메뉴 건너뛰기




Volumn 28, Issue 5, 2013, Pages 411-415

Mechanism-based inhibition profiles of erythromycin and clarithromycin with cytochrome P450 3A4 genetic variants

Author keywords

Clarithromycin; CYP3A4; Erythromycin; Genetic variants; Mechanism based inhibition

Indexed keywords

6BETA HYDROXYTESTOSTERONE; CLARITHROMYCIN; CYTOCHROME P450 3A4; ERYTHROMYCIN; RECOMBINANT CYTOCHROME P450 3A4; RECOMBINANT ENZYME; TESTOSTERONE; TESTOSTERONE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84886403500     PISSN: 13474367     EISSN: 18800920     Source Type: Journal    
DOI: 10.2133/dmpk.DMPK-12-RG-134     Document Type: Article
Times cited : (28)

References (31)
  • 1
    • 0028237729 scopus 로고
    • Interindividual variation in human liver cytochrome P450 enzymes involved in the oxidation of drugs, carcinogens, and toxic chemicals
    • Shimada, T., Yamazaki, H., Mimura, M., Inui, Y. and Guengerich, F. P.: Interindividual variation in human liver cytochrome P450 enzymes involved in the oxidation of drugs, carcinogens, and toxic chemicals. J. Pharmacol. Exp. Ther., 270: 414-423 (1994).
    • (1994) J. Pharmacol. Exp. Ther. , vol.270 , pp. 414-423
    • Shimada, T.1    Yamazaki, H.2    Mimura, M.3    Inui, Y.4    Guengerich, F.P.5
  • 2
    • 0032924934 scopus 로고    scopus 로고
    • Human cytochrome P450 3A4: Regulation and role in drug metabolism
    • Guengerich, F. P.: Human cytochrome P450 3A4: regulation and role in drug metabolism. Annu. Rev. Pharmacol. Toxicol., 39: 1-17 (1999).
    • (1999) Annu. Rev. Pharmacol. Toxicol. , vol.39 , pp. 1-17
    • Guengerich, F.P.1
  • 3
    • 38949094492 scopus 로고    scopus 로고
    • Cytochrome P450 and chemical toxicology
    • Guengerich, F. P.: Cytochrome P450 and chemical toxicology. Chem. Res. Toxicol., 21: 70-83 (2008).
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 70-83
    • Guengerich, F.P.1
  • 4
    • 84886445548 scopus 로고    scopus 로고
    • the Human Cytochrome P450 (CYP) Allele Nomenclature Committee Web Site
    • http://www.cypalleles.ki.se/cyp3a4.htm the Human Cytochrome P450 (CYP) Allele Nomenclature Committee Web Site.
  • 5
    • 54349104898 scopus 로고    scopus 로고
    • Defective activity of recombinant cytochromes P450 3A4.2 and 3A4.16 in oxidation of midazolam, nifedipine, and testosterone
    • Miyazaki, M., Nakamura, K., Fujita, Y., Guengerich, F. P., Horiuchi, R. and Yamamoto, K.: Defective activity of recombinant cytochromes P450 3A4.2 and 3A4.16 in oxidation of midazolam, nifedipine, and testosterone. Drug Metab. Dispos., 36: 2287-2291 (2008).
    • (2008) Drug Metab. Dispos. , vol.36 , pp. 2287-2291
    • Miyazaki, M.1    Nakamura, K.2    Fujita, Y.3    Guengerich, F.P.4    Horiuchi, R.5    Yamamoto, K.6
  • 7
    • 73349103803 scopus 로고    scopus 로고
    • Prediction of drug-drug interactions based on time-dependent inhibition from high throughput screening of cytochrome P450 3A4 inhibition
    • Sekiguchi, N., Higashida, A., Kato, M., Nabuchi, Y., Mitsui, T., Takanashi, K., Aso, Y. and Ishigai, M.: Prediction of drug-drug interactions based on time-dependent inhibition from high throughput screening of cytochrome P450 3A4 inhibition. Drug Metab. Pharmacokinet., 24: 500-510 (2009).
    • (2009) Drug Metab. Pharmacokinet. , vol.24 , pp. 500-510
    • Sekiguchi, N.1    Higashida, A.2    Kato, M.3    Nabuchi, Y.4    Mitsui, T.5    Takanashi, K.6    Aso, Y.7    Ishigai, M.8
  • 8
    • 33644827609 scopus 로고    scopus 로고
    • Quantitative prediction of macrolide drug-drug interaction potential from in vitro studies using testosterone as the human cytochrome P4503A substrate
    • Polasek, T. M. and Miners, J. O.: Quantitative prediction of macrolide drug-drug interaction potential from in vitro studies using testosterone as the human cytochrome P4503A substrate. Eur. J. Clin. Pharmacol., 62: 203-208 (2006).
    • (2006) Eur. J. Clin. Pharmacol. , vol.62 , pp. 203-208
    • Polasek, T.M.1    Miners, J.O.2
  • 9
    • 34548070044 scopus 로고    scopus 로고
    • Computational approaches that predict metabolic intermediate complex formation with CYP3A4 (+b5)
    • Jones, D. R., Ekins, S., Li, L. and Hall, S. D.: Computational approaches that predict metabolic intermediate complex formation with CYP3A4 (+b5). Drug Metab. Dispos., 35: 1466-1475 (2007).
    • (2007) Drug Metab. Dispos. , vol.35 , pp. 1466-1475
    • Jones, D.R.1    Ekins, S.2    Li, L.3    Hall, S.D.4
  • 10
    • 13244299150 scopus 로고    scopus 로고
    • Mechanism-based inactivation of CYP3A by HIV protease inhibitors
    • Ernest, C. S., 2nd, Hall, S. D. and Jones, D. R.: Mechanism-based inactivation of CYP3A by HIV protease inhibitors. J. Pharmacol. Exp. Ther., 312: 583-591 (2005).
    • (2005) J. Pharmacol. Exp. Ther. , vol.312 , pp. 583-591
    • Ernest II, C.S.1    Hall, S.D.2    Jones, D.R.3
  • 12
    • 0019854279 scopus 로고
    • A pharmacokinetic analysis program (multi) for microcomputer
    • Yamaoka, K., Tanigawara, Y., Nakagawa, T. and Uno, T.: A pharmacokinetic analysis program (multi) for microcomputer. J. Pharmacobiodyn., 4: 879-885 (1981).
    • (1981) J. Pharmacobiodyn. , vol.4 , pp. 879-885
    • Yamaoka, K.1    Tanigawara, Y.2    Nakagawa, T.3    Uno, T.4
  • 13
    • 0033632228 scopus 로고    scopus 로고
    • CYP3A4 allelic variants with amino acid substitutions in exons 7 and 12: Evidence for an allelic variant with altered catalytic activity
    • Sata, F., Sapone, A., Elizondo, G., Stocker, P., Miller, V. P., Zheng, W., Raunio, H., Crespi, C. L. and Gonzalez, F. J.: CYP3A4 allelic variants with amino acid substitutions in exons 7 and 12: Evidence for an allelic variant with altered catalytic activity. Clin. Pharmacol. Ther., 67: 48-56 (2000).
    • (2000) Clin. Pharmacol. Ther. , vol.67 , pp. 48-56
    • Sata, F.1    Sapone, A.2    Elizondo, G.3    Stocker, P.4    Miller, V.P.5    Zheng, W.6    Raunio, H.7    Crespi, C.L.8    Gonzalez, F.J.9
  • 18
    • 0036891948 scopus 로고    scopus 로고
    • The influence of nonspecific microsmal binding on apparent intrinsic clearance, and its prediction from physicochemical properties
    • Austin, R. P., Barton, P., Cockroft, S. L., Wenlock, M. C. and Riley, R. J.: The influence of nonspecific microsmal binding on apparent intrinsic clearance, and its prediction from physicochemical properties. Drug Metab. Dispos., 30: 1497-1503 (2002).
    • (2002) Drug Metab. Dispos. , vol.30 , pp. 1497-1503
    • Austin, R.P.1    Barton, P.2    Cockroft, S.L.3    Wenlock, M.C.4    Riley, R.J.5
  • 19
    • 14044251501 scopus 로고    scopus 로고
    • The binding of drugs to hepatocytes and its relationship to physicochemical properties
    • Austin, R. P., Barton, P., Mohmed, S. and Riley, R. J.: The binding of drugs to hepatocytes and its relationship to physicochemical properties. Drug Metab. Dispos., 33: 419-425 (2005).
    • (2005) Drug Metab. Dispos. , vol.33 , pp. 419-425
    • Austin, R.P.1    Barton, P.2    Mohmed, S.3    Riley, R.J.4
  • 20
    • 0026542989 scopus 로고
    • Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences
    • Gotoh, O.: Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences. J. Biol. Chem., 267: 83-90 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 83-90
    • Gotoh, O.1
  • 21
    • 0029781481 scopus 로고    scopus 로고
    • Structural alignments of P450s and extrapolations to the unknown
    • In Graham-Lorence, S. E. and Peterson, J. A. (eds.): New York, Academic Press
    • Johnson, E. F. and Waterman, M. R.: Structural alignments of P450s and extrapolations to the unknown. In Graham-Lorence, S. E. and Peterson, J. A. (eds.): Methods in Enzymology, New York, Academic Press, 1996, pp. 315-327.
    • (1996) Methods in Enzymology , pp. 315-327
    • Johnson, E.F.1    Waterman, M.R.2
  • 22
    • 0033970047 scopus 로고    scopus 로고
    • Mammalian microsomal cytochrome P450 monooxygenase: Structural adaptations for membrane binding and functional diversity
    • Williams, P. A., Cosme, J., Sridhar, V., Johnson, E. F. and McRee, D. E.: Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity. Mol. Cell, 5: 121-131 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 121-131
    • Williams, P.A.1    Cosme, J.2    Sridhar, V.3    Johnson, E.F.4    McRee, D.E.5
  • 23
    • 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, K. K., He, Y. Q., Domanski, T. L. and Halpert, J. R.: 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).
    • (2002) Mol. Pharmacol. , vol.61 , pp. 495-506
    • Khan, K.K.1    He, Y.Q.2    Domanski, T.L.3    Halpert, J.R.4
  • 25
    • 4644301430 scopus 로고    scopus 로고
    • The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05-Å resolution
    • Yano, J. K., Wester, M. R., Schoch, G. A., Griffin, K. J., Stout, C. D. and Johnson, E. F.: The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05-Å resolution. J. Biol. Chem., 279: 38091-38094 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 38091-38094
    • Yano, J.K.1    Wester, M.R.2    Schoch, G.A.3    Griffin, K.J.4    Stout, C.D.5    Johnson, E.F.6
  • 26
    • 84857473710 scopus 로고    scopus 로고
    • Peripheral ligand-binding site in cytochrome P450 3A4 located with fluorescence resonance energy transfer (FRET)
    • Davydov, D. R., Rumfeldt, J. A., Sineva, E. V., Fernando, H., Davydova, N. Y. and Halpert, J. R.: Peripheral ligand-binding site in cytochrome P450 3A4 located with fluorescence resonance energy transfer (FRET). J. Biol. Chem., 287: 6797-6809 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 6797-6809
    • Davydov, D.R.1    Rumfeldt, J.A.2    Sineva, E.V.3    Fernando, H.4    Davydova, N.Y.5    Halpert, J.R.6
  • 27
    • 67649382514 scopus 로고    scopus 로고
    • Application of mechanism-based CYP inhibition for predicting drug-drug interactions
    • Review
    • Zhou, Z. W. and Zhou, S. F.: Application of mechanism-based CYP inhibition for predicting drug-drug interactions. Expert Opin. Drug Metab. Toxicol., 5: 579-605. Review (2009).
    • (2009) Expert Opin. Drug Metab. Toxicol. , vol.5 , pp. 579-605
    • Zhou, Z.W.1    Zhou, S.F.2
  • 28
    • 33750547308 scopus 로고    scopus 로고
    • CYP2C9 inhibition: Impact of probe selection and pharmacogenetics on in vitro inhibition profiles
    • Kumar, V., Wahlstrom, J. L., Rock, D. A., Warren, C. J., Gorman, L. A. and Tracy, T. S.: CYP2C9 inhibition: Impact of probe selection and pharmacogenetics on in vitro inhibition profiles. Drug Metab. Dispos., 34: 1966-1975 (2006).
    • (2006) Drug Metab. Dispos. , vol.34 , pp. 1966-1975
    • Kumar, V.1    Wahlstrom, J.L.2    Rock, D.A.3    Warren, C.J.4    Gorman, L.A.5    Tracy, T.S.6
  • 29
    • 67649392513 scopus 로고    scopus 로고
    • A framework for assessing inter-individual variability in pharmacokinetics using virtual human populations and integrating general knowledge of physical chemistry, biology, anatomy, physiology and genetics: A tale of 'bottom-up' vs 'top-down' recognition of covariates
    • Jamei, M., Dickinson, G. L. and Rostami-Hodjegan, A.: A framework for assessing inter-individual variability in pharmacokinetics using virtual human populations and integrating general knowledge of physical chemistry, biology, anatomy, physiology and genetics: A tale of 'bottom-up' vs 'top-down' recognition of covariates. Drug Metab. Pharmacokinet., 24: 53-75 (2009).
    • (2009) Drug Metab. Pharmacokinet. , vol.24 , pp. 53-75
    • Jamei, M.1    Dickinson, G.L.2    Rostami-Hodjegan, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.