메뉴 건너뛰기




Volumn 25, Issue 2, 1997, Pages 256-266

Selective biotransformation of the human immunodeficiency virus protease inhibitor saquinavir by human small-intestinal cytochrome P4503A4: Potential contribution to high first-pass metabolism

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA NAPHTHOFLAVONE; CHLORZOXAZONE; CYCLOSPORIN A; CYTOCHROME P450 INHIBITOR; CYTOCHROME P450 ISOENZYME; FLUVOXAMINE; FURAFYLLINE; INDINAVIR; KETOCONAZOLE; MEPHENYTOIN; MIDAZOLAM; PROTEINASE INHIBITOR; QUERCETIN; QUINIDINE; SAQUINAVIR; SULFAPHENAZOLE; TERFENADINE; TROLEANDOMYCIN;

EID: 0031024382     PISSN: 00909556     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (226)

References (44)
  • 3
    • 0028843163 scopus 로고
    • Characterization of human immunodeficiency virus type 1 mutants with decreased sensitivity to proteinase inhibitor Ro 31-8959
    • H. Jacobsen, K. Yasargil, D. L. Winslow, C. Craig, A. Kröhn, I. B. Duncan, and J. Mous: Characterization of human immunodeficiency virus type 1 mutants with decreased sensitivity to proteinase inhibitor Ro 31-8959. Virology 206, 527-534 (1995).
    • (1995) Virology , vol.206 , pp. 527-534
    • Jacobsen, H.1    Yasargil, K.2    Winslow, D.L.3    Craig, C.4    Kröhn, A.5    Duncan, I.B.6    Mous, J.7
  • 4
    • 0030028130 scopus 로고    scopus 로고
    • Identification of bilirubin UDP-GTs in the human alimentary tract in accordance with the gut as a putative metabolic organ
    • M. W. McDonnell, E. Hitomi, and F. K. Askari: Identification of bilirubin UDP-GTs in the human alimentary tract in accordance with the gut as a putative metabolic organ. Biochem. Pharmacol. 51, 483-488 (1996).
    • (1996) Biochem. Pharmacol. , vol.51 , pp. 483-488
    • McDonnell, M.W.1    Hitomi, E.2    Askari, F.K.3
  • 6
    • 0027501606 scopus 로고
    • (+) and (-) Terbutaline are sulphated at a higher rate in human intestine than in liver
    • G. M. Pacifici, M. Eligi, and L. Giuliani: (+) and (-) Terbutaline are sulphated at a higher rate in human intestine than in liver. Eur. J. Clin. Pharmacol. 45, 483-487 (1993).
    • (1993) Eur. J. Clin. Pharmacol. , vol.45 , pp. 483-487
    • Pacifici, G.M.1    Eligi, M.2    Giuliani, L.3
  • 8
    • 0029998275 scopus 로고    scopus 로고
    • Comparative studies of drug-metabolizing enzymes in dog, monkey, and human small intestines, and in CACO-2 cells
    • T. Prueksaritanont, L. M. Gorham, J. H. Hochman, L. O. Tran, and K. P. Vyas: Comparative studies of drug-metabolizing enzymes in dog, monkey, and human small intestines, and in CACO-2 cells. Drug Metab. Dispos. 24, 634-642 (1996).
    • (1996) Drug Metab. Dispos. , vol.24 , pp. 634-642
    • Prueksaritanont, T.1    Gorham, L.M.2    Hochman, J.H.3    Tran, L.O.4    Vyas, K.P.5
  • 9
    • 0024604149 scopus 로고
    • Cytochrome P450 in the intestinal mucosa of man
    • W. H. M. Peters and P. G. Kremers: Cytochrome P450 in the intestinal mucosa of man. Biochem. Pharmacol. 38, 1535-1538 (1989).
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 1535-1538
    • Peters, W.H.M.1    Kremers, P.G.2
  • 10
    • 0028820208 scopus 로고
    • Differentiation of absorption and first-pass gut and hepatic metabolism in humans: Studies with cyclosporine
    • C. Y. Wu, L. Z. Benet, M. F. Hebert, S. K. Gupta, M. Rowland, D. Y. Gomez, and V. J. Wacher: Differentiation of absorption and first-pass gut and hepatic metabolism in humans: studies with cyclosporine. Clin. Pharmacol. Ther. 58, 492-497 (1995).
    • (1995) Clin. Pharmacol. Ther. , vol.58 , pp. 492-497
    • Wu, C.Y.1    Benet, L.Z.2    Hebert, M.F.3    Gupta, S.K.4    Rowland, M.5    Gomez, D.Y.6    Wacher, V.J.7
  • 11
    • 0026659150 scopus 로고
    • Cyclosporin metabolism by human gastrointestinal mucosal microsomes
    • I. R. Webber, W. H. M. Peters, and D. J. Back: Cyclosporin metabolism by human gastrointestinal mucosal microsomes. Br. J. Clin. Pharmacol. 33, 661-664 (1992).
    • (1992) Br. J. Clin. Pharmacol. , vol.33 , pp. 661-664
    • Webber, I.R.1    Peters, W.H.M.2    Back, D.J.3
  • 12
    • 0025719746 scopus 로고
    • First pass metabolism of cyclosporin by the gut
    • J. C. Kolars, W. M. Awni, R. Merion, and P. B. Watkins: First pass metabolism of cyclosporin by the gut. Lancet 338, 1488-1490 (1991).
    • (1991) Lancet , vol.338 , pp. 1488-1490
    • Kolars, J.C.1    Awni, W.M.2    Merion, R.3    Watkins, P.B.4
  • 14
    • 0030068752 scopus 로고    scopus 로고
    • Rifampin drastically reduces plasma concentrations and effects of oral midazolam
    • J. T. Backman, K. T. Olkkola, and P. J. Neuvonen: Rifampin drastically reduces plasma concentrations and effects of oral midazolam. Clin. Pharmacol. Ther. 59, 7-13 (1996).
    • (1996) Clin. Pharmacol. Ther. , vol.59 , pp. 7-13
    • Backman, J.T.1    Olkkola, K.T.2    Neuvonen, P.J.3
  • 15
    • 0029123393 scopus 로고
    • The effects of ketoconazole on the intestinal metabolism and bioavailability of cyclosporine
    • D. Y. Gomez, V. J. Wacher, S. J. Tomlanovich, M. F. Hebert, and L. Z. Benet: The effects of ketoconazole on the intestinal metabolism and bioavailability of cyclosporine. Clin. Pharmacol. Ther. 58, 15-19 (1995).
    • (1995) Clin. Pharmacol. Ther. , vol.58 , pp. 15-19
    • Gomez, D.Y.1    Wacher, V.J.2    Tomlanovich, S.J.3    Hebert, M.F.4    Benet, L.Z.5
  • 16
    • 0026457407 scopus 로고
    • Bioavailability of cyclosporin with concomitant rifampin administration is markedly less than predicted by hepatic enzyme induction
    • M. F. Herbert, J. P. Roberts, T. Prueksaritanont, and L. Z. Benet: Bioavailability of cyclosporin with concomitant rifampin administration is markedly less than predicted by hepatic enzyme induction. Clin. Pharmacol. Ther. 52, 453-457 (1992).
    • (1992) Clin. Pharmacol. Ther. , vol.52 , pp. 453-457
    • Herbert, M.F.1    Roberts, J.P.2    Prueksaritanont, T.3    Benet, L.Z.4
  • 17
    • 0027957132 scopus 로고
    • Metabolism of taxol by human hepatic microsomes and liver slices: Participation of cytochrome P450 3A4 and an unknown P450 enzyme
    • J. W. Harris, A. Rahman, B. R. Kim, F. P. Guengerich, and J. M. Collins: Metabolism of taxol by human hepatic microsomes and liver slices: participation of cytochrome P450 3A4 and an unknown P450 enzyme. Cancer Res. 54, 4026-4035 (1994).
    • (1994) Cancer Res. , vol.54 , pp. 4026-4035
    • Harris, J.W.1    Rahman, A.2    Kim, B.R.3    Guengerich, F.P.4    Collins, J.M.5
  • 19
    • 0027168405 scopus 로고
    • Oxidation of the antihistaminic drug terfenadine in human liver microsomes
    • C. Yun, R. A. Okerholm, and F. P. Guengerich: Oxidation of the antihistaminic drug terfenadine in human liver microsomes. Drug Metab. Dispos. 21, 403-409 (1990).
    • (1990) Drug Metab. Dispos. , vol.21 , pp. 403-409
    • Yun, C.1    Okerholm, R.A.2    Guengerich, F.P.3
  • 20
    • 0027996327 scopus 로고
    • Terfenadine metabolism in human liver: In vitro inhibition by macrolide antibiotics and azole antifungals
    • M. Jurima-Romet, K. Crawford, T. Cyr, and T. Inaba: Terfenadine metabolism in human liver: in vitro inhibition by macrolide antibiotics and azole antifungals. Drug Metab. Dispos. 22, 849-857 (1994).
    • (1994) Drug Metab. Dispos. , vol.22 , pp. 849-857
    • Jurima-Romet, M.1    Crawford, K.2    Cyr, T.3    Inaba, T.4
  • 22
    • 0028307539 scopus 로고
    • Activation of CYP3A4: Evidence for the simultaneous binding of two substrates in a cytochrome P450 active site
    • M. Shou, J. Grogan, J. A. Mancewicz, K. W. Krausz, F. J. Gonzalez, H. V. Gelboin, and K. R. Korzekwa: Activation of CYP3A4: evidence for the simultaneous binding of two substrates in a cytochrome P450 active site. Biochemistry 33, 6450-6455 (1994).
    • (1994) Biochemistry , vol.33 , pp. 6450-6455
    • Shou, M.1    Grogan, J.2    Mancewicz, J.A.3    Krausz, K.W.4    Gonzalez, F.J.5    Gelboin, H.V.6    Korzekwa, K.R.7
  • 23
    • 0026459382 scopus 로고
    • Speculations on the substrate structure-activity relationship (SSAR) of cytochrome P450 enzymes
    • D. A. Smith and B. C. Jones: Speculations on the substrate structure-activity relationship (SSAR) of cytochrome P450 enzymes. Biochem. Pharmacol. 44, 2089-2098 (1992).
    • (1992) Biochem. Pharmacol. , vol.44 , pp. 2089-2098
    • Smith, D.A.1    Jones, B.C.2
  • 24
    • 0023949862 scopus 로고
    • Modulation of rabbit and human hepatic cytochrome P-450-catalyzed steroid hydroxylations by α-naphthoflavone
    • G. E. Schwab, L. L. Raucy, and E. F. Johnson: Modulation of rabbit and human hepatic cytochrome P-450-catalyzed steroid hydroxylations by α-naphthoflavone. Mol. Pharmacol. 33, 493-499 (1988).
    • (1988) Mol. Pharmacol. , vol.33 , pp. 493-499
    • Schwab, G.E.1    Raucy, L.L.2    Johnson, E.F.3
  • 25
    • 0015055235 scopus 로고
    • Aryl hydrocarbon (benzo(a)pyrene)hydroxylase in microsomes from rat tissues: Differential inhibition and stimulation by benzoflavones and organic solvents
    • F. J. Wiebel, L. C. Leutz, L. Diamond, and H. V. Gelboin: Aryl hydrocarbon (benzo(a)pyrene)hydroxylase in microsomes from rat tissues: differential inhibition and stimulation by benzoflavones and organic solvents. Arch. Biochem. Biophys. 144, 78-86 (1971).
    • (1971) Arch. Biochem. Biophys. , vol.144 , pp. 78-86
    • Wiebel, F.J.1    Leutz, L.C.2    Diamond, L.3    Gelboin, H.V.4
  • 27
    • 0028362263 scopus 로고
    • Characterization of the inhibition of P4501A2 by furafylline
    • S. E. Clarke, A. D. Ayrton, and R. J. Chenery: Characterization of the inhibition of P4501A2 by furafylline. Xenobiotica 24, 517-526 (1994).
    • (1994) Xenobiotica , vol.24 , pp. 517-526
    • Clarke, S.E.1    Ayrton, A.D.2    Chenery, R.J.3
  • 28
    • 0027380074 scopus 로고
    • Isoform-selective mechanism-based inhibition of human cytochrome P450 1A2 by furafylline
    • K. L. Kunze and W. F. Trager: Isoform-selective mechanism-based inhibition of human cytochrome P450 1A2 by furafylline. Chem. Res. Toxicol. 6, 649-656 (1993).
    • (1993) Chem. Res. Toxicol. , vol.6 , pp. 649-656
    • Kunze, K.L.1    Trager, W.F.2
  • 30
    • 0023873591 scopus 로고
    • Tolbutamide hydroxylation by human liver microsomes: Kinetic characterization and relationship to other cytochrome P-450 dependent xenobiotic oxidations
    • J. O. Miners, K. J. Smith, R. A. Robson, M. E. McManus, M. E. Veronese, and D. J. Birkett: Tolbutamide hydroxylation by human liver microsomes: kinetic characterization and relationship to other cytochrome P-450 dependent xenobiotic oxidations. Biochem. Pharmacol. 37, 1137-1144 (1988).
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 1137-1144
    • Miners, J.O.1    Smith, K.J.2    Robson, R.A.3    McManus, M.E.4    Veronese, M.E.5    Birkett, D.J.6
  • 31
    • 0027445449 scopus 로고
    • Isolation and characterization of human liver cytochrome P450 2C19: Correlation between 2C19 and S-mephenytoin 4′-hydroxylation
    • S. A. Wrighton, J. C. Stevens, G. W. Becker, and M. Vandenbranden: Isolation and characterization of human liver cytochrome P450 2C19: correlation between 2C19 and S-mephenytoin 4′-hydroxylation. Arch. Biochem. Biophys. 306, 240-245 (1993).
    • (1993) Arch. Biochem. Biophys. , vol.306 , pp. 240-245
    • Wrighton, S.A.1    Stevens, J.C.2    Becker, G.W.3    Vandenbranden, M.4
  • 32
    • 0025733250 scopus 로고
    • Role of P450IID6, the target of the sparteine-debrisoquin oxidation polymorphism, in the metabolism of imipramine
    • K. Brosen, T. Zeugin, and U. A. Meyer: Role of P450IID6, the target of the sparteine-debrisoquin oxidation polymorphism, in the metabolism of imipramine. Clin. Pharmacol. Ther. 49, 609-617 (1991).
    • (1991) Clin. Pharmacol. Ther. , vol.49 , pp. 609-617
    • Brosen, K.1    Zeugin, T.2    Meyer, U.A.3
  • 33
    • 0022390883 scopus 로고
    • In vitro inhibition studies of two isozymes of human liver cytochrome P450: Mephenytoin p-hydroxylase and sparteine monooxygenase
    • T. Inaba, M. Jurima, W. A. Mahon, and W. Kalow: In vitro inhibition studies of two isozymes of human liver cytochrome P450: mephenytoin p-hydroxylase and sparteine monooxygenase. Drug Metab. Dispos. 13, 443-448 (1985).
    • (1985) Drug Metab. Dispos. , vol.13 , pp. 443-448
    • Inaba, T.1    Jurima, M.2    Mahon, W.A.3    Kalow, W.4
  • 35
    • 0028858960 scopus 로고
    • Cytochrome P450 inhibitors: Evaluation of specificities in the in vitro metabolism of therapeutic agents by human liver microsomes
    • D. J. Newton, R. W. Wang, and A. Y. H. Lu: Cytochrome P450 inhibitors: evaluation of specificities in the in vitro metabolism of therapeutic agents by human liver microsomes. Drug Metab. Dispos. 23, 154-158 (1995).
    • (1995) Drug Metab. Dispos. , vol.23 , pp. 154-158
    • Newton, D.J.1    Wang, R.W.2    Lu, A.Y.H.3
  • 36
    • 0022467917 scopus 로고
    • Oxidation of quinidine by human liver cytochrome P-450
    • F. P. Guengerich, D. Muller-Enoch, and I. A. Blair: Oxidation of quinidine by human liver cytochrome P-450. Mol. Pharmacol. 30, 287-295 (1986).
    • (1986) Mol. Pharmacol. , vol.30 , pp. 287-295
    • Guengerich, F.P.1    Muller-Enoch, D.2    Blair, I.A.3
  • 38
    • 0024343858 scopus 로고
    • PA (P-450IA2), the phenacetin O-deethylase, is primarily responsible for the hepatic 3-demethylation of caffeine and N-oxidation of carcinogenic arylamines
    • PA (P-450IA2), the phenacetin O-deethylase, is primarily responsible for the hepatic 3-demethylation of caffeine and N-oxidation of carcinogenic arylamines. Proc. Natl. Acad. Sci. U.S.A. 86, 7696-7700 (1989).
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 7696-7700
    • Butler, M.A.1    Iwasaki, M.2    Guengerich, F.P.3    Kadlubar, F.F.4
  • 39
    • 0030058076 scopus 로고    scopus 로고
    • Metabolic interactions of putative cytochrome P4503A substrates with alternative pathways of dapsone metabolism in human liver microsomes
    • Y. Irshaid, R. A. Branch, and A. Adedoyin: Metabolic interactions of putative cytochrome P4503A substrates with alternative pathways of dapsone metabolism in human liver microsomes. Drug Metab. Dispos. 24, 164-171 (1996).
    • (1996) Drug Metab. Dispos. , vol.24 , pp. 164-171
    • Irshaid, Y.1    Branch, R.A.2    Adedoyin, A.3
  • 40
    • 0029872126 scopus 로고    scopus 로고
    • Role of cytochrome P450 3A4 in human metabolism of MK-639, a potent human immunodeficiency virus protease inhibitor
    • M. Chiba, M. Hensleigh, J. A. Nishime, S. K. Balani, and J. H. Lin: Role of cytochrome P450 3A4 in human metabolism of MK-639, a potent human immunodeficiency virus protease inhibitor. Drug Metab. Dispos. 24, 307-314 (1996).
    • (1996) Drug Metab. Dispos. , vol.24 , pp. 307-314
    • Chiba, M.1    Hensleigh, M.2    Nishime, J.A.3    Balani, S.K.4    Lin, J.H.5
  • 42
    • 0027267566 scopus 로고
    • Itraconazole prevents terfenadine metabolism and increases risk of torsades de pointes ventricular tachycardia
    • S. Pohjola-Sintonen, M. Viitasalo, L. Toivonen, and P. Neuvonen: Itraconazole prevents terfenadine metabolism and increases risk of torsades de pointes ventricular tachycardia. Eur. J. Clin. Pharmacol. 45, 191-193 (1993).
    • (1993) Eur. J. Clin. Pharmacol. , vol.45 , pp. 191-193
    • Pohjola-Sintonen, S.1    Viitasalo, M.2    Toivonen, L.3    Neuvonen, P.4
  • 43
    • 0027231225 scopus 로고
    • The effect of fluconazole on the steady-state pharmacokinetics and electrocardiographic pharmacodynamics of terfenadine in humans
    • P. K. Honig, D. C. Worham, K. Zamani, J. C. Mullin, D. P. Conner, and L. R. Cantilena: The effect of fluconazole on the steady-state pharmacokinetics and electrocardiographic pharmacodynamics of terfenadine in humans. Clin. Pharmacol. Ther. 53, 630-636 (1993).
    • (1993) Clin. Pharmacol. Ther. , vol.53 , pp. 630-636
    • Honig, P.K.1    Worham, D.C.2    Zamani, K.3    Mullin, J.C.4    Conner, D.P.5    Cantilena, L.R.6
  • 44
    • 0026671408 scopus 로고
    • Changes in the pharmacokinetics and electrocardiographic pharmacodynamics of terfenadine with concomitant administration of erythromycin
    • P. K. Honig, R. L. Woosley, K. Zamani, D. P. Conner, and L. R. Cantilena: Changes in the pharmacokinetics and electrocardiographic pharmacodynamics of terfenadine with concomitant administration of erythromycin. Clin. Pharmacol. Ther. 52, 231-238 (1992).
    • (1992) Clin. Pharmacol. Ther. , vol.52 , pp. 231-238
    • Honig, P.K.1    Woosley, R.L.2    Zamani, K.3    Conner, D.P.4    Cantilena, L.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.