메뉴 건너뛰기




Volumn 38, Issue 1, 2010, Pages 32-39

Comparison of the drug-drug interactions potential of erlotinib and gefitinib via inhibition of UDP-glucuronosyltransferases

Author keywords

[No Author keywords available]

Indexed keywords

4 METHYL UMBELLIFERONE GLUCURONIDE; BILIRUBIN GLUCURONIDE; ERLOTINIB; GEFITINIB; GLUCURONIDE; GLUCURONOSYLTRANSFERASE; GLUCURONOSYLTRANSFERASE 1A1; GLUCURONOSYLTRANSFERASE 1A7; GLUCURONOSYLTRANSFERASE 1A9; GLUCURONOSYLTRANSFERASE 2B7; IMIPRAMINE N GLUCURONIDE; ISOENZYME; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

EID: 73149090339     PISSN: 00909556     EISSN: 1521009X     Source Type: Journal    
DOI: 10.1124/dmd.109.029660     Document Type: Article
Times cited : (98)

References (39)
  • 4
    • 38849197491 scopus 로고    scopus 로고
    • The UDP-glucuronosyltransferases as oligomeric enzymes
    • Finel M and Kurkela M (2008) The UDP-glucuronosyltransferases as oligomeric enzymes. Curr Drug Metab 9:70-76.
    • (2008) Curr Drug Metab , vol.9 , pp. 70-76
    • Finel, M.1    Kurkela, M.2
  • 5
    • 32944469063 scopus 로고    scopus 로고
    • Evaluation of the absolute oral bioavailability and bioequivalence of erlotinib, an inhibitor of the epidermal growth factor receptor tyrosine kinase, in a randomized, crossover study in healthy subjects
    • Frohna P, Lu J, Eppler S, Hamilton M, Wolf J, Rakhit A, Ling J, Kenkare-Mitra SR, and Lum BL (2006) Evaluation of the absolute oral bioavailability and bioequivalence of erlotinib, an inhibitor of the epidermal growth factor receptor tyrosine kinase, in a randomized, crossover study in healthy subjects. J Clin Pharmacol 46:282-290.
    • (2006) J Clin Pharmacol , vol.46 , pp. 282-290
    • Frohna, P.1    Lu, J.2    Eppler, S.3    Hamilton, M.4    Wolf, J.5    Rakhit, A.6    Ling, J.7    Kenkare-Mitra, S.R.8    Lum, B.L.9
  • 6
    • 34548009373 scopus 로고    scopus 로고
    • Significant drug interaction: Phenytoin toxicity due to erlotinib
    • Grenader T, Gipps M, Shavit L, and Gabizon A (2007) Significant drug interaction: phenytoin toxicity due to erlotinib. Lung Cancer 57:404-406.
    • (2007) Lung Cancer , vol.57 , pp. 404-406
    • Grenader, T.1    Gipps, M.2    Shavit, L.3    Gabizon, A.4
  • 8
    • 1942455361 scopus 로고    scopus 로고
    • Database analyses for the prediction of in vivo drug-drug interactions from in vitro data
    • Ito K, Brown HS, and Houston JB (2004) Database analyses for the prediction of in vivo drug-drug interactions from in vitro data. Br J Clin Pharmacol 57:473-486.
    • (2004) Br J Clin Pharmacol , vol.57 , pp. 473-486
    • Ito, K.1    Brown, H.S.2    Houston, J.B.3
  • 9
    • 54449085941 scopus 로고    scopus 로고
    • Pediatric phase I and pharmacokinetic study of erlotinib followed by the combination of erlotinib and temozolomide: A Children's Oncology Group Phase I Consortium Study
    • Jakacki RI, Hamilton M, Gilbertson RJ, Blaney SM, Tersak J, Krailo MD, Ingle AM, Voss SD, Dancey JE, and Adamson PC (2008) Pediatric phase I and pharmacokinetic study of erlotinib followed by the combination of erlotinib and temozolomide: a Children's Oncology Group Phase I Consortium Study. J Clin Oncol 26:4921-4927.
    • (2008) J Clin Oncol , vol.26 , pp. 4921-4927
    • Jakacki, R.I.1    Hamilton, M.2    Gilbertson, R.J.3    Blaney, S.M.4    Tersak, J.5    Krailo, M.D.6    Ingle, A.M.7    Voss, S.D.8    Dancey, J.E.9    Adamson, P.C.10
  • 10
    • 0025996996 scopus 로고
    • Intracellular roles of SN-38, a metabolite of the camptothecin derivative CPT-11, in the antitumor effect of CPT-11
    • Kawato Y, Aonuma M, Hirota Y, Kuga H, and Sato K (1991) Intracellular roles of SN-38, a metabolite of the camptothecin derivative CPT-11, in the antitumor effect of CPT-11. Cancer Res 51:4187-4191.
    • (1991) Cancer Res , vol.51 , pp. 4187-4191
    • Kawato, Y.1    Aonuma, M.2    Hirota, Y.3    Kuga, H.4    Sato, K.5
  • 11
    • 15244342411 scopus 로고    scopus 로고
    • UDP-glucuronosyltransferases and clinical drug-drug interactions
    • Kiang TK, Ensom MH, and Chang TK (2005) UDP-glucuronosyltransferases and clinical drug-drug interactions. Pharmacol Ther 106:97-132.
    • (2005) Pharmacol Ther , vol.106 , pp. 97-132
    • Kiang, T.K.1    Ensom, M.H.2    Chang, T.K.3
  • 12
    • 33646533631 scopus 로고    scopus 로고
    • Binding of gefitinib, an inhibitor of epidermal growth factor receptor-tyrosine kinase, to plasma proteins and blood cells: In vitro and in cancer patients
    • Li J, Brahmer J, Messersmith W, Hidalgo M, and Baker SD (2006) Binding of gefitinib, an inhibitor of epidermal growth factor receptor-tyrosine kinase, to plasma proteins and blood cells: in vitro and in cancer patients. Invest New Drugs 24:291-297.
    • (2006) Invest New Drugs , vol.24 , pp. 291-297
    • Li, J.1    Brahmer, J.2    Messersmith, W.3    Hidalgo, M.4    Baker, S.D.5
  • 13
    • 34250694236 scopus 로고    scopus 로고
    • Differential metabolism of gefitinib and erlotinib by human cytochrome P450 enzymes
    • Li J, Zhao M, He P, Hidalgo M, and Baker SD (2007) Differential metabolism of gefitinib and erlotinib by human cytochrome P450 enzymes. Clin Cancer Res 13:3731-3737.
    • (2007) Clin Cancer Res , vol.13 , pp. 3731-3737
    • Li, J.1    Zhao, M.2    He, P.3    Hidalgo, M.4    Baker, S.D.5
  • 16
    • 33646077674 scopus 로고    scopus 로고
    • In vitro-in vivo correlation for drugs and other compounds eliminated by glucuronidation in humans: Pitfalls and promises
    • Miners JO, Knights KM, Houston JB, and Mackenzie PI (2006) In vitro-in vivo correlation for drugs and other compounds eliminated by glucuronidation in humans: pitfalls and promises. Biochem Pharmacol 71:1531-1539.
    • (2006) Biochem Pharmacol , vol.71 , pp. 1531-1539
    • Miners, J.O.1    Knights, K.M.2    Houston, J.B.3    Mackenzie, P.I.4
  • 17
    • 0036266825 scopus 로고    scopus 로고
    • Imipramine N-glucuronidation in human liver microsomes: Biphasic kinetics and characterization of UDP-glucuronosyltransferase isoforms
    • Nakajima M, Tanaka E, Kobayashi T, Ohashi N, Kume T, and Yokoi T (2002) Imipramine N-glucuronidation in human liver microsomes: biphasic kinetics and characterization of UDP-glucuronosyltransferase isoforms. Drug Metab Dispos 30:636-642.
    • (2002) Drug Metab Dispos , vol.30 , pp. 636-642
    • Nakajima, M.1    Tanaka, E.2    Kobayashi, T.3    Ohashi, N.4    Kume, T.5    Yokoi, T.6
  • 20
    • 0036569870 scopus 로고    scopus 로고
    • ZD1839, a selective oral epidermal growth factor receptor-tyrosine kinase inhibitor, is well tolerated and active in patients with solid, malignant tumors: Results of a phase I trial
    • Ranson M, Hammond LA, Ferry D, Kris M, Tullo A, Murray PI, Miller V, Averbuch S, Ochs J, Morris C, et al. (2002) ZD1839, a selective oral epidermal growth factor receptor-tyrosine kinase inhibitor, is well tolerated and active in patients with solid, malignant tumors: results of a phase I trial. J Clin Oncol 20:2240-2250.
    • (2002) J Clin Oncol , vol.20 , pp. 2240-2250
    • Ranson, M.1    Hammond, L.A.2    Ferry, D.3    Kris, M.4    Tullo, A.5    Murray, P.I.6    Miller, V.7    Averbuch, S.8    Ochs, J.9    Morris, C.10
  • 21
    • 0036893374 scopus 로고    scopus 로고
    • Inhibition and active sites of UDP-glucuronosyltransferases 2B7 and 1A1
    • Rios GR and Tephly TR (2002) Inhibition and active sites of UDP-glucuronosyltransferases 2B7 and 1A1. Drug Metab Dispos 30:1364-1367.
    • (2002) Drug Metab Dispos , vol.30 , pp. 1364-1367
    • Rios, G.R.1    Tephly, T.R.2
  • 24
    • 39649116928 scopus 로고    scopus 로고
    • EGFR tyrosine kinase inhibitors in lung cancer: An evolving story
    • Sequist LV and Lynch TJ (2008) EGFR tyrosine kinase inhibitors in lung cancer: an evolving story. Annu Rev Med 59:429-442.
    • (2008) Annu Rev Med , vol.59 , pp. 429-442
    • Sequist, L.V.1    Lynch, T.J.2
  • 25
    • 26444519872 scopus 로고    scopus 로고
    • Current knowledge and future directions of the selective epidermal growth factor receptor inhibitors erlotinib (Tarceva) and gefitinib (Iressa)
    • Siegel-Lakhai WS, Beijnen JH, and Schellens JH (2005) Current knowledge and future directions of the selective epidermal growth factor receptor inhibitors erlotinib (Tarceva) and gefitinib (Iressa). Oncologist 10:579-589.
    • (2005) Oncologist , vol.10 , pp. 579-589
    • Siegel-Lakhai, W.S.1    Beijnen, J.H.2    Schellens, J.H.3
  • 26
    • 28444489982 scopus 로고    scopus 로고
    • Erlotinib: Small-molecule targeted therapy in the treatment of non-small-cell lung cancer
    • Smith J (2005) Erlotinib: small-molecule targeted therapy in the treatment of non-small-cell lung cancer. Clin Ther 27:1513-1534.
    • (2005) Clin Ther , vol.27 , pp. 1513-1534
    • Smith, J.1
  • 27
    • 0030800075 scopus 로고    scopus 로고
    • Differential expression of the UGT1A locus in human liver, biliary, and gastric tissue: Identification of UGT1A7 and UGT1A10 transcripts in extrahepatic tissue
    • Strassburg CP, Oldhafer K, Manns MP, and Tukey RH (1997) Differential expression of the UGT1A locus in human liver, biliary, and gastric tissue: identification of UGT1A7 and UGT1A10 transcripts in extrahepatic tissue. Mol Pharmacol 52:212-220.
    • (1997) Mol Pharmacol , vol.52 , pp. 212-220
    • Strassburg, C.P.1    Oldhafer, K.2    Manns, M.P.3    Tukey, R.H.4
  • 28
    • 33745899929 scopus 로고    scopus 로고
    • Exploring the relationship between expression of cytochrome P450 enzymes and gefitinib pharmacokinetics
    • Swaisland HC, Cantarini MV, Fuhr R, and Holt A (2006) Exploring the relationship between expression of cytochrome P450 enzymes and gefitinib pharmacokinetics. Clin Pharmacokinet 45:633-644.
    • (2006) Clin Pharmacokinet , vol.45 , pp. 633-644
    • Swaisland, H.C.1    Cantarini, M.V.2    Fuhr, R.3    Holt, A.4
  • 30
    • 33344473930 scopus 로고    scopus 로고
    • Selectivity of substrate (trifluoperazine) and inhibitor (amitriptyline, androsterone, canrenoic acid, hecogenin, phenylbutazone, quinidine, quinine, and sulfinpyrazone) "probes" for human UDP-glucuronosyltransferases
    • Uchaipichat V, Mackenzie PI, Elliot DJ, and Miners JO (2006a) Selectivity of substrate (trifluoperazine) and inhibitor (amitriptyline, androsterone, canrenoic acid, hecogenin, phenylbutazone, quinidine, quinine, and sulfinpyrazone) "probes" for human UDP-glucuronosyltransferases. Drug Metab Dispos 34:449-456.
    • (2006) Drug Metab Dispos , vol.34 , pp. 449-456
    • Uchaipichat, V.1    Mackenzie, P.I.2    Elliot, D.J.3    Miners, J.O.4
  • 31
    • 1842536833 scopus 로고    scopus 로고
    • Human UDP-glucuronosyltransferases: Isoform selectivity and kinetics of 4-methylumbelliferone and 1-naphthol glucuronidation, effects of organic solvents, and inhibition by diclofenac and probenecid
    • Uchaipichat V, Mackenzie PI, Guo XH, Gardner-Stephen D, Galetin A, Houston JB, and Miners JO (2004) Human UDP-glucuronosyltransferases: isoform selectivity and kinetics of 4-methylumbelliferone and 1-naphthol glucuronidation, effects of organic solvents, and inhibition by diclofenac and probenecid. Drug Metab Dispos 32:413-423.
    • (2004) Drug Metab Dispos , vol.32 , pp. 413-423
    • Uchaipichat, V.1    Mackenzie, P.I.2    Guo, X.H.3    Gardner-Stephen, D.4    Galetin, A.5    Houston, J.B.6    Miners, J.O.7
  • 32
    • 33344478229 scopus 로고    scopus 로고
    • Quantitative prediction of in vivo inhibitory interactions involving glucuronidated drugs from in vitro data: The effect of fluconazole on zidovudine glucuronidation
    • Uchaipichat V, Winner LK, Mackenzie PI, Elliot DJ, Williams JA, and Miners JO (2006b) Quantitative prediction of in vivo inhibitory interactions involving glucuronidated drugs from in vitro data: the effect of fluconazole on zidovudine glucuronidation. Br J Clin Pharmacol 61:427-439.
    • (2006) Br J Clin Pharmacol , vol.61 , pp. 427-439
    • Uchaipichat, V.1    Winner, L.K.2    Mackenzie, P.I.3    Elliot, D.J.4    Williams, J.A.5    Miners, J.O.6
  • 33
    • 34748822655 scopus 로고    scopus 로고
    • Influence of mutations associated with Gilbert and Crigler-Najjar type II syndromes on the glucuronidation kinetics of bilirubin and other UDP-glucuronosyltransferase 1A substrates
    • Udomuksorn W, Elliot DJ, Lewis BC, Mackenzie PI, Yoovathaworn K, and Miners JO (2007) Influence of mutations associated with Gilbert and Crigler-Najjar type II syndromes on the glucuronidation kinetics of bilirubin and other UDP-glucuronosyltransferase 1A substrates. Pharmacogenet Genomics 17:1017-1029.
    • (2007) Pharmacogenet Genomics , vol.17 , pp. 1017-1029
    • Udomuksorn, W.1    Elliot, D.J.2    Lewis, B.C.3    Mackenzie, P.I.4    Yoovathaworn, K.5    Miners, J.O.6
  • 34
    • 20344380924 scopus 로고    scopus 로고
    • A phase II trial of gefitinib with 5-fluorouracil, leucovorin, and irinotecan in patients with colorectal cancer
    • Veronese ML, Sun W, Giantonio B, Berlin J, Shults J, Davis L, Haller DG, and O'Dwyer PJ (2005) A phase II trial of gefitinib with 5-fluorouracil, leucovorin, and irinotecan in patients with colorectal cancer. Br J Cancer 92:1846-1849.
    • (2005) Br J Cancer , vol.92 , pp. 1846-1849
    • Veronese, M.L.1    Sun, W.2    Giantonio, B.3    Berlin, J.4    Shults, J.5    Davis, L.6    Haller, D.G.7    O'Dwyer, P.J.8
  • 35
    • 33847358669 scopus 로고    scopus 로고
    • UDP- glucuronosyltransferase 1A1 is the principal enzyme responsible for etoposide glucuronidation in human liver and intestinal microsomes: Structural characterization of phenolic and alcoholic glucuronides of etoposide and estimation of enzyme kinetics
    • Wen Z, Tallman MN, Ali SY, and Smith PC (2007) UDP- glucuronosyltransferase 1A1 is the principal enzyme responsible for etoposide glucuronidation in human liver and intestinal microsomes: structural characterization of phenolic and alcoholic glucuronides of etoposide and estimation of enzyme kinetics. Drug Metab Dispos 35:371-380.
    • (2007) Drug Metab Dispos , vol.35 , pp. 371-380
    • Wen, Z.1    Tallman, M.N.2    Ali, S.Y.3    Smith, P.C.4
  • 36
    • 6944221357 scopus 로고    scopus 로고
    • Drug-drug interactions for UDP- glucuronosyltransferase substrates: A pharmacokinetic explanation for typically observed low exposure (AUCi/AUC) ratios
    • Williams JA, Hyland R, Jones BC, Smith DA, Hurst S, Goosen TC, Peterkin V, Koup JR, and Ball SE (2004) Drug-drug interactions for UDP- glucuronosyltransferase substrates: a pharmacokinetic explanation for typically observed low exposure (AUCi/AUC) ratios. Drug Metab Dispos 32:1201-1208.
    • (2004) Drug Metab Dispos , vol.32 , pp. 1201-1208
    • Williams, J.A.1    Hyland, R.2    Jones, B.C.3    Smith, D.A.4    Hurst, S.5    Goosen, T.C.6    Peterkin, V.7    Koup, J.R.8    Ball, S.E.9
  • 37
    • 0036843701 scopus 로고    scopus 로고
    • Differential modulation of UDP-glucuronosyltransferase 1A1 (UGT1A1)-catalyzed estradiol-3-glucuronidation by the addition of UGT1A1 substrates and other compounds to human liver microsomes
    • Williams JA, Ring BJ, Cantrell VE, Campanale K, Jones DR, Hall SD, and Wrighton SA (2002) Differential modulation of UDP-glucuronosyltransferase 1A1 (UGT1A1)-catalyzed estradiol-3-glucuronidation by the addition of UGT1A1 substrates and other compounds to human liver microsomes. Drug Metab Dispos 30:1266-1273.
    • (2002) Drug Metab Dispos , vol.30 , pp. 1266-1273
    • Williams, J.A.1    Ring, B.J.2    Cantrell, V.E.3    Campanale, K.4    Jones, D.R.5    Hall, S.D.6    Wrighton, S.A.7
  • 38
    • 37249041552 scopus 로고    scopus 로고
    • Phase I dose-finding and pharmacokinetic study of the oral epidermal growth factor receptor tyrosine kinase inhibitor Ro50-8231 (erlotinib) in Japanese patients with solid tumors
    • Yamamoto N, Horiike A, Fujisaka Y, Murakami H, Shimoyama T, Yamada Y, and Tamura T (2008) Phase I dose-finding and pharmacokinetic study of the oral epidermal growth factor receptor tyrosine kinase inhibitor Ro50-8231 (erlotinib) in Japanese patients with solid tumors. Cancer Chemother Pharmacol 61:489-496.
    • (2008) Cancer Chemother Pharmacol , vol.61 , pp. 489-496
    • Yamamoto, N.1    Horiike, A.2    Fujisaka, Y.3    Murakami, H.4    Shimoyama, T.5    Yamada, Y.6    Tamura, T.7
  • 39
    • 27544468948 scopus 로고    scopus 로고
    • In vitro inhibition of UDP glucuronosyltransferases by atazanavir and other HIV protease inhibitors and the relationship of this property to in vivo bilirubin glucuronidation
    • Zhang D, Chando TJ, Everett DW, Patten CJ, Dehal SS, and Humphreys WG (2005) In vitro inhibition of UDP glucuronosyltransferases by atazanavir and other HIV protease inhibitors and the relationship of this property to in vivo bilirubin glucuronidation. Drug Metab Dispos 33:1729-1739.
    • (2005) Drug Metab Dispos , vol.33 , pp. 1729-1739
    • Zhang, D.1    Chando, T.J.2    Everett, D.W.3    Patten, C.J.4    Dehal, S.S.5    Humphreys, W.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.