메뉴 건너뛰기




Volumn 61, Issue 1, 2010, Pages 76-84

Xenopus laevis oocytes expressing human P-glycoprotein: Probing trans- and cis-inhibitory effects on [3H]vinblastine and [3H]digoxin efflux

Author keywords

ABC transporter; Drug efflux; P glycoprotein; Xenopus laevis oocyte

Indexed keywords

ADENOSINE TRIPHOSPHATE; CIMETIDINE; DIGOXIN; DOXORUBICIN; GLYCOPROTEIN P; MULTIDRUG RESISTANCE PROTEIN 1; QUINIDINE; TRITIUM; VERAPAMIL; VINBLASTINE SULFATE;

EID: 72749119475     PISSN: 10436618     EISSN: 10961186     Source Type: Journal    
DOI: 10.1016/j.phrs.2009.07.002     Document Type: Article
Times cited : (11)

References (62)
  • 1
    • 0026621245 scopus 로고
    • ABC transporters: from microorganisms to man
    • Higgins C.F. ABC transporters: from microorganisms to man. Annu Rev Cell Biol 8 (1992) 67-113
    • (1992) Annu Rev Cell Biol , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 2
    • 0029954843 scopus 로고    scopus 로고
    • P-glycoprotein- a mediator of multidrug resistance in tumor cells
    • Germann U.A. P-glycoprotein- a mediator of multidrug resistance in tumor cells. Eur J Cancer 32A (1996) 927-944
    • (1996) Eur J Cancer , vol.32 A , pp. 927-944
    • Germann, U.A.1
  • 3
    • 38849159071 scopus 로고    scopus 로고
    • Pharmacokinetics of saquinavir after intravenous and oral dosing of saquinavir: hydroxybutenyl-cyclodextrin formulations
    • Buchanan C.M., Buchanan N.L., Edgar K.J., Little J.L., Ramsey M.G., Ruble K.M., et al. Pharmacokinetics of saquinavir after intravenous and oral dosing of saquinavir: hydroxybutenyl-cyclodextrin formulations. Biomacromolecules 9 (2008) 305-313
    • (2008) Biomacromolecules , vol.9 , pp. 305-313
    • Buchanan, C.M.1    Buchanan, N.L.2    Edgar, K.J.3    Little, J.L.4    Ramsey, M.G.5    Ruble, K.M.6
  • 4
    • 0033739725 scopus 로고    scopus 로고
    • Role of metabolic enzymes and efflux transporters in the absorption of drugs from the small intestine
    • Suzuki H., and Sugiyama Y. Role of metabolic enzymes and efflux transporters in the absorption of drugs from the small intestine. Eur J Pharm Sci 12 (2000) 3-12
    • (2000) Eur J Pharm Sci , vol.12 , pp. 3-12
    • Suzuki, H.1    Sugiyama, Y.2
  • 5
    • 0023033333 scopus 로고
    • Increased vinblastine binding to membrane vesicle from multidrug-resistant KB cells
    • Cornwell M.M., Gottesman M.M., and Pastan I.H. Increased vinblastine binding to membrane vesicle from multidrug-resistant KB cells. J Biol Chem 261 (1986) 7921-7928
    • (1986) J Biol Chem , vol.261 , pp. 7921-7928
    • Cornwell, M.M.1    Gottesman, M.M.2    Pastan, I.H.3
  • 6
    • 0007630205 scopus 로고
    • ATP-dependent transport of vinblastine in vesicles from human multidrug-resistant cells
    • Horio M., Gottesman M.M., and Pastan I. ATP-dependent transport of vinblastine in vesicles from human multidrug-resistant cells. Proc Natl Acad Sci USA 85 (1988) 3580-3584
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 3580-3584
    • Horio, M.1    Gottesman, M.M.2    Pastan, I.3
  • 8
    • 0026722467 scopus 로고
    • Expression of the human multidrug resistance cDNA in insect cells generates a high activity drug-stimulated membrane ATPase
    • Sarkadi B., Price E.M., Boucher R.C., Germann U.A., and Scarborough G.A. Expression of the human multidrug resistance cDNA in insect cells generates a high activity drug-stimulated membrane ATPase. J Biol Chem 267 (1992) 484-4858
    • (1992) J Biol Chem , vol.267 , pp. 484-4858
    • Sarkadi, B.1    Price, E.M.2    Boucher, R.C.3    Germann, U.A.4    Scarborough, G.A.5
  • 9
    • 33644691806 scopus 로고    scopus 로고
    • Comparison of species differences of P-glycoproteins in beagle dog, rhesus monkey, and human using ATPase activity assays
    • Xia C.Q., Xiao G., Liu N., Primprale S., Fox L., Patten C.J., et al. Comparison of species differences of P-glycoproteins in beagle dog, rhesus monkey, and human using ATPase activity assays. Mol Pharm 3 (2006) 78-86
    • (2006) Mol Pharm , vol.3 , pp. 78-86
    • Xia, C.Q.1    Xiao, G.2    Liu, N.3    Primprale, S.4    Fox, L.5    Patten, C.J.6
  • 10
    • 33845362976 scopus 로고    scopus 로고
    • Evaluation of human P-glycoprotein (MDR1/ABCB1) ATPase activity assay method by comparing with in vitro transport measurements: Michaelis-Menten kinetic analysis to estimate the affinity of P-glycoprotein to drugs
    • Shirasaka Y., Onishi Y., Sakurai A., Nakagawa H., Ishikawa T., and Yamashita S. Evaluation of human P-glycoprotein (MDR1/ABCB1) ATPase activity assay method by comparing with in vitro transport measurements: Michaelis-Menten kinetic analysis to estimate the affinity of P-glycoprotein to drugs. Biol Pharm Bull 29 (2006) 2465-2471
    • (2006) Biol Pharm Bull , vol.29 , pp. 2465-2471
    • Shirasaka, Y.1    Onishi, Y.2    Sakurai, A.3    Nakagawa, H.4    Ishikawa, T.5    Yamashita, S.6
  • 11
    • 33947359030 scopus 로고    scopus 로고
    • P-glycoprotein kinetics measured in plasma membrane vesicles and living cells
    • Aanismaa P., and Seelig A. P-glycoprotein kinetics measured in plasma membrane vesicles and living cells. Biochemistry 46 (2007) 3394-3404
    • (2007) Biochemistry , vol.46 , pp. 3394-3404
    • Aanismaa, P.1    Seelig, A.2
  • 12
    • 0026662530 scopus 로고
    • Partial purification and reconstitution of the human multidrug-resistance pump-characterization of the drug-stimulatable ATP hydrolysis
    • Ambudkar S.V., Lelong I.H., Zhang J.P., Cardarelli C.O., Gottesman M.M., and Pastan I. Partial purification and reconstitution of the human multidrug-resistance pump-characterization of the drug-stimulatable ATP hydrolysis. Proc Natl Acad Sci USA 89 (1992) 8472-8476
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8472-8476
    • Ambudkar, S.V.1    Lelong, I.H.2    Zhang, J.P.3    Cardarelli, C.O.4    Gottesman, M.M.5    Pastan, I.6
  • 14
    • 0027482461 scopus 로고
    • Functional reconstitution of drug transport and ATPase activity in proteoliposomes containing partially purified P-glycoprotein
    • Sharom F.J., Yu X., and Doige C.A. Functional reconstitution of drug transport and ATPase activity in proteoliposomes containing partially purified P-glycoprotein. J Biol Chem 268 (1993) 24197-24202
    • (1993) J Biol Chem , vol.268 , pp. 24197-24202
    • Sharom, F.J.1    Yu, X.2    Doige, C.A.3
  • 15
    • 0029061103 scopus 로고
    • Reconstitution of drug transport by purified P-glycoprotein
    • Shapiro A.B., and Ling V. Reconstitution of drug transport by purified P-glycoprotein. J Biol Chem 270 (1995) 16167-16175
    • (1995) J Biol Chem , vol.270 , pp. 16167-16175
    • Shapiro, A.B.1    Ling, V.2
  • 16
    • 0031581819 scopus 로고    scopus 로고
    • Effect of quercetin on Hoechst 33342 transport by purified and reconstituted P-glycoprotein
    • Shapiro A.B., and Ling V. Effect of quercetin on Hoechst 33342 transport by purified and reconstituted P-glycoprotein. Biochem Pharmacol 53 (1997) 587-596
    • (1997) Biochem Pharmacol , vol.53 , pp. 587-596
    • Shapiro, A.B.1    Ling, V.2
  • 17
    • 0035119989 scopus 로고    scopus 로고
    • In vitro substrate identification studies for P-glycoprotein-mediated transport: species difference and predictability of in vivo results
    • Yamazaki M., Neway W.E., Ohe T., Chen I., Rowe J.F., Hochman J.H., et al. In vitro substrate identification studies for P-glycoprotein-mediated transport: species difference and predictability of in vivo results. J Pharmacol Exp Ther 296 (2001) 723-735
    • (2001) J Pharmacol Exp Ther , vol.296 , pp. 723-735
    • Yamazaki, M.1    Neway, W.E.2    Ohe, T.3    Chen, I.4    Rowe, J.F.5    Hochman, J.H.6
  • 18
    • 0035668339 scopus 로고    scopus 로고
    • Comparative studies on in vitro methods for evaluating in vivo function of MDR1 P-glycoprotein
    • Adachi Y., Suzuki H., and Sugiyama Y. Comparative studies on in vitro methods for evaluating in vivo function of MDR1 P-glycoprotein. Pharm Res 18 (2001) 1660-1668
    • (2001) Pharm Res , vol.18 , pp. 1660-1668
    • Adachi, Y.1    Suzuki, H.2    Sugiyama, Y.3
  • 19
    • 0036293772 scopus 로고    scopus 로고
    • Are MDCK cells transfected with the human MDR1 gene a good model of the human intestinal mucosa?
    • Tang F., Horie K., and Borchardt R.T. Are MDCK cells transfected with the human MDR1 gene a good model of the human intestinal mucosa?. Pharm Res 19 (2002) 765-772
    • (2002) Pharm Res , vol.19 , pp. 765-772
    • Tang, F.1    Horie, K.2    Borchardt, R.T.3
  • 20
    • 27544483787 scopus 로고    scopus 로고
    • Functional assessment of multiple P-glycoprotein (P-gp) probe substrates: influence of cell line and modulator concentration on P-gp activity
    • Taub M.E., Podila L., Ely D., and Almeida I. Functional assessment of multiple P-glycoprotein (P-gp) probe substrates: influence of cell line and modulator concentration on P-gp activity. Drug Metab Dispos 33 (2005) 1679-1687
    • (2005) Drug Metab Dispos , vol.33 , pp. 1679-1687
    • Taub, M.E.1    Podila, L.2    Ely, D.3    Almeida, I.4
  • 21
    • 33745632043 scopus 로고    scopus 로고
    • Establishment and characterization of the transformants stably-expressing MDR1 derived from various animal species in LLC-PK1
    • Takeuchi T., Yoshitomi S., Higuchi T., Ikemoto K., Niwa S., Ebihara T., et al. Establishment and characterization of the transformants stably-expressing MDR1 derived from various animal species in LLC-PK1. Pharm Res 23 (2006) 1460-1472
    • (2006) Pharm Res , vol.23 , pp. 1460-1472
    • Takeuchi, T.1    Yoshitomi, S.2    Higuchi, T.3    Ikemoto, K.4    Niwa, S.5    Ebihara, T.6
  • 22
    • 18344364851 scopus 로고    scopus 로고
    • Application of three dimensional quantitative structure-activity relationships of P-glycoprotein inhibitors and substrates
    • Ekins S., Kim R.B., Leake B.F., Dantzig A.H., Schuetz E.G., Lan L.B., et al. Application of three dimensional quantitative structure-activity relationships of P-glycoprotein inhibitors and substrates. Mol Pharmacol 61 (2002) 974-981
    • (2002) Mol Pharmacol , vol.61 , pp. 974-981
    • Ekins, S.1    Kim, R.B.2    Leake, B.F.3    Dantzig, A.H.4    Schuetz, E.G.5    Lan, L.B.6
  • 23
    • 18344390872 scopus 로고    scopus 로고
    • Three dimensional quantitative structure-activity relationships of inhibitors of P-glycoprotein
    • Ekins S., Kim R.B., Leake B.F., Dantzig A.H., Schuetz E.G., Lan L.B., et al. Three dimensional quantitative structure-activity relationships of inhibitors of P-glycoprotein. Mol Pharmacol 61 (2002) 964-973
    • (2002) Mol Pharmacol , vol.61 , pp. 964-973
    • Ekins, S.1    Kim, R.B.2    Leake, B.F.3    Dantzig, A.H.4    Schuetz, E.G.5    Lan, L.B.6
  • 25
    • 0025991731 scopus 로고
    • Azidopine noncompetitively interacts with vinblastine and cyclosporine A binding to P-gluycoprotein in multidrug resistant cells
    • Tamai I., and Safa A.R. Azidopine noncompetitively interacts with vinblastine and cyclosporine A binding to P-gluycoprotein in multidrug resistant cells. J Biol Chem 266 (1991) 16796-16800
    • (1991) J Biol Chem , vol.266 , pp. 16796-16800
    • Tamai, I.1    Safa, A.R.2
  • 27
    • 0030782511 scopus 로고    scopus 로고
    • Positively cooperative sites for drug transport by P-glycoprotein with distinct drug specificities
    • Shapiro A.B., and Ling V. Positively cooperative sites for drug transport by P-glycoprotein with distinct drug specificities. Eur J Biochem 250 (1997) 130-137
    • (1997) Eur J Biochem , vol.250 , pp. 130-137
    • Shapiro, A.B.1    Ling, V.2
  • 28
    • 0033083015 scopus 로고    scopus 로고
    • Stimulation of P-glycoprotein-mediated drug transport by prazosin and progesterone-evidence for a third drug-binding site
    • Shapiro A.B., Fox K., Lam P., and Ling V. Stimulation of P-glycoprotein-mediated drug transport by prazosin and progesterone-evidence for a third drug-binding site. Eur J Biochem 259 (1999) 841-850
    • (1999) Eur J Biochem , vol.259 , pp. 841-850
    • Shapiro, A.B.1    Fox, K.2    Lam, P.3    Ling, V.4
  • 30
    • 0027218689 scopus 로고
    • Biochemistry of multidrug resistance mediated by the multidrug transporter
    • Gottesman M.M., and Pastan I. Biochemistry of multidrug resistance mediated by the multidrug transporter. Annu Rev Biochem 62 (1993) 385-427
    • (1993) Annu Rev Biochem , vol.62 , pp. 385-427
    • Gottesman, M.M.1    Pastan, I.2
  • 31
    • 0000245851 scopus 로고    scopus 로고
    • P-glycoprotein
    • Levy R.H., Thummel K.E., Trager W.F., Hansten P.D., and Eichelbaum M. (Eds), Lippincott Williams & Wilkins, Philadelphia [Chapter 11]
    • Silverman J.A. P-glycoprotein. In: Levy R.H., Thummel K.E., Trager W.F., Hansten P.D., and Eichelbaum M. (Eds). Metabolic Drug Interactions (2000), Lippincott Williams & Wilkins, Philadelphia 135-144 [Chapter 11]
    • (2000) Metabolic Drug Interactions , pp. 135-144
    • Silverman, J.A.1
  • 32
    • 34250822863 scopus 로고    scopus 로고
    • Mechanism of inhibition of P-glycoprotein mediated efflux by vitamin E TPGS: influence on ATPase activity and membrane fluidity
    • Collnot E.-M., Baldes C., Wempe M.F., Kappl R., Hüttermann J., Hyatt J.A., et al. Mechanism of inhibition of P-glycoprotein mediated efflux by vitamin E TPGS: influence on ATPase activity and membrane fluidity. Mol Pharm 4 (2007) 465-474
    • (2007) Mol Pharm , vol.4 , pp. 465-474
    • Collnot, E.-M.1    Baldes, C.2    Wempe, M.F.3    Kappl, R.4    Hüttermann, J.5    Hyatt, J.A.6
  • 33
    • 0025193531 scopus 로고
    • Photosensitized labeling of a functional multidrug transporter in living drug-resistant tumor cells
    • Raviv Y., Pollard H.B., Bruggemann E.P., Pastan I., and Gottesman M.M. Photosensitized labeling of a functional multidrug transporter in living drug-resistant tumor cells. J Biol Chem 265 (1990) 3975-3980
    • (1990) J Biol Chem , vol.265 , pp. 3975-3980
    • Raviv, Y.1    Pollard, H.B.2    Bruggemann, E.P.3    Pastan, I.4    Gottesman, M.M.5
  • 34
    • 0027432409 scopus 로고
    • Fluorescent cellular indicators are extruded by the multidrug resistance protein
    • Homolya L., Hollo Z., Germann U.A., Pastan I., Gottesman M.M., and Sarkadi B. Fluorescent cellular indicators are extruded by the multidrug resistance protein. J Biol Chem 268 (1993) 21493-21496
    • (1993) J Biol Chem , vol.268 , pp. 21493-21496
    • Homolya, L.1    Hollo, Z.2    Germann, U.A.3    Pastan, I.4    Gottesman, M.M.5    Sarkadi, B.6
  • 35
    • 0030822996 scopus 로고    scopus 로고
    • P-glycoprotein-mediated Hoechst 33342 transport out of the lipid bilayer
    • Shapiro A.B., Corder A.B., and Ling V. P-glycoprotein-mediated Hoechst 33342 transport out of the lipid bilayer. Eur J Biochem 250 (1997) 115-121
    • (1997) Eur J Biochem , vol.250 , pp. 115-121
    • Shapiro, A.B.1    Corder, A.B.2    Ling, V.3
  • 36
    • 0028342805 scopus 로고
    • Unidirectional fluxes of rhodamine 123 in multidrug-resistant cells: evidence against drug extrusion from plasma membrane
    • Altenberg G.A., Vanoye C.G., Horton J.K., and Reuss L. Unidirectional fluxes of rhodamine 123 in multidrug-resistant cells: evidence against drug extrusion from plasma membrane. Proc Natl Acad Sci USA 91 (1994) 4654-4657
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4654-4657
    • Altenberg, G.A.1    Vanoye, C.G.2    Horton, J.K.3    Reuss, L.4
  • 37
    • 0034753085 scopus 로고    scopus 로고
    • Mercapturic acids (N-acetylcysteine S-conjugates) as endogenous substrates for the renal organic anion transporter-1
    • Pombrio J.M., Giangreco A., Li L., Wempe M.F., Anders M.W., Sweet D.H., et al. Mercapturic acids (N-acetylcysteine S-conjugates) as endogenous substrates for the renal organic anion transporter-1. Mol Pharm 60 (2001) 1091-1099
    • (2001) Mol Pharm , vol.60 , pp. 1091-1099
    • Pombrio, J.M.1    Giangreco, A.2    Li, L.3    Wempe, M.F.4    Anders, M.W.5    Sweet, D.H.6
  • 38
    • 33845887252 scopus 로고    scopus 로고
    • Concentration-dependent mode of interaction of angiotensin II receptor blockers with uric acid transporter
    • Iwanaga T., Sato M., Maeda T., Ogihara T., and Tamai I. Concentration-dependent mode of interaction of angiotensin II receptor blockers with uric acid transporter. J Pharmacol Exp Ther 320 (2007) 211-217
    • (2007) J Pharmacol Exp Ther , vol.320 , pp. 211-217
    • Iwanaga, T.1    Sato, M.2    Maeda, T.3    Ogihara, T.4    Tamai, I.5
  • 39
    • 0031304363 scopus 로고    scopus 로고
    • Localized sampling of cytoplasm from Xenopus oocytes for capillary electrophoresis
    • Luzzi V., Lee C.L., and Allbritton N.L. Localized sampling of cytoplasm from Xenopus oocytes for capillary electrophoresis. Anal Chem 69 (1997) 4761-4767
    • (1997) Anal Chem , vol.69 , pp. 4761-4767
    • Luzzi, V.1    Lee, C.L.2    Allbritton, N.L.3
  • 40
    • 0033214147 scopus 로고    scopus 로고
    • Xenopus oocyte maturation: new lessons from a good egg
    • Ferrell Jr. J.E. Xenopus oocyte maturation: new lessons from a good egg. Bioessays 21 (1999) 833-842
    • (1999) Bioessays , vol.21 , pp. 833-842
    • Ferrell Jr., J.E.1
  • 41
    • 3242785620 scopus 로고    scopus 로고
    • Importance of P-glycoprotein at blood-tissue barriers
    • Fromm M.F. Importance of P-glycoprotein at blood-tissue barriers. Trends Pharmacol Sci 25 (2004) 423-429
    • (2004) Trends Pharmacol Sci , vol.25 , pp. 423-429
    • Fromm, M.F.1
  • 42
    • 0031900997 scopus 로고    scopus 로고
    • Role of P-glycoprotein as a secretory mechanism in quinidine absorption from rat small intestine
    • Emi Y., Tsunashima D., Ogawara K.I., Higaki K., and Kimura T. Role of P-glycoprotein as a secretory mechanism in quinidine absorption from rat small intestine. J Pharm Sci 87 (1998) 295-299
    • (1998) J Pharm Sci , vol.87 , pp. 295-299
    • Emi, Y.1    Tsunashima, D.2    Ogawara, K.I.3    Higaki, K.4    Kimura, T.5
  • 43
    • 0344665555 scopus 로고    scopus 로고
    • ABC of oral bioavailablility: transporters as gatekeepers in the gut
    • Dietrich C.G., Geier A., and Oude Elferink R.P.J. ABC of oral bioavailablility: transporters as gatekeepers in the gut. Gut 52 (2003) 1788-1795
    • (2003) Gut , vol.52 , pp. 1788-1795
    • Dietrich, C.G.1    Geier, A.2    Oude Elferink, R.P.J.3
  • 44
    • 33745831231 scopus 로고    scopus 로고
    • Structure, function, expression, genomic organization, and single nucleotide polymorphisms of human ABCB1 (MDR1), ABCC (MRP), and ABCG2 (BCRP) efflux transporters
    • Choudhuri S., and Klaassen C.D. Structure, function, expression, genomic organization, and single nucleotide polymorphisms of human ABCB1 (MDR1), ABCC (MRP), and ABCG2 (BCRP) efflux transporters. Int J Toxicol 25 (2006) 231-259
    • (2006) Int J Toxicol , vol.25 , pp. 231-259
    • Choudhuri, S.1    Klaassen, C.D.2
  • 45
    • 61449188212 scopus 로고    scopus 로고
    • Inhibiting efflux with novel non-ionic surfactants: rational design based on vitamin E TPGS
    • Wempe M.F., Wright C., Little J.L., Lightner J.W., Large S.E., Caflisch G.B., et al. Inhibiting efflux with novel non-ionic surfactants: rational design based on vitamin E TPGS. Int J Pharm 370 (2009) 93-102
    • (2009) Int J Pharm , vol.370 , pp. 93-102
    • Wempe, M.F.1    Wright, C.2    Little, J.L.3    Lightner, J.W.4    Large, S.E.5    Caflisch, G.B.6
  • 48
    • 0033514320 scopus 로고    scopus 로고
    • Inhibition of P-glycoprotein-mediated drug transport: A unifying mechanism to explain the interaction between digoxin and quinidine
    • Fromm M.F., Kim R.B., Stein C.M., Wilkinson G.R., and Roden D.M. Inhibition of P-glycoprotein-mediated drug transport: A unifying mechanism to explain the interaction between digoxin and quinidine. Circulation 99 (1999) 552-557
    • (1999) Circulation , vol.99 , pp. 552-557
    • Fromm, M.F.1    Kim, R.B.2    Stein, C.M.3    Wilkinson, G.R.4    Roden, D.M.5
  • 50
    • 0033862088 scopus 로고    scopus 로고
    • Specificity of doxorubicin versus rhodamine-123 in assessing P-glycoprotein functionality in the LLC-PK1:MDR1 and Caco-2 cell lines
    • van der Sandt I.C., Blom-Roosemalen M.C., de Boer A.G., and Breimer D.D. Specificity of doxorubicin versus rhodamine-123 in assessing P-glycoprotein functionality in the LLC-PK1:MDR1 and Caco-2 cell lines. Eur J Pharm Sci 11 (2000) 207-214
    • (2000) Eur J Pharm Sci , vol.11 , pp. 207-214
    • van der Sandt, I.C.1    Blom-Roosemalen, M.C.2    de Boer, A.G.3    Breimer, D.D.4
  • 53
    • 0027180795 scopus 로고
    • Drug absorption limited by P-glycoprotein-mediated secretory drug transport in human intestinal epithelial Caco-2 cell layer
    • Hunter J., Hirst B.H., and Simmons N.L. Drug absorption limited by P-glycoprotein-mediated secretory drug transport in human intestinal epithelial Caco-2 cell layer. Pharm Res 10 (1993) 743-749
    • (1993) Pharm Res , vol.10 , pp. 743-749
    • Hunter, J.1    Hirst, B.H.2    Simmons, N.L.3
  • 54
    • 0030963896 scopus 로고    scopus 로고
    • Evidence for diminished functional expression of intestinal transporters in Caco-2 cell monolayers at high passages
    • Yu H., Cook T.J., and Sink P.J. Evidence for diminished functional expression of intestinal transporters in Caco-2 cell monolayers at high passages. Pharm Res 14 (1997) 757-762
    • (1997) Pharm Res , vol.14 , pp. 757-762
    • Yu, H.1    Cook, T.J.2    Sink, P.J.3
  • 55
    • 0034811602 scopus 로고    scopus 로고
    • Correlation of gene expression of ten drug efflux proteins of the atp-binding cassette transporter family in normal human jejunum and in human intestinal epithelial Caco-2 cell monolayers
    • Taipalensuu J., Törnblom H., Lindberg G., Einarsson C., Sjöqvist F., Melhus H., et al. Correlation of gene expression of ten drug efflux proteins of the atp-binding cassette transporter family in normal human jejunum and in human intestinal epithelial Caco-2 cell monolayers. J Pharmacol Exp Ther 299 (2001) 164-170
    • (2001) J Pharmacol Exp Ther , vol.299 , pp. 164-170
    • Taipalensuu, J.1    Törnblom, H.2    Lindberg, G.3    Einarsson, C.4    Sjöqvist, F.5    Melhus, H.6
  • 56
    • 0036805724 scopus 로고    scopus 로고
    • Comparison of human duodenum and Caco-2 gene expression profiles for 12,000 gene sequences tags and correlation with permeability of 26 drugs
    • Sun D., Lennernas H., Welage L.S., Barnett J.L., Landowski C.P., Foster D., et al. Comparison of human duodenum and Caco-2 gene expression profiles for 12,000 gene sequences tags and correlation with permeability of 26 drugs. Pharm Res 19 (2002) 1400-1416
    • (2002) Pharm Res , vol.19 , pp. 1400-1416
    • Sun, D.1    Lennernas, H.2    Welage, L.S.3    Barnett, J.L.4    Landowski, C.P.5    Foster, D.6
  • 59
    • 14644425991 scopus 로고    scopus 로고
    • Do drug substrates enter the common drug-binding pocket of P-glycoprotein through "gates"?
    • Loo T.P., and Clarke D.M. Do drug substrates enter the common drug-binding pocket of P-glycoprotein through "gates"?. Biochem Biophys Res Commun 329 (2005) 419-422
    • (2005) Biochem Biophys Res Commun , vol.329 , pp. 419-422
    • Loo, T.P.1    Clarke, D.M.2
  • 60
    • 18144419703 scopus 로고    scopus 로고
    • Liposome-encapsulated vincristine, vinblastine and vinorelbine: a comparative study of drug loading and retention
    • Zhigaltsev I.V., Maurer N., Akhong Q.-F., Leone R., Leng E., Wang J., et al. Liposome-encapsulated vincristine, vinblastine and vinorelbine: a comparative study of drug loading and retention. J Cont Rel 104 (2005) 103-111
    • (2005) J Cont Rel , vol.104 , pp. 103-111
    • Zhigaltsev, I.V.1    Maurer, N.2    Akhong, Q.-F.3    Leone, R.4    Leng, E.5    Wang, J.6
  • 61
    • 40549137751 scopus 로고    scopus 로고
    • A comparison of theoretical methods of calculation of partition coefficients for selected drugs
    • Pyka A., Babuśka M., and Zachariasz M. A comparison of theoretical methods of calculation of partition coefficients for selected drugs. Acta Pol Pharm 63 (2006) 159-167
    • (2006) Acta Pol Pharm , vol.63 , pp. 159-167
    • Pyka, A.1    Babuśka, M.2    Zachariasz, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.