevance of heme transfer reactions. Biochemistry 40: 5018-31.10.1021/bi002305w
  13. Harlow, G. R., and J. R. Halpert. (1998) Analysis of human cytochrome P450 3A4 cooperativity: construction and characterization of a site-directed mutant that displays hyperbolic steroid hydroxylation kinetics. Proc Natl Acad Sci U S A 95: 6636-41.10.1073/pnas.95.12.6636
  14. Haugen, D. A., and M. J. Coon. (1976) Properties of electrophoretically homogeneous phenobarbital-inducible and beta-naphthoflavone-inducible forms of liver microsomal cytochrome P-450. J Biol Chem 251: 7929-39.10.1016/S0021-9258(19)57022-3
  15. Hosea, N. A., G. P. Miller, and F. P. Guengerich. (2000) Elucidation of distinct ligand binding sites for cytochrome P450 3A4. Biochemistry 39: 5929-39.10.1021/bi992765t
  16. Isin, E. M., and F. P. Guengerich. (2006) Kinetics and thermodynamics of ligand binding by cytochrome P450 3A4. J Biol Chem 281: 9127-36.10.1074/jbc.M511375200
  17. Kitada, M., T. Kamataki, K. Itahashi, T. Rikihisa, R. Kato, and Y. Kanakubo. (1985) Purification and properties of cytochrome P-450 from homogenates of human fetal livers. Arch Biochem Biophys 241: 275-80.10.1016/0003-9861(85)90383-2
  18. Koley, A. P., J. T. Buters, R. C. Robinson, A. Markowitz, and F. K. Friedman. (1997) Differential mechanisms of cytochrome P450 inhibition and activation by alpha-naphthoflavone. J Biol Chem 272: 3149-52.10.1074/jbc.272.6.3149
  19. Kumar, S., D. R. Davydov, and J. R. Halpert. (2005) Role of cytochrome B5 in modulating peroxide-supported cyp3a4 activity: evidence for a conformational transition and cytochrome P450 heterogeneity. Drug Metab Dispos 33: 1131-6.10.1124/dmd.105.004606
  20. Omura, T., and R. Sato. (1964) The Carbon Monoxide-Binding Pigment of Liver Microsomes. II. Solubilization, Purification, and Properties. J Biol Chem 239: 2379-85.
  21. Ortiz de Montellano, P. R. (1995) The 1994 Bernard B. Brodie Award Lecture. Structure, mechanism, and inhibition of cytochrome P450. Drug Metab Dispos 23: 1181-7.
  22. Patki, K. C., L. L. Von Moltke, and D. J. Greenblatt. (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: 938-44.10.1124/dmd.31.7.938
  23. Reed, J. R., and P. F. Hollenberg. (2003a) Comparison of substrate metabolism by cytochromes P450 2B1, 2B4, and 2B6: relationship of heme spin state, catalysis, and the effects of cytochrome b5. J Inorg Biochem 93: 152-60.10.1016/S0162-0134(02)00597-4
  24. Reed, J. R., and P. F. Hollenberg. (2003b) Examining the mechanism of stimulation of cytochrome P450 by cytochrome b5: the effect of cytochrome b5 on the interaction between cytochrome P450 2B4 and P450 reductase. J Inorg Biochem 97: 265-75.10.1016/S0162-0134(03)00275-7
  25. Shimada, T., and H. Yamazaki. (1998) Cytochrome P450 reconstitution systems. Methods Mol Biol 107: 85-93.10.1385/0-89603-519-0:85
  26. Shimada, T., H. Yamazaki, M. Mimura, Y. Inui, and F. P. Guengerich. (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: 414-23.
  27. Shou, M., J. Grogan, J. A. Mancewicz, K. W. Krausz, F. J. Gonzalez, H. V. Gelboin, and K. R. Korzekwa. (1994) Activation of CYP3A4: evidence for the simultaneous binding of two substrates in a cytochrome P450 active site. Biochemistry 33: 6450-5.10.1021/bi00187a009
  28. Schenkman, J. B., and I. Jansson. (1999) Interactions between cytochrome P450 and cytochrome b5. Drug Metab Rev 31: 351-64.10.1081/DMR-100101923
  29. Stiborova, M., B. Asfaw, E. Frei, H. H. Schmeiser, and M. Wiessler. (1995) Benzenediazonium ion derived from Sudan I forms an 8-(phenylazo) guanine adduct in DNA. Chem Res Toxicol 8: 489-98.10.1021/tx00046a002
  30. Stiborova, M., E. Frei, H. H. Schmeiser, M. Wiessler, and J. Hradec. (1990) Mechanism of formation and 32P-postlabeling of DNA adducts derived from peroxidative activation of carcinogenic non-aminoazo dye 1-phenylazo- 2-hydroxynaphthalene (Sudan I). Carcinogenesis 11: 1843-8.10.1093/carcin/11.10.1843
  31. Tang, W., and R. A. Stearns. (2001) Heterotropic cooperativity of cytochrome P450 3A4 and potential drug-drug interactions. Curr Drug Metab 2: 185-98.10.2174/1389200013338658
  32. Thakker, D. R., W. Levin, M. Buening, H. Yagi, R. E. Lehr, A. W. Wood, A. H. Conney, and D. M. Jerina. (1981) Species-specific enhancement by 7,8-benzoflavone of hepatic microsomal metabolism of benzo[e]pyrene 9,10-dihydrodiol to bay-region diol epoxides. Cancer Res 41: 1389-96.
  33. Tsalkova, T. N., N. Y. Davydova, J. R. Halpert, and D. R. Davydov. (2007) Mechanism of interactions of alpha-naphthoflavone with cytochrome P450 3A4 explored with an engineered enzyme bearing a fluorescent probe. Biochemistry 46: 106-19.10.1021/bi061944p
  34. Ueng, Y. F., T. Kuwabara, Y. J. Chun, and F. P. Guengerich. (1997) Cooperativity in oxidations catalyzed by cytochrome P450 3A4. Biochemistry 36: 370-81.10.1021/bi962359z
  35. Wiechelman, K. J., R. D. Braun, and J. D. Fitzpatrick. (1988) Investigation of the bicinchoninic acid protein assay: identification of the groups responsible for color formation. Anal Biochem 175: 231-7.10.1016/0003-2697(88)90383-1
  36. Yamada, M., Y. Ohta, G. I. Bachmanova, Y. Nishimoto, A. I. Archakov, and S. Kawato. (1995) Dynamic interactions of rabbit liver cytochromes P450IA2 and P450IIB4 with cytochrome b5 and NADPH-cytochrome P450 reductase in proteoliposomes. Biochemistry 34: 10113-9.10.1021/bi00032a0037640265
  37. Yamaori, S., H. Yamazaki, A. Suzuki, A. Yamada, H. Tani, T. Kamidate, K. Fujita, and T. Kamataki. (2003) Effects of cytochrome b(5) on drug oxidation activities of human cytochrome P450 (CYP) 3As: similarity of CYP3A5 with CYP3A4 but not CYP3A7. Biochem Pharmacol 66: 2333-40.10.1016/j.bcp.2003.08.00414637191
  38. Yamazaki, H., W. W. Johnson, Y. F. Ueng, T. Shimada, and F. P. Guengerich. (1996) Lack of electron transfer from cytochrome b5 in stimulation of catalytic activities of cytochrome P450 3A4. Characterization of a reconstituted cytochrome P450 3A4/NADPH-cytochrome P450 reductase system and studies with apo-cytochrome b5. J Biol Chem 271: 27438-44.10.1074/jbc.271.44.274388910324
  39. Yamazaki, H., M. Nakajima, M. Nakamura, S. Asahi, N. Shimada, E. M. Gillam, F. P. Guengerich, T. Shimada, and T. Yokoi. (1999) Enhancement of cytochrome P-450 3A4 catalytic activities by cytochrome b(5) in bacterial membranes. Drug Metab Dispos 27: 999-1004.
  40. Yamazaki, H., T. Shimada, M. V. Martin, and F. P. Guengerich. (2001) Stimulation of cytochrome P450 reactions by apo-cytochrome b5: evidence against transfer of heme from cytochrome P450 3A4 to apo-cytochrome b5 or heme oxygenase. J Biol Chem 276: 30885-91.10.1074/jbc.M10501120011413149
  41. Yang, C. S., Y. Y. Tu, D. R. Koop, and M. J. Coon. (1985) Metabolism of nitrosamines by purified rabbit liver cytochrome P-450 isozymes. Cancer Res 45: 1140-5.
  42. Yasukochi, Y., J. A. Peterson, and B. S. Masters. (1979) NADPH-cytochrome c (P-450) reductase. Spectrophotometric and stopped flow kinetic studies on the formation of reduced flavoprotein intermediates. J Biol Chem 254: 7097-104.
DOI: https://doi.org/10.2478/v10102-010-0032-0 | Journal eISSN: 1337-9569 | Journal ISSN: 1337-6853
Language: English
Page range: 155 - 159
Published on: Nov 1, 2010
Published by: Slovak Academy of Sciences, Institute of Experimental Pharmacology & Toxicology, Centre of Experimental Medicine
In partnership with: Paradigm Publishing Services
Publication frequency: 4 issues per year

© 2010 Lucie Bořek-Dohalská, Petr Hodek, Jiří Hudeček, Marie Stiborová, published by Slovak Academy of Sciences, Institute of Experimental Pharmacology & Toxicology, Centre of Experimental Medicine
This work is licensed under the Creative Commons License.

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