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Volumn 39, Issue 11, 2011, Pages 2117-2129

Bovine serum albumin decreases K m values of human UDP-glucuronosyltransferases 1A9 and 2B7 and increases V max values of UGT1A9

Author keywords

[No Author keywords available]

Indexed keywords

AGLYCONE; BOVINE SERUM ALBUMIN; ENTACAPONE; GLUCURONOSYLTRANSFERASE 1A9; GLUCURONOSYLTRANSFERASE 2B7; HYMECROMONE; RECOMBINANT ENZYME; URIDINE DIPHOSPHATE GLUCURONIC ACID; ZIDOVUDINE;

EID: 80054737088     PISSN: 00909556     EISSN: 1521009X     Source Type: Journal    
DOI: 10.1124/dmd.111.041418     Document Type: Article
Times cited : (55)

References (27)
  • 1
    • 0036435763 scopus 로고    scopus 로고
    • In vitro-in vivo correlations for drugs eliminated by glucuronidation: Investigations with the model substrate zidovudine
    • DOI 10.1046/j.1365-2125.2002.01669.x
    • Boase S and Miners JO (2002) In vitro-in vivo correlations for drugs eliminated by glucuronidation: investigations with the model substrate zidovudine. Br J Clin Pharmacol 54:493-503. (Pubitemid 35356875)
    • (2002) British Journal of Clinical Pharmacology , vol.54 , Issue.5 , pp. 493-503
    • Boase, S.1    Miners, J.O.2
  • 2
    • 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
    • DOI 10.1124/dmd.105.005058
    • Engtrakul JJ, Foti RS, Strelevitz TJ, and Fisher MB (2005) 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 33:1621-1627. (Pubitemid 41539959)
    • (2005) Drug Metabolism and Disposition , vol.33 , Issue.11 , pp. 1621-1627
    • Engtrakul, J.J.1    Foti, R.S.2    Strelevitz, T.J.3    Fisher, M.B.4
  • 4
    • 33645961595 scopus 로고    scopus 로고
    • The impact of in vitro binding on in vitro-in vivo extrapolations, projections of metabolic clearance and clinical drug-drug interactions
    • Grime K and Riley RJ (2006) The impact of in vitro binding on in vitro-in vivo extrapolations, projections of metabolic clearance and clinical drug-drug interactions. Curr Drug Metab 7:251-264.
    • (2006) Curr Drug Metab , vol.7 , pp. 251-264
    • Grime, K.1    Riley, R.J.2
  • 5
    • 0034105896 scopus 로고    scopus 로고
    • In vitro-in vivo scaling of cyp kinetic data not consistent with the classical Michaelis-Menten model
    • Houston JB and Kenworthy KE (2000) In vitro-in vivo scaling of CYP kinetic data not consistent with the classical Michaelis-Menten model. Drug Metab Dispos 28:246-254. (Pubitemid 30137047)
    • (2000) Drug Metabolism and Disposition , vol.28 , Issue.3 , pp. 246-254
    • Houston, J.B.1    Kenworthy, K.E.2
  • 6
    • 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
    • Kilford PJ, Stringer R, Sohal B, Houston JB, and Galetin A (2009) 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 37:82-89.
    • (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
  • 7
    • 0000574406 scopus 로고    scopus 로고
    • Evaluation of atypical cytochrome P450 kinetics with two-substrate models: Evidence that multiple substrates can simultaneously bind to cytochrome P450 active sites
    • DOI 10.1021/bi9715627
    • Korzekwa KR, Krishnamachary N, Shou M, Ogai A, Parise RA, Rettie AE, Gonzalez FJ, and Tracy TS (1998) Evaluation of atypical cytochrome P450 kinetics with two-substrate models: evidence that multiple substrates can simultaneously bind to cytochrome P450 active sites. Biochemistry 37:4137-4147. (Pubitemid 28166435)
    • (1998) Biochemistry , vol.37 , Issue.12 , pp. 4137-4147
    • Korzekwa, K.R.1    Krishnamachary, N.2    Shou, M.3    Ogai, A.4    Parise, R.A.5    Rettie, A.E.6    Gonzalez, F.J.7    Tracy, T.S.8
  • 8
    • 0037423299 scopus 로고    scopus 로고
    • Expression and characterization of recombinant human UDP- glucuronosyltransferases (UGTs): UGT1A9 is more resistant to detergent inhibition than the other UGTs and was purified as an active dimeric enzyme
    • DOI 10.1074/jbc.M206136200
    • Kurkela M, García-Horsman JA, Luukkanen L, Mörsky S, Taskinen J, Baumann M, Kostiainen R, Hirvonen J, and Finel M (2003) Expression and characterization of recombinant human UDP-glucuronosyltransferases (UGTs). UGT1A9 is more resistant to detergent inhibition than other UGTs and was purified as an active dimeric enzyme. J Biol Chem 278:3536-3544. (Pubitemid 36801076)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.6 , pp. 3536-3544
    • Kurkela, M.1    Garcia-Horsmant, J.A.2    Luukkanen, L.3    Morsky, S.4    Taskinen, J.5    Baumann, M.6    Kostiainen, R.7    Hirvonen, J.8    Finel, M.9
  • 9
    • 33847043537 scopus 로고    scopus 로고
    • Interactions with other human UDP-glucuronosyltransferases attenuate the consequences of the Y485D mutation on the activity and substrate affinity of UGT1A6
    • Kurkela M, Patana AS, Mackenzie PI, Court MH, Tate CG, Hirvonen J, Goldman A, and Finel M (2007) Interactions with other human UDP- glucuronosyltransferases attenuate the consequences of the Y485D mutation on the activity and substrate affinity of UGT1A6. Pharmacogenet Genomics 17:115-126.
    • (2007) Pharmacogenet Genomics , vol.17 , pp. 115-126
    • Kurkela, M.1    Patana, A.S.2    Mackenzie, P.I.3    Court, M.H.4    Tate, C.G.5    Hirvonen, J.6    Goldman, A.7    Finel, M.8
  • 10
    • 0033786733 scopus 로고    scopus 로고
    • The specificity of glucuronidation of entacapone and tolcapone by recombinant human UDP-glucuronosyltransferases
    • Lautala P, Ethell BT, Taskinen J, and Burchell B (2000) The specificity of glucuronidation of entacapone and tolcapone by recombinant human UDP-glucuronosyltransferases. Drug Metab Dispos 28:1385-1389.
    • (2000) Drug Metab Dispos , vol.28 , pp. 1385-1389
    • Lautala, P.1    Ethell, B.T.2    Taskinen, J.3    Burchell, B.4
  • 12
    • 0344178210 scopus 로고    scopus 로고
    • Enzyme-assisted synthesis and structural characterization of nitrocatechol glucuronides
    • DOI 10.1021/bc980064n
    • Luukkanen L, Kilpeläinen I, Kangas H, Ottoila P, Elovaara E, and Taskinen J (1999) Enzyme-assisted synthesis and structural characterization of nitrocatechol glucuronides. Bioconjug Chem 10:150-154. (Pubitemid 29062532)
    • (1999) Bioconjugate Chemistry , vol.10 , Issue.1 , pp. 150-154
    • Luukkanen, L.1    Kilpelainen, I.2    Kangas, H.3    Ottoila, P.4    Elovaara, E.5    Taskinen, J.6
  • 13
    • 18144406492 scopus 로고    scopus 로고
    • Kinetic characterization of the 1A subfamily of recombinant human UDP-glucuronosyltransferases
    • DOI 10.1124/dmd.105.004093
    • Luukkanen L, Taskinen J, Kurkela M, Kostiainen R, Hirvonen J, and Finel M (2005) Kinetic characterization of the 1A subfamily of recombinant human UDP-glucuronosyltransferases. Drug Metab Dispos 33:1017-1026. (Pubitemid 41002784)
    • (2005) Drug Metabolism and Disposition , vol.33 , Issue.7 , pp. 1017-1026
    • Luukkanen, L.1    Taskinen, J.2    Kurkela, M.3    Kostiainen, R.4    Hirvonen, J.5    Finel, M.6
  • 16
    • 0344820768 scopus 로고    scopus 로고
    • Lipid composition of Spodoptera frugiperda (Sf9) and Trichoplusia ni (Tn) insect cells used for baculovirus infection
    • DOI 10.1016/S0014-5793(98)01523-3, PII S0014579398015233
    • Marheineke K, Grünewald S, Christie W, and Reiländer H (1998) Lipid composition of Spodoptera frugiperda (Sf9) and Trichoplusia ni (Tn) insect cells used for baculovirus infection. FEBS Lett 441:49-52. (Pubitemid 29012370)
    • (1998) FEBS Letters , vol.441 , Issue.1 , pp. 49-52
    • Marheineke, K.1    Grunewald, S.2    Christie, W.3    Reilander, H.4
  • 17
    • 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
  • 18
    • 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
    • Miners JO, Mackenzie PI, and Knights KM (2010) 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 42:196-208.
    • (2010) Drug Metab Rev , vol.42 , pp. 196-208
    • Miners, J.O.1    Mackenzie, P.I.2    Knights, K.M.3
  • 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
    • Ohno S and Nakajin S (2009) 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 37:32-40.
    • (2009) Drug Metab Dispos , vol.37 , pp. 32-40
    • Ohno, S.1    Nakajin, S.2
  • 20
    • 15444378115 scopus 로고    scopus 로고
    • A historical overview of the heterologous expression of mammalian UDP-glucuronosyltransferase isoforms over the past twenty years
    • DOI 10.2174/1389200053586127
    • Radominska-Pandya A, Bratton S, and Little JM (2005) A historical overview of the heterologous expression of mammalian UDP-glucuronosyltransferase isoforms over the past twenty years. Curr Drug Metab 6:141-160. (Pubitemid 40394342)
    • (2005) Current Drug Metabolism , vol.6 , Issue.2 , pp. 141-160
    • Radominska-Pandya, A.1    Bratton, S.2    Little, J.M.3
  • 21
    • 77954896503 scopus 로고    scopus 로고
    • In vitro-in vivo extrapolation predicts drug-drug interactions arising from inhibition of codeine glucuronidation by dextropropoxyphene, fluconazole, ketoconazole, and methadone in humans
    • Raungrut P, Uchaipichat V, Elliot DJ, Janchawee B, Somogyi AA, and Miners JO (2010) In vitro-in vivo extrapolation predicts drug-drug interactions arising from inhibition of codeine glucuronidation by dextropropoxyphene, fluconazole, ketoconazole, and methadone in humans. J Pharmacol Exp Ther 334:609-618.
    • (2010) J Pharmacol Exp Ther , vol.334 , pp. 609-618
    • Raungrut, P.1    Uchaipichat, V.2    Elliot, D.J.3    Janchawee, B.4    Somogyi, A.A.5    Miners, J.O.6
  • 22
    • 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
    • DOI 10.1124/jpet.106.118216
    • Rowland A, Gaganis P, Elliot DJ, Mackenzie PI, Knights KM, and Miners JO (2007) 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 321:137-147. (Pubitemid 46456976)
    • (2007) Journal of Pharmacology and Experimental Therapeutics , vol.321 , Issue.1 , 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
  • 23
    • 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
    • DOI 10.1124/dmd.108.021105
    • Rowland A, Knights KM, Mackenzie PI, and Miners JO (2008) 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 36:1056-1062. (Pubitemid 351717462)
    • (2008) Drug Metabolism and Disposition , vol.36 , Issue.6 , pp. 1056-1062
    • Rowland, A.1    Knights, K.M.2    Mackenzie, P.I.3    Miners, J.O.4
  • 24
    • 33645045860 scopus 로고    scopus 로고
    • Modification of the ultrafiltration technique to overcome solubility and non-specific binding challenges associated with the measurement of plasma protein binding of corticosteroids
    • Taylor S and Harker A (2006) Modification of the ultrafiltration technique to overcome solubility and non-specific binding challenges associated with the measurement of plasma protein binding of corticosteroids. J Pharm Biomed Anal 41:299-303.
    • (2006) J Pharm Biomed Anal , vol.41 , pp. 299-303
    • Taylor, S.1    Harker, A.2
  • 25
    • 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 (2006) 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
  • 26
    • 75449095230 scopus 로고    scopus 로고
    • Ligand binding strategies of human serum albumin: How can the cargo be utilized?
    • Varshney A, Sen P, Ahmad E, Rehan M, Subbarao N, and Khan RH (2010) Ligand binding strategies of human serum albumin: how can the cargo be utilized? Chirality 22:77-87.
    • (2010) Chirality , vol.22 , pp. 77-87
    • Varshney, A.1    Sen, P.2    Ahmad, E.3    Rehan, M.4    Subbarao, N.5    Khan, R.H.6
  • 27
    • 79951921433 scopus 로고    scopus 로고
    • Effects of cell differentiation and assay conditions on the UDP-glucuronosyltransferase activity in Caco-2 cells
    • Zhang H, Tolonen A, Rousu T, Hirvonen J, and Finel M (2011) Effects of cell differentiation and assay conditions on the UDP-glucuronosyltransferase activity in Caco-2 cells. Drug Metab Dispos 39:456-464.
    • (2011) Drug Metab Dispos , vol.39 , pp. 456-464
    • Zhang, H.1    Tolonen, A.2    Rousu, T.3    Hirvonen, J.4    Finel, M.5


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