메뉴 건너뛰기




Volumn 30, Issue 1, 2015, Pages 21-29

Prediction of hepatic and intestinal glucuronidation using in vitro-in vivo extrapolation

Author keywords

Availability; Clearance Prediction; Glucuronidation; In vitro in vivo extrapolation; Intestine; Liver; UDP glucuronosyltransferase

Indexed keywords

GLUCURONOSYLTRANSFERASE; DRUG; GLUCURONIDE; ISOENZYME;

EID: 84924967299     PISSN: 13474367     EISSN: 18800920     Source Type: Journal    
DOI: 10.1016/j.dmpk.2014.10.001     Document Type: Review
Times cited : (29)

References (63)
  • 1
    • 4344645978 scopus 로고    scopus 로고
    • Can the pharmaceutical industry reduce attrition rates?
    • I. Kola, and J. Landis Can the pharmaceutical industry reduce attrition rates? Nat Rev Drug Discov 3 2004 711 715
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 711-715
    • Kola, I.1    Landis, J.2
  • 2
    • 0030937636 scopus 로고    scopus 로고
    • Prediction of in vivo drug metabolism in the human liver from in vitro metabolism data
    • T. Iwatsubo, N. Hirota, T. Ooie, H. Suzuki, N. Shimada, and K. Chiba Prediction of in vivo drug metabolism in the human liver from in vitro metabolism data Pharmacol Ther 73 1997 147 171
    • (1997) Pharmacol Ther , vol.73 , pp. 147-171
    • Iwatsubo, T.1    Hirota, N.2    Ooie, T.3    Suzuki, H.4    Shimada, N.5    Chiba, K.6
  • 3
    • 0025719746 scopus 로고
    • First-pass metabolism of cyclosporin by the gut
    • J.C. Kolars, W.M. Awni, R.M. Merion, and P.B. Watkins First-pass metabolism of cyclosporin by the gut Lancet 338 1991 1488 1490
    • (1991) Lancet , vol.338 , pp. 1488-1490
    • Kolars, J.C.1    Awni, W.M.2    Merion, R.M.3    Watkins, P.B.4
  • 5
    • 79551661535 scopus 로고    scopus 로고
    • Predicting clearance in humans from in vitro data
    • R.S. Obach Predicting clearance in humans from in vitro data Curr Top Med Chem 11 2011 334 339
    • (2011) Curr Top Med Chem , vol.11 , pp. 334-339
    • Obach, R.S.1
  • 6
    • 84860281804 scopus 로고    scopus 로고
    • A practical and direct comparison of intrinsic metabolic clearance of several non-CYP enzyme substrates in freshly isolated and cryopreserved hepatocytes
    • T. Akabane, N. Gerst, Y. Naritomi, J.N. Masters, and K. Tamura A practical and direct comparison of intrinsic metabolic clearance of several non-CYP enzyme substrates in freshly isolated and cryopreserved hepatocytes Drug Metab Pharmacokinet 27 2012 181 191
    • (2012) Drug Metab Pharmacokinet , vol.27 , pp. 181-191
    • Akabane, T.1    Gerst, N.2    Naritomi, Y.3    Masters, J.N.4    Tamura, K.5
  • 7
    • 67650591016 scopus 로고    scopus 로고
    • Intestinal glucuronidation metabolism may have a greater impact on oral bioavailability than hepatic glucuronidation metabolism in humans: A study with raloxifene, substrate for UGT1A1, 1A8, 1A9, and 1A10
    • T. Mizuma Intestinal glucuronidation metabolism may have a greater impact on oral bioavailability than hepatic glucuronidation metabolism in humans: a study with raloxifene, substrate for UGT1A1, 1A8, 1A9, and 1A10 Int J Pharm 378 2009 140 141
    • (2009) Int J Pharm , vol.378 , pp. 140-141
    • Mizuma, T.1
  • 8
    • 77953777072 scopus 로고    scopus 로고
    • Quantitative prediction of intestinal metabolism in humans from a simplified intestinal availability model and empirical scaling factor
    • K. Kadono, T. Akabane, K. Tabata, K. Gato, S. Terashita, and T. Teramura Quantitative prediction of intestinal metabolism in humans from a simplified intestinal availability model and empirical scaling factor Drug Metab Dispos 38 2010 1230 1237
    • (2010) Drug Metab Dispos , vol.38 , pp. 1230-1237
    • Kadono, K.1    Akabane, T.2    Tabata, K.3    Gato, K.4    Terashita, S.5    Teramura, T.6
  • 9
    • 6944221357 scopus 로고    scopus 로고
    • Drug-drug interactions for UDP-glucuronosyltransferase substrates: A pharmacokinetic explanation for typically observed low exposure (AUCi/AUC) ratios
    • J.A. Williams, R. Hyland, B.C. Jones, D.A. Smith, S. Hurst, and T.C. Goosen Drug-drug interactions for UDP-glucuronosyltransferase substrates: a pharmacokinetic explanation for typically observed low exposure (AUCi/AUC) ratios Drug Metab Dispos 32 2004 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
  • 10
    • 0036890353 scopus 로고    scopus 로고
    • Complexities of glucuronidation affecting in vitro in vivo extrapolation
    • J.H. Lin, and B.K. Wong Complexities of glucuronidation affecting in vitro in vivo extrapolation Curr Drug Metab 3 2002 623 646
    • (2002) Curr Drug Metab , vol.3 , pp. 623-646
    • Lin, J.H.1    Wong, B.K.2
  • 11
    • 0344610168 scopus 로고    scopus 로고
    • Predicting human drug glucuronidation parameters: Application of in vitro and in silico modeling approaches
    • J.O. Miners, P.A. Smith, M.J. Sorich, R.A. McKinnon, and P.I. Mackenzie Predicting human drug glucuronidation parameters: application of in vitro and in silico modeling approaches Annu Rev Pharmacol Toxicol 44 2004 1 25
    • (2004) Annu Rev Pharmacol Toxicol , vol.44 , pp. 1-25
    • Miners, J.O.1    Smith, P.A.2    Sorich, M.J.3    McKinnon, R.A.4    Mackenzie, P.I.5
  • 12
    • 33646077674 scopus 로고    scopus 로고
    • In vitro-in vivo correlation for drugs and other compounds eliminated by glucuronidation in humans: Pitfalls and promises
    • J.O. Miners, K.M. Knights, J.B. Houston, and P.I. Mackenzie In vitro-in vivo correlation for drugs and other compounds eliminated by glucuronidation in humans: pitfalls and promises Biochem Pharmacol 71 2006 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
  • 13
    • 34250329999 scopus 로고    scopus 로고
    • Intestinal UGTs as potential modifiers of pharmacokinetics and biological responses to drugs and xenobiotics
    • J.K. Ritter Intestinal UGTs as potential modifiers of pharmacokinetics and biological responses to drugs and xenobiotics Expert Opin Drug Metab Toxicol 3 2007 93 107
    • (2007) Expert Opin Drug Metab Toxicol , vol.3 , pp. 93-107
    • Ritter, J.K.1
  • 14
    • 74549222703 scopus 로고    scopus 로고
    • The prediction of drug-glucuronidation parameters in humans: UDP-glucuronosyltransferase enzyme-selective substrate and inhibitor probes for reaction phenotyping and in vitro-in vivo extrapolation of drug clearance and drug-drug interaction potential
    • J.O. Miners, P.I. Mackenzie, and K.M. Knights The prediction of drug-glucuronidation parameters in humans: UDP-glucuronosyltransferase enzyme-selective substrate and inhibitor probes for reaction phenotyping and in vitro-in vivo extrapolation of drug clearance and drug-drug interaction potential Drug Metab Rev 42 2010 196 208
    • (2010) Drug Metab Rev , vol.42 , pp. 196-208
    • Miners, J.O.1    Mackenzie, P.I.2    Knights, K.M.3
  • 15
    • 84881324657 scopus 로고    scopus 로고
    • Quantitative prediction of glucuronidation in humans using the in vitro- in vivo extrapolation approach
    • B. Wu, D. Dong, M. Hu, and S. Zhang Quantitative prediction of glucuronidation in humans using the in vitro- in vivo extrapolation approach Curr Top Med Chem 13 2013 1343 1352
    • (2013) Curr Top Med Chem , vol.13 , pp. 1343-1352
    • Wu, B.1    Dong, D.2    Hu, M.3    Zhang, S.4
  • 16
    • 0027216642 scopus 로고
    • Latency is the major determinant of UDP-glucuronosyltransferase activity in isolated hepatocytes
    • G. Bánhegyi, T. Garzó, R. Fulceri, A. Benedetti, and J. Mandl Latency is the major determinant of UDP-glucuronosyltransferase activity in isolated hepatocytes FEBS Lett 328 1993 149 152
    • (1993) FEBS Lett , vol.328 , pp. 149-152
    • Bánhegyi, G.1    Garzó, T.2    Fulceri, R.3    Benedetti, A.4    Mandl, J.5
  • 17
    • 0034128936 scopus 로고    scopus 로고
    • Human UDP-glucuronosyltransferases: Metabolism, expression, and disease
    • R.H. Tukey, and C.P. Strassburg Human UDP-glucuronosyltransferases: metabolism, expression, and disease Annu Rev Pharmacol Toxicol 40 2000 581 616
    • (2000) Annu Rev Pharmacol Toxicol , vol.40 , pp. 581-616
    • Tukey, R.H.1    Strassburg, C.P.2
  • 19
    • 58149467072 scopus 로고    scopus 로고
    • Determination of mRNA expression of human UDP-glucuronosyltransferases and application for localization in various human tissues by real-time reverse transcriptase-polymerase chain reaction
    • S. Ohno, and S. Nakajin Determination of mRNA expression of human UDP-glucuronosyltransferases and application for localization in various human tissues by real-time reverse transcriptase-polymerase chain reaction Drug Metab Dispos 37 2009 32 40
    • (2009) Drug Metab Dispos , vol.37 , pp. 32-40
    • Ohno, S.1    Nakajin, S.2
  • 20
    • 84898813968 scopus 로고    scopus 로고
    • Optimized methods for targeted peptide-based quantification of human uridine 5'-diphosphate-glucuronosyltransferases in biological specimens using liquid chromatography-tandem mass spectrometry
    • Y. Sato, M. Nagata, K. Tetsuka, K. Tamura, A. Miyashita, and A. Kawamura Optimized methods for targeted peptide-based quantification of human uridine 5'-diphosphate-glucuronosyltransferases in biological specimens using liquid chromatography-tandem mass spectrometry Drug Metab Dispos 42 2014 885 889
    • (2014) Drug Metab Dispos , vol.42 , pp. 885-889
    • Sato, Y.1    Nagata, M.2    Tetsuka, K.3    Tamura, K.4    Miyashita, A.5    Kawamura, A.6
  • 21
    • 84885222454 scopus 로고    scopus 로고
    • Targeted quantitative proteomics for the analysis of 14 UGT1As and -2Bs in human liver using NanoUPLC-MS/MS with selected reaction monitoring
    • J.K. Fallon, H. Neubert, R. Hyland, T.C. Goosen, and P.C. Smith Targeted quantitative proteomics for the analysis of 14 UGT1As and -2Bs in human liver using NanoUPLC-MS/MS with selected reaction monitoring J Proteome Res 12 2013 4402 4413
    • (2013) J Proteome Res , vol.12 , pp. 4402-4413
    • Fallon, J.K.1    Neubert, H.2    Hyland, R.3    Goosen, T.C.4    Smith, P.C.5
  • 22
    • 84855405567 scopus 로고    scopus 로고
    • Quantification of human uridine-diphosphate glucuronosyl transferase 1A isoforms in liver, intestine, and kidney using nanobore liquid chromatography-tandem mass spectrometry
    • D.E. Harbourt, J.K. Fallon, S. Ito, T. Baba, J.K. Ritter, and G.L. Glish Quantification of human uridine-diphosphate glucuronosyl transferase 1A isoforms in liver, intestine, and kidney using nanobore liquid chromatography-tandem mass spectrometry Anal Chem 84 2012 98 105
    • (2012) Anal Chem , vol.84 , pp. 98-105
    • Harbourt, D.E.1    Fallon, J.K.2    Ito, S.3    Baba, T.4    Ritter, J.K.5    Glish, G.L.6
  • 23
    • 10044251943 scopus 로고    scopus 로고
    • Modelling atypical CYP3A4 kinetics: Principles and pragmatism
    • J.B. Houston, and A. Galetin Modelling atypical CYP3A4 kinetics: principles and pragmatism Arch Biochem Biophys 433 2005 351 360
    • (2005) Arch Biochem Biophys , vol.433 , pp. 351-360
    • Houston, J.B.1    Galetin, A.2
  • 24
    • 0034835463 scopus 로고    scopus 로고
    • Prediction of human hepatic clearance from in vivo animal experiments and in vitro metabolic studies with liver microsomes from animals and humans
    • Y. Naritomi, S. Terashita, S. Kimura, A. Suzuki, A. Kagayama, and Y. Sugiyama Prediction of human hepatic clearance from in vivo animal experiments and in vitro metabolic studies with liver microsomes from animals and humans Drug Metab Dispos 29 2001 1316 1324
    • (2001) Drug Metab Dispos , vol.29 , pp. 1316-1324
    • Naritomi, Y.1    Terashita, S.2    Kimura, S.3    Suzuki, A.4    Kagayama, A.5    Sugiyama, Y.6
  • 26
    • 0017335453 scopus 로고
    • Prediction of hepatic extraction ratio from in vitro measurement of intrinsic clearance
    • A. Rane, G.R. Wilkinson, and D.G. Shand Prediction of hepatic extraction ratio from in vitro measurement of intrinsic clearance J Pharmacol Exp Ther 200 1977 420 424
    • (1977) J Pharmacol Exp Ther , vol.200 , pp. 420-424
    • Rane, A.1    Wilkinson, G.R.2    Shand, D.G.3
  • 27
    • 0017603437 scopus 로고
    • Hepatic clearance of drugs. I. Theoretical considerations of a "well-stirred" model and a "parallel tube" model. Influence of hepatic blood flow, plasma and blood cell binding, and the hepatocellular enzymatic activity on hepatic drug clearance
    • K.S. Pang, and M. Rowland Hepatic clearance of drugs. I. Theoretical considerations of a "well-stirred" model and a "parallel tube" model. Influence of hepatic blood flow, plasma and blood cell binding, and the hepatocellular enzymatic activity on hepatic drug clearance J Pharmacokinet Biopharm 5 1977 625 653
    • (1977) J Pharmacokinet Biopharm , vol.5 , pp. 625-653
    • Pang, K.S.1    Rowland, M.2
  • 28
    • 0022609024 scopus 로고
    • Correlation between in-vitro microsomal enzyme activity and whole organ hepatic elimination kinetics: Analysis with a dispersion model
    • M.S. Roberts, and M. Rowland Correlation between in-vitro microsomal enzyme activity and whole organ hepatic elimination kinetics: analysis with a dispersion model J Pharm Pharmacol 38 1986 177 181
    • (1986) J Pharm Pharmacol , vol.38 , pp. 177-181
    • Roberts, M.S.1    Rowland, M.2
  • 29
    • 0030833366 scopus 로고    scopus 로고
    • Improving the in vivo duration of 5-lipoxygenase inhibitors: Application of an in vitro glucuronosyltransferase assay
    • J.J. Bouska, R.L. Bell, C.L. Goodfellow, A.O. Stewart, C.D. Brooks, and G.W. Carter Improving the in vivo duration of 5-lipoxygenase inhibitors: application of an in vitro glucuronosyltransferase assay Drug Metab Dispos 25 1997 1032 1038
    • (1997) Drug Metab Dispos , vol.25 , pp. 1032-1038
    • Bouska, J.J.1    Bell, R.L.2    Goodfellow, C.L.3    Stewart, A.O.4    Brooks, C.D.5    Carter, G.W.6
  • 30
    • 0023488459 scopus 로고
    • Glucuronidation in vitro and in vivo. Comparison of intestinal and hepatic conjugation of morphine, naloxone, and buprenorphine
    • M. Mistry, and J.B. Houston Glucuronidation in vitro and in vivo. Comparison of intestinal and hepatic conjugation of morphine, naloxone, and buprenorphine Drug Metab Dispos 15 1987 710 717
    • (1987) Drug Metab Dispos , vol.15 , pp. 710-717
    • Mistry, M.1    Houston, J.B.2
  • 31
    • 0030973810 scopus 로고    scopus 로고
    • Pharmacokinetics of troglitazone, an antidiabetic agent: Prediction of in vivo stereoselective sulfation and glucuronidation from in vitro data
    • T. Izumi, K. Hosiyama, S. Enomoto, K. Sasahara, and Y. Sugiyama Pharmacokinetics of troglitazone, an antidiabetic agent: prediction of in vivo stereoselective sulfation and glucuronidation from in vitro data J Pharmacol Exp Ther 280 1997 1392 1400
    • (1997) J Pharmacol Exp Ther , vol.280 , pp. 1392-1400
    • Izumi, T.1    Hosiyama, K.2    Enomoto, S.3    Sasahara, K.4    Sugiyama, Y.5
  • 32
    • 42249089353 scopus 로고    scopus 로고
    • Prediction of metabolic clearance of diclofenac in adjuvant-induced arthritis rats using a substrate depletion assay
    • S. Uno, A. Fujii, H. Komura, A. Kawase, and M. Iwaki Prediction of metabolic clearance of diclofenac in adjuvant-induced arthritis rats using a substrate depletion assay Xenobiotica 38 2008 482 495
    • (2008) Xenobiotica , vol.38 , pp. 482-495
    • Uno, S.1    Fujii, A.2    Komura, H.3    Kawase, A.4    Iwaki, M.5
  • 33
    • 80055076448 scopus 로고    scopus 로고
    • Correlation of intrinsic in vitro and in vivo clearance for drugs metabolized by hepatic UDP-glucuronosyltransferases in rats
    • F. Nakamori, Y. Naritomi, M. Furutani, F. Takamura, H. Miura, and H. Murai Correlation of intrinsic in vitro and in vivo clearance for drugs metabolized by hepatic UDP-glucuronosyltransferases in rats Drug Metab Pharmacokinet 26 2011 465 473
    • (2011) Drug Metab Pharmacokinet , vol.26 , pp. 465-473
    • Nakamori, F.1    Naritomi, Y.2    Furutani, M.3    Takamura, F.4    Miura, H.5    Murai, H.6
  • 35
    • 0036894822 scopus 로고    scopus 로고
    • Extrapolation of diclofenac clearance from in vitro microsomal metabolism data: Role of acyl glucuronidation and sequential oxidative metabolism of the acyl glucuronide
    • S. Kumar, K. Samuel, R. Subramanian, M.P. Braun, R.A. Stearns, and S.H. Chiu Extrapolation of diclofenac clearance from in vitro microsomal metabolism data: role of acyl glucuronidation and sequential oxidative metabolism of the acyl glucuronide J Pharmacol Exp Ther 303 2002 969 978
    • (2002) J Pharmacol Exp Ther , vol.303 , pp. 969-978
    • Kumar, S.1    Samuel, K.2    Subramanian, R.3    Braun, M.P.4    Stearns, R.A.5    Chiu, S.H.6
  • 36
    • 0038532316 scopus 로고    scopus 로고
    • The effect of incubation conditions on the enzyme kinetics of UDP-glucuronosyltransferases
    • M.G. Soars, B.J. Ring, and S.A. Wrighton The effect of incubation conditions on the enzyme kinetics of UDP-glucuronosyltransferases Drug Metab Dispos 31 2003 762 767
    • (2003) Drug Metab Dispos , vol.31 , pp. 762-767
    • Soars, M.G.1    Ring, B.J.2    Wrighton, S.A.3
  • 37
    • 33745253947 scopus 로고    scopus 로고
    • Predominant contribution of OATP1B3 to the hepatic uptake of telmisartan, an angiotensin II receptor antagonist, in humans
    • N. Ishiguro, K. Maeda, W. Kishimoto, A. Saito, A. Harada, and T. Ebner Predominant contribution of OATP1B3 to the hepatic uptake of telmisartan, an angiotensin II receptor antagonist, in humans Drug Metab Dispos 34 2006 1109 1115
    • (2006) Drug Metab Dispos , vol.34 , pp. 1109-1115
    • Ishiguro, N.1    Maeda, K.2    Kishimoto, W.3    Saito, A.4    Harada, A.5    Ebner, T.6
  • 38
    • 33947398317 scopus 로고    scopus 로고
    • Binding of inhibitory fatty acids is responsible for the enhancement of UDP-glucuronosyltransferase 2B7 activity by albumin: Implications for in vitro-in vivo extrapolation
    • A. Rowland, P. Gaganis, D.J. Elliot, P.I. Mackenzie, K.M. Knights, and J.O. Miners Binding of inhibitory fatty acids is responsible for the enhancement of UDP-glucuronosyltransferase 2B7 activity by albumin: implications for in vitro-in vivo extrapolation J Pharmacol Exp Ther 321 2007 137 147
    • (2007) J Pharmacol Exp Ther , vol.321 , pp. 137-147
    • Rowland, A.1    Gaganis, P.2    Elliot, D.J.3    Mackenzie, P.I.4    Knights, K.M.5    Miners, J.O.6
  • 39
    • 0036435763 scopus 로고    scopus 로고
    • In vitro-in vivo correlations for drugs eliminated by glucuronidation: Investigations with the model substrate zidovudine
    • S. Boase, and J.O. Miners In vitro-in vivo correlations for drugs eliminated by glucuronidation: investigations with the model substrate zidovudine Br J Clin Pharmacol 54 2002 493 503
    • (2002) Br J Clin Pharmacol , vol.54 , pp. 493-503
    • Boase, S.1    Miners, J.O.2
  • 40
    • 0036194124 scopus 로고    scopus 로고
    • In vitro analysis of human drug glucuronidation and prediction of in vivo metabolic clearance
    • M.G. Soars, B. Burchell, and R.J. Riley In vitro analysis of human drug glucuronidation and prediction of in vivo metabolic clearance J Pharmacol Exp Ther 301 2002 382 390
    • (2002) J Pharmacol Exp Ther , vol.301 , pp. 382-390
    • Soars, M.G.1    Burchell, B.2    Riley, R.J.3
  • 41
    • 0036707622 scopus 로고    scopus 로고
    • Glucuronidation of dihydroartemisinin in vivo and by human liver microsomes and expressed UDP-glucuronosyltransferases
    • K.F. Ilett, B.T. Ethell, J.L. Maggs, T.M. Davis, K.T. Batty, and B. Burchell Glucuronidation of dihydroartemisinin in vivo and by human liver microsomes and expressed UDP-glucuronosyltransferases Drug Metab Dispos 30 2002 1005 1012
    • (2002) Drug Metab Dispos , vol.30 , pp. 1005-1012
    • Ilett, K.F.1    Ethell, B.T.2    Maggs, J.L.3    Davis, T.M.4    Batty, K.T.5    Burchell, B.6
  • 42
    • 27544506707 scopus 로고    scopus 로고
    • Altered AZT (3′-azido-3'-deoxythymidine) glucuronidation kinetics in liver microsomes as an explanation for underprediction of in vivo clearance: Comparison to hepatocytes and effect of incubation environment
    • J.J. Engtrakul, R.S. Foti, T.J. Strelevitz, and M.B. Fisher Altered AZT (3′-azido-3'-deoxythymidine) glucuronidation kinetics in liver microsomes as an explanation for underprediction of in vivo clearance: comparison to hepatocytes and effect of incubation environment Drug Metab Dispos 33 2005 1621 1627
    • (2005) Drug Metab Dispos , vol.33 , pp. 1621-1627
    • Engtrakul, J.J.1    Foti, R.S.2    Strelevitz, T.J.3    Fisher, M.B.4
  • 43
    • 0345549371 scopus 로고    scopus 로고
    • Evidence that unsaturated fatty acids are potent inhibitors of renal UDP-glucuronosyltransferases (UGT): Kinetic studies using human kidney cortical microsomes and recombinant UGT1A9 and UGT2B7
    • P. Tsoutsikos, J.O. Miners, A. Stapleton, A. Thomas, B.C. Sallustio, and K.M. Knights Evidence that unsaturated fatty acids are potent inhibitors of renal UDP-glucuronosyltransferases (UGT): kinetic studies using human kidney cortical microsomes and recombinant UGT1A9 and UGT2B7 Biochem Pharmacol 67 2004 191 199
    • (2004) Biochem Pharmacol , vol.67 , pp. 191-199
    • Tsoutsikos, P.1    Miners, J.O.2    Stapleton, A.3    Thomas, A.4    Sallustio, B.C.5    Knights, K.M.6
  • 44
    • 44149117018 scopus 로고    scopus 로고
    • The "albumin effect" and drug glucuronidation: Bovine serum albumin and fatty acid-free human serum albumin enhance the glucuronidation of UDP-glucuronosyltransferase (UGT) 1A9 substrates but not UGT1A1 and UGT1A6 activities
    • A. Rowland, K.M. Knights, P.I. Mackenzie, and J.O. Miners The "albumin effect" and drug glucuronidation: bovine serum albumin and fatty acid-free human serum albumin enhance the glucuronidation of UDP-glucuronosyltransferase (UGT) 1A9 substrates but not UGT1A1 and UGT1A6 activities Drug Metab Dispos 36 2008 1056 1062
    • (2008) Drug Metab Dispos , vol.36 , pp. 1056-1062
    • Rowland, A.1    Knights, K.M.2    Mackenzie, P.I.3    Miners, J.O.4
  • 45
    • 67649411647 scopus 로고    scopus 로고
    • Characterization of the binding of drugs to human intestinal fatty acid binding protein (IFABP): Potential role of IFABP as an alternative to albumin for in vitro-in vivo extrapolation of drug kinetic parameters
    • A. Rowland, K.M. Knights, P.I. Mackenzie, and J.O. Miners Characterization of the binding of drugs to human intestinal fatty acid binding protein (IFABP): potential role of IFABP as an alternative to albumin for in vitro-in vivo extrapolation of drug kinetic parameters Drug Metab Dispos 37 2009 1395 1403
    • (2009) Drug Metab Dispos , vol.37 , pp. 1395-1403
    • Rowland, A.1    Knights, K.M.2    Mackenzie, P.I.3    Miners, J.O.4
  • 46
    • 80054737088 scopus 로고    scopus 로고
    • Bovine serum albumin decreases Km values of human UDP-glucuronosyltransferases 1A9 and 2B7 and increases Vmax values of UGT1A9
    • N. Manevski, P.S. Moreolo, J. Yli-Kauhaluoma, and M. Finel Bovine serum albumin decreases Km values of human UDP-glucuronosyltransferases 1A9 and 2B7 and increases Vmax values of UGT1A9 Drug Metab Dispos 39 2011 2117 2129
    • (2011) Drug Metab Dispos , vol.39 , pp. 2117-2129
    • Manevski, N.1    Moreolo, P.S.2    Yli-Kauhaluoma, J.3    Finel, M.4
  • 47
    • 58149472377 scopus 로고    scopus 로고
    • Prediction of drug clearance by glucuronidation from in vitro data: Use of combined cytochrome P450 and UDP-glucuronosyltransferase cofactors in alamethicin-activated human liver microsomes
    • P.J. Kilford, R. Stringer, B. Sohal, J.B. Houston, and A. Galetin Prediction of drug clearance by glucuronidation from in vitro data: use of combined cytochrome P450 and UDP-glucuronosyltransferase cofactors in alamethicin-activated human liver microsomes Drug Metab Dispos 37 2009 82 89
    • (2009) Drug Metab Dispos , vol.37 , pp. 82-89
    • Kilford, P.J.1    Stringer, R.2    Sohal, B.3    Houston, J.B.4    Galetin, A.5
  • 48
    • 79955023850 scopus 로고    scopus 로고
    • Prediction of human drug clearance by multiple metabolic pathways: Integration of hepatic and intestinal microsomal and cytosolic data
    • H.E. Cubitt, J.B. Houston, and A. Galetin Prediction of human drug clearance by multiple metabolic pathways: integration of hepatic and intestinal microsomal and cytosolic data Drug Metab Dispos 39 2011 864 873
    • (2011) Drug Metab Dispos , vol.39 , pp. 864-873
    • Cubitt, H.E.1    Houston, J.B.2    Galetin, A.3
  • 49
    • 34748895120 scopus 로고    scopus 로고
    • Prediction of metabolic clearance of bisphenol A (4,4 '-dihydroxy-2,2-diphenylpropane) using cryopreserved human hepatocytes
    • R.K. Kuester, and I.G. Sipes Prediction of metabolic clearance of bisphenol A (4,4 '-dihydroxy-2,2-diphenylpropane) using cryopreserved human hepatocytes Drug Metab Dispos 35 2007 1910 1915
    • (2007) Drug Metab Dispos , vol.35 , pp. 1910-1915
    • Kuester, R.K.1    Sipes, I.G.2
  • 50
    • 33745727113 scopus 로고    scopus 로고
    • Prediction of total propofol clearance based on enzyme activities in microsomes from human kidney and liver
    • W.S. Al-Jahdari, K. Yamamoto, H. Hiraoka, K. Nakamura, F. Goto, and R. Horiuchi Prediction of total propofol clearance based on enzyme activities in microsomes from human kidney and liver Eur J Clin Pharmacol 62 2006 527 533
    • (2006) Eur J Clin Pharmacol , vol.62 , pp. 527-533
    • Al-Jahdari, W.S.1    Yamamoto, K.2    Hiraoka, H.3    Nakamura, K.4    Goto, F.5    Horiuchi, R.6
  • 51
    • 84858404510 scopus 로고    scopus 로고
    • Characterization of in vitro glucuronidation clearance of a range of drugs in human kidney microsomes: Comparison with liver and intestinal glucuronidation and impact of albumin
    • K.L. Gill, J.B. Houston, and A. Galetin Characterization of in vitro glucuronidation clearance of a range of drugs in human kidney microsomes: comparison with liver and intestinal glucuronidation and impact of albumin Drug Metab Dispos 40 2012 825 835
    • (2012) Drug Metab Dispos , vol.40 , pp. 825-835
    • Gill, K.L.1    Houston, J.B.2    Galetin, A.3
  • 52
    • 84875859773 scopus 로고    scopus 로고
    • Application of a physiologically based pharmacokinetic model to assess propofol hepatic and renal glucuronidation in isolation: Utility of in vitro and in vivo data
    • K.L. Gill, M. Gertz, J.B. Houston, and A. Galetin Application of a physiologically based pharmacokinetic model to assess propofol hepatic and renal glucuronidation in isolation: utility of in vitro and in vivo data Drug Metab Dispos 41 2013 744 753
    • (2013) Drug Metab Dispos , vol.41 , pp. 744-753
    • Gill, K.L.1    Gertz, M.2    Houston, J.B.3    Galetin, A.4
  • 53
    • 84887231773 scopus 로고    scopus 로고
    • Using human recombinant UDP-glucuronosyltransferase isoforms and a relative activity factor approach to model total body clearance of laropiprant (MK-0524) in humans
    • C.R. Gibson, P. Lu, C. Maciolek, C. Wudarski, Z. Barter, and K. Rowland-Yeo Using human recombinant UDP-glucuronosyltransferase isoforms and a relative activity factor approach to model total body clearance of laropiprant (MK-0524) in humans Xenobiotica 43 2013 1027 1036
    • (2013) Xenobiotica , vol.43 , pp. 1027-1036
    • Gibson, C.R.1    Lu, P.2    Maciolek, C.3    Wudarski, C.4    Barter, Z.5    Rowland-Yeo, K.6
  • 55
    • 77953737073 scopus 로고    scopus 로고
    • Prediction of human intestinal first-pass metabolism of 25 CYP3A substrates from in vitro clearance and permeability data
    • M. Gertz, A. Harrison, J.B. Houston, and A. Galetin Prediction of human intestinal first-pass metabolism of 25 CYP3A substrates from in vitro clearance and permeability data Drug Metab Dispos 38 2010 1147 1158
    • (2010) Drug Metab Dispos , vol.38 , pp. 1147-1158
    • Gertz, M.1    Harrison, A.2    Houston, J.B.3    Galetin, A.4
  • 56
    • 84855219592 scopus 로고    scopus 로고
    • Prediction of the intestinal first-pass metabolism of CYP3A and UGT substrates in humans from in vitro data
    • H. Nishimuta, K. Sato, M. Yabuki, and S. Komuro Prediction of the intestinal first-pass metabolism of CYP3A and UGT substrates in humans from in vitro data Drug Metab Pharmacokinet 26 2011 592 601
    • (2011) Drug Metab Pharmacokinet , vol.26 , pp. 592-601
    • Nishimuta, H.1    Sato, K.2    Yabuki, M.3    Komuro, S.4
  • 57
    • 84865859368 scopus 로고    scopus 로고
    • Method for predicting human intestinal first-pass metabolism of UGT substrate compounds
    • T. Furukawa, K. Yamano, Y. Naritomi, K. Tanaka, S. Terashita, and T. Teramura Method for predicting human intestinal first-pass metabolism of UGT substrate compounds Xenobiotica 42 2012 980 988
    • (2012) Xenobiotica , vol.42 , pp. 980-988
    • Furukawa, T.1    Yamano, K.2    Naritomi, Y.3    Tanaka, K.4    Terashita, S.5    Teramura, T.6
  • 58
    • 84860298606 scopus 로고    scopus 로고
    • Quantitative prediction of intestinal glucuronidation of drugs in rats using in vitro metabolic clearance data
    • T. Furukawa, F. Nakamori, K. Tetsuka, Y. Naritomi, H. Moriguchi, and K. Yamano Quantitative prediction of intestinal glucuronidation of drugs in rats using in vitro metabolic clearance data Drug Metab Pharmacokinet 27 2012 171 180
    • (2012) Drug Metab Pharmacokinet , vol.27 , pp. 171-180
    • Furukawa, T.1    Nakamori, F.2    Tetsuka, K.3    Naritomi, Y.4    Moriguchi, H.5    Yamano, K.6
  • 60
    • 67649336984 scopus 로고    scopus 로고
    • Tissue-specific mRNA expression profiles of drug-metabolizing enzymes and transporters in the cynomolgus monkey
    • M. Nishimura, A. Koeda, H. Morikawa, T. Satoh, S. Narimatsu, and S. Naito Tissue-specific mRNA expression profiles of drug-metabolizing enzymes and transporters in the cynomolgus monkey Drug Metab Pharmacokinet 24 2009 139 144
    • (2009) Drug Metab Pharmacokinet , vol.24 , pp. 139-144
    • Nishimura, M.1    Koeda, A.2    Morikawa, H.3    Satoh, T.4    Narimatsu, S.5    Naito, S.6
  • 61
    • 84865196896 scopus 로고    scopus 로고
    • Quantitative prediction of human intestinal glucuronidation effects on intestinal availability of UDP-glucuronosyltransferase substrates using in vitro data
    • F. Nakamori, Y. Naritomi, K. Hosoya, H. Moriguchi, K. Tetsuka, and T. Furukawa Quantitative prediction of human intestinal glucuronidation effects on intestinal availability of UDP-glucuronosyltransferase substrates using in vitro data Drug Metab Dispos 40 2012 1771 1777
    • (2012) Drug Metab Dispos , vol.40 , pp. 1771-1777
    • Nakamori, F.1    Naritomi, Y.2    Hosoya, K.3    Moriguchi, H.4    Tetsuka, K.5    Furukawa, T.6
  • 62
    • 80054948359 scopus 로고    scopus 로고
    • In vitro and in vivo small intestinal metabolism of CYP3A and UGT substrates in preclinical animals species and humans: Species differences
    • H. Komura, and M. Iwaki In vitro and in vivo small intestinal metabolism of CYP3A and UGT substrates in preclinical animals species and humans: species differences Drug Metab Rev 43 2011 476 498
    • (2011) Drug Metab Rev , vol.43 , pp. 476-498
    • Komura, H.1    Iwaki, M.2
  • 63
    • 84893623513 scopus 로고    scopus 로고
    • Species differences in intestinal glucuronidation activities between humans, rats, dogs and monkeys
    • T. Furukawa, Y. Naritomi, K. Tetsuka, F. Nakamori, H. Moriguchi, and K. Yamano Species differences in intestinal glucuronidation activities between humans, rats, dogs and monkeys Xenobiotica 44 2014 205 216
    • (2014) Xenobiotica , vol.44 , pp. 205-216
    • Furukawa, T.1    Naritomi, Y.2    Tetsuka, K.3    Nakamori, F.4    Moriguchi, H.5    Yamano, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.