메뉴 건너뛰기




Volumn 131, Issue 2, 2013, Pages 502-511

Interaction of digitalis-like compounds with P-glycoprotein

Author keywords

Baculovirus; Digitalis like compounds; Mutagenesis; P glycoprotein; Vesicle assay

Indexed keywords

ALANINE; CYMARIN; DIGITALIS LIKE FACTOR; DIGITOXIN; DIGOXIN; HYDROXYL GROUP; ISOLEUCINE; LEUCINE; MULTIDRUG RESISTANCE PROTEIN; PERUVOSIDE; PHENYLALANINE; PROSCILLARIDIN; QUINIDINE DERIVATIVE; STROPHANTHIDIN; THREONINE; VALINE;

EID: 84873821809     PISSN: 10966080     EISSN: 10960929     Source Type: Journal    
DOI: 10.1093/toxsci/kfs307     Document Type: Article
Times cited : (23)

References (41)
  • 1
    • 0034127539 scopus 로고    scopus 로고
    • Digoxin level and clinical manifestations as determinants in the diagnosis of digoxin toxicity
    • Abad-Santos, F., Carcas, A. J., Ibanez, C., and Frias, J. (2000). Digoxin level and clinical manifestations as determinants in the diagnosis of digoxin toxicity. Ther. Drug Monit. 22, 163-168.
    • (2000) Ther. Drug Monit. , vol.22 , pp. 163-168
    • Abad-Santos, F.1    Carcas, A.J.2    Ibanez, C.3    Frias, J.4
  • 3
    • 0020614706 scopus 로고
    • Interaction between digoxin and calcium antagonists and antiarrhythmic drugs
    • Belz, G. G., Doering, W., Munkes, R., and Matthews, J. (1983). Interaction between digoxin and calcium antagonists and antiarrhythmic drugs. Clin. Pharmacol. Ther. 33, 410-417.
    • (1983) Clin. Pharmacol. Ther. , vol.33 , pp. 410-417
    • Belz, G.G.1    Doering, W.2    Munkes, R.3    Matthews, J.4
  • 4
    • 0033678688 scopus 로고    scopus 로고
    • Atorvastatin coadministration may increase digoxin concentrations by inhibition of intestinal P-glycoproteinmediated secretion
    • Boyd, R. A., Stern, R. H., Stewart, B. H., Wu, X., Reyner, E. L., Zegarac, E. A., Randinitis, E. J., and Whitfield, L. (2000). Atorvastatin coadministration may increase digoxin concentrations by inhibition of intestinal P-glycoproteinmediated secretion. J. Clin. Pharmacol. 40, 91-98.
    • (2000) J. Clin. Pharmacol. , vol.40 , pp. 91-98
    • Boyd, R.A.1    Stern, R.H.2    Stewart, B.H.3    Wu, X.4    Reyner, E.L.5    Zegarac, E.A.6    Randinitis, E.J.7    Whitfield, L.8
  • 5
    • 0029997940 scopus 로고    scopus 로고
    • Transport and epithelial secretion of the cardiac glycoside, digoxin, by human intestinal epithelial (Caco-2) cells
    • Cavet, M. E., West, M., and Simmons, N. L. (1996). Transport and epithelial secretion of the cardiac glycoside, digoxin, by human intestinal epithelial (Caco-2) cells. Br. J. Pharmacol. 118, 1389-1396.
    • (1996) Br. J. Pharmacol. , vol.118 , pp. 1389-1396
    • Cavet, M.E.1    West, M.2    Simmons, N.L.3
  • 6
    • 0027102401 scopus 로고
    • The MDR1 gene product, P-glycoprotein, mediates the transport of the cardiac glycoside, digoxin
    • de Lannoy, I. A., and Silverman, M. (1992). The MDR1 gene product, P-glycoprotein, mediates the transport of the cardiac glycoside, digoxin. Biochem. Biophys. Res. Commun. 189, 551-557.
    • (1992) Biochem. Biophys. Res. Commun. , vol.189 , pp. 551-557
    • de Lannoy, I.A.1    Silverman, M.2
  • 7
    • 52949106057 scopus 로고    scopus 로고
    • Functional role of arginine 375 in transmembrane helix 6 of multidrug resistance protein 4 (MRP4/ABCC4)
    • El-Sheikh, A. A., van den Heuvel, J. J., Krieger, E., Russel, F. G., and Koenderink, J. B. (2008). Functional role of arginine 375 in transmembrane helix 6 of multidrug resistance protein 4 (MRP4/ABCC4). Mol. Pharmacol. 74, 964-971.
    • (2008) Mol. Pharmacol. , vol.74 , pp. 964-971
    • El-Sheikh, A.A.1    van den Heuvel, J.J.2    Krieger, E.3    Russel, F.G.4    Koenderink, J.B.5
  • 8
    • 4243091738 scopus 로고    scopus 로고
    • Association between the number of coadministered P-glycoprotein inhibitors and serum digoxin levels in patients on therapeutic drug monitoring
    • Englund, G., Hallberg, P., Artursson, P., Michaelsson, K., and Melhus, H. (2004). Association between the number of coadministered P-glycoprotein inhibitors and serum digoxin levels in patients on therapeutic drug monitoring. BMC Med. 2, 8.
    • (2004) BMC Med , vol.2 , pp. 8
    • Englund, G.1    Hallberg, P.2    Artursson, P.3    Michaelsson, K.4    Melhus, H.5
  • 11
    • 0034724324 scopus 로고    scopus 로고
    • Functional polymorphisms of the human multidrug-resistance gene: Multiple sequence variations and correlation of one allele with P-glycoprotein expression and activity in vivo
    • Hoffmeyer, S., Burk, O., von Richter, O., Arnold, H. P., Brockmoller, J., Johne, A., Cascorbi, I., Gerloff, T., Roots, I., and Eichelbaum, M., et al. (2000). Functional polymorphisms of the human multidrug-resistance gene: Multiple sequence variations and correlation of one allele with P-glycoprotein expression and activity in vivo. Proc. Natl. Acad. Sci. U.S.A. 97, 3473-3478.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 3473-3478
    • Hoffmeyer, S.1    Burk, O.2    von Richter, O.3    Arnold, H.P.4    Brockmoller, J.5    Johne, A.6    Cascorbi, I.7    Gerloff, T.8    Roots, I.9    Eichelbaum, M.10
  • 12
    • 0036965593 scopus 로고    scopus 로고
    • Stereoselective transport of hydrophilic quaternary drugs by human MDR1 and rat Mdr1b P-glycoproteins
    • Hooiveld, G. J., Heegsma, J., van Montfoort, J. E., Jansen, P. L., Meijer, D. K., and Muller, M. (2002). Stereoselective transport of hydrophilic quaternary drugs by human MDR1 and rat Mdr1b P-glycoproteins. Br. J. Pharmacol. 135, 1685-1694.
    • (2002) Br. J. Pharmacol. , vol.135 , pp. 1685-1694
    • Hooiveld, G.J.1    Heegsma, J.2    van Montfoort, J.E.3    Jansen, P.L.4    Meijer, D.K.5    Muller, M.6
  • 14
    • 72749119475 scopus 로고    scopus 로고
    • Xenopus laevis oocytes expressing human P-glycoprotein: Probing trans- and cis-inhibitory effects on [3H]vinblastine and [3H]digoxin efflux
    • Jutabha, P., Wempe, M. F., Anzai, N., Otomo, J., Kadota, T., and Endou, H. (2010). Xenopus laevis oocytes expressing human P-glycoprotein: Probing trans- and cis-inhibitory effects on [3H]vinblastine and [3H]digoxin efflux. Pharmacol. Res. 61, 76-84.
    • (2010) Pharmacol. Res. , vol.61 , pp. 76-84
    • Jutabha, P.1    Wempe, M.F.2    Anzai, N.3    Otomo, J.4    Kadota, T.5    Endou, H.6
  • 15
    • 34047185923 scopus 로고    scopus 로고
    • Impact of ABCB1 (MDR1) gene polymorphism and P-glycoprotein inhibitors on digoxin serum concentration in congestive heart failure patients
    • Kurzawski, M., Bartnicka, L., Florczak, M., Gornik, W., and Drozdzik, M. (2007). Impact of ABCB1 (MDR1) gene polymorphism and P-glycoprotein inhibitors on digoxin serum concentration in congestive heart failure patients. Pharmacol. Rep. 59, 107-111.
    • (2007) Pharmacol. Rep. , vol.59 , pp. 107-111
    • Kurzawski, M.1    Bartnicka, L.2    Florczak, M.3    Gornik, W.4    Drozdzik, M.5
  • 16
    • 77951265890 scopus 로고    scopus 로고
    • P-glycoprotein related drug interactions: Clinical importance and a consideration of disease states
    • Lee, C. A., Cook, J. A., Reyner, E. L., and Smith, D. A. (2010). P-glycoprotein related drug interactions: Clinical importance and a consideration of disease states. Expert Opin. Drug Metab. Toxicol. 6, 603-619.
    • (2010) Expert Opin. Drug Metab. Toxicol. , vol.6 , pp. 603-619
    • Lee, C.A.1    Cook, J.A.2    Reyner, E.L.3    Smith, D.A.4
  • 17
    • 32044453808 scopus 로고    scopus 로고
    • Recent progress in understanding the mechanism of P-glycoprotein-mediated drug efflux
    • Loo, T. W., and Clarke, D. M. (2005). Recent progress in understanding the mechanism of P-glycoprotein-mediated drug efflux. J. Membr. Biol. 206, 173-185.
    • (2005) J. Membr. Biol. , vol.206 , pp. 173-185
    • Loo, T.W.1    Clarke, D.M.2
  • 18
    • 33745008903 scopus 로고    scopus 로고
    • Transmembrane segment 1 of human P-glycoprotein contributes to the drug-binding pocket
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2006a). Transmembrane segment 1 of human P-glycoprotein contributes to the drug-binding pocket. Biochem. J. 396, 537-545.
    • (2006) Biochem. J. , vol.396 , pp. 537-545
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 19
    • 33749985062 scopus 로고    scopus 로고
    • Transmembrane segment 7 of human P-glycoprotein forms part of the drug-binding pocket
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2006b). Transmembrane segment 7 of human P-glycoprotein forms part of the drug-binding pocket. Biochem. J. 399, 351-359.
    • (2006) Biochem. J. , vol.399 , pp. 351-359
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 20
    • 36148958644 scopus 로고    scopus 로고
    • Suppressor mutations in the transmembrane segments of P-glycoprotein promote maturation of processing mutants and disrupt a subset of drug-binding sites
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2007). Suppressor mutations in the transmembrane segments of P-glycoprotein promote maturation of processing mutants and disrupt a subset of drug-binding sites. J. Biol. Chem. 282, 32043-32052.
    • (2007) J. Biol. Chem. , vol.282 , pp. 32043-32052
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 21
    • 57649134969 scopus 로고    scopus 로고
    • Processing mutations disrupt interactions between the nucleotide binding and transmembrane domains of P-glycoprotein and the cystic fibrosis transmembrane conductance regulator (CFTR)
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2008). Processing mutations disrupt interactions between the nucleotide binding and transmembrane domains of P-glycoprotein and the cystic fibrosis transmembrane conductance regulator (CFTR). J. Biol. Chem. 283, 28190-28197.
    • (2008) J. Biol. Chem. , vol.283 , pp. 28190-28197
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 22
    • 69949167524 scopus 로고    scopus 로고
    • Identification of residues in the drug translocation pathway of the human multidrug resistance P-glycoprotein by arginine mutagenesis
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2009). Identification of residues in the drug translocation pathway of the human multidrug resistance P-glycoprotein by arginine mutagenesis. J. Biol. Chem. 284, 24074-24087.
    • (2009) J. Biol. Chem. , vol.284 , pp. 24074-24087
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 23
    • 0029909604 scopus 로고    scopus 로고
    • Inhibition of oxidative cross-linking between engineered cysteine residues at positions 332 in predicted transmembrane segments ™ 6 and 975 in predicted TM12 of human P-glycoprotein by drug substrates
    • Loo, T. W., and Clarke, D. M. (1996). Inhibition of oxidative cross-linking between engineered cysteine residues at positions 332 in predicted transmembrane segments ™ 6 and 975 in predicted TM12 of human P-glycoprotein by drug substrates. J. Biol. Chem. 271, 27482-27487.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27482-27487
    • Loo, T.W.1    Clarke, D.M.2
  • 24
    • 0032700184 scopus 로고    scopus 로고
    • Determining the structure and mechanism of the human multidrug resistance P-glycoprotein using cysteine-scanning mutagenesis and thiol-modification techniques
    • Loo, T. W., and Clarke, D. M. (1999a). Determining the structure and mechanism of the human multidrug resistance P-glycoprotein using cysteine-scanning mutagenesis and thiol-modification techniques. Biochim. Biophys. Acta 1461, 315-325.
    • (1999) Biochim. Biophys. Acta , vol.1461 , pp. 315-325
    • Loo, T.W.1    Clarke, D.M.2
  • 25
    • 0033544851 scopus 로고    scopus 로고
    • Identification of residues in the drugbinding domain of human P-glycoprotein. Analysis of transmembrane segment 11 by cysteine-scanning mutagenesis and inhibition by dibromobimane
    • Loo, T. W., and Clarke, D. M. (1999b). Identification of residues in the drugbinding domain of human P-glycoprotein. Analysis of transmembrane segment 11 by cysteine-scanning mutagenesis and inhibition by dibromobimane. J. Biol. Chem. 274, 35388-35392.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35388-35392
    • Loo, T.W.1    Clarke, D.M.2
  • 26
    • 0037113961 scopus 로고    scopus 로고
    • Location of the rhodamine-binding site in the human multidrug resistance P-glycoprotein
    • Loo, T. W., and Clarke, D. M. (2002a). Location of the rhodamine-binding site in the human multidrug resistance P-glycoprotein. J. Biol. Chem. 277, 44332-44338.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44332-44338
    • Loo, T.W.1    Clarke, D.M.2
  • 27
    • 0037133616 scopus 로고    scopus 로고
    • Vanadate trapping of nucleotide at the ATPbinding sites of human multidrug resistance P-glycoprotein exposes different residues to the drug-binding site
    • Loo, T. W., and Clarke, D. M. (2002b). Vanadate trapping of nucleotide at the ATPbinding sites of human multidrug resistance P-glycoprotein exposes different residues to the drug-binding site. Proc. Natl. Acad. Sci. U.S.A. 99, 3511-3516.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 3511-3516
    • Loo, T.W.1    Clarke, D.M.2
  • 28
    • 34547754022 scopus 로고    scopus 로고
    • Digitoxin as an anticancer agent with selectivity for cancer cells: Possible mechanisms involved
    • Lopez-Lazaro, M. (2007). Digitoxin as an anticancer agent with selectivity for cancer cells: Possible mechanisms involved. Expert Opin. Ther. Targets 11, 1043-1053.
    • (2007) Expert Opin. Ther. Targets , vol.11 , pp. 1043-1053
    • Lopez-Lazaro, M.1
  • 29
    • 0037222807 scopus 로고    scopus 로고
    • Evidence for a non-MDR1 component in digoxin secretion by human intestinal Caco-2 epithelial layers
    • Lowes, S., Cavet, M. E., and Simmons, N. L. (2003). Evidence for a non-MDR1 component in digoxin secretion by human intestinal Caco-2 epithelial layers. Eur. J. Pharmacol. 458, 49-56.
    • (2003) Eur. J. Pharmacol. , vol.458 , pp. 49-56
    • Lowes, S.1    Cavet, M.E.2    Simmons, N.L.3
  • 31
    • 70349512492 scopus 로고    scopus 로고
    • Binding site of ABC transporter homology models confirmed by ABCB1 crystal structure
    • Ravna, A. W., Sylte, I., and Sager, G. (2009). Binding site of ABC transporter homology models confirmed by ABCB1 crystal structure. Theor. Biol. Med. Model. 6, 20.
    • (2009) Theor. Biol. Med. Model. , vol.6 , pp. 20
    • Ravna, A.W.1    Sylte, I.2    Sager, G.3
  • 33
    • 0028914111 scopus 로고
    • Characterization and functional reconstitution of the multidrug transporter
    • Sharom, F. J. (1995). Characterization and functional reconstitution of the multidrug transporter. J. Bioenerg. Biomembr. 27, 15-22.
    • (1995) J. Bioenerg. Biomembr. , vol.27 , pp. 15-22
    • Sharom, F.J.1
  • 34
    • 79955544324 scopus 로고    scopus 로고
    • In vitro P-glycoprotein interactions and steady-state pharmacokinetic interactions between tolvaptan and digoxin in healthy subjects
    • Shoaf, S. E., Ohzone, Y., Ninomiya, S. I., Furukawa, M., Bricmont, P., Kashiyama, E., and Mallikaarjun, S. (2011). In vitro P-glycoprotein interactions and steady-state pharmacokinetic interactions between tolvaptan and digoxin in healthy subjects. J. Clin. Pharmacol. 51, 761-769.
    • (2011) J. Clin. Pharmacol. , vol.51 , pp. 761-769
    • Shoaf, S.E.1    Ohzone, Y.2    Ninomiya, S.I.3    Furukawa, M.4    Bricmont, P.5    Kashiyama, E.6    Mallikaarjun, S.7
  • 35
    • 84855998504 scopus 로고    scopus 로고
    • Use of baculovirus BacMam vectors for expression of ABC drug transporters in mammalian cells
    • Shukla, S., Schwartz, C., Kapoor, K., Kouanda A., and Ambudkar, S. A. (2012). Use of baculovirus BacMam vectors for expression of ABC drug transporters in mammalian cells. Drug Metab. Dispos. 40, 304-312.
    • (2012) Drug Metab. Dispos. , vol.40 , pp. 304-312
    • Shukla, S.1    Schwartz, C.2    Kapoor, K.3    Kouanda, A.4    Ambudkar, S.A.5
  • 36
    • 11244309507 scopus 로고    scopus 로고
    • The elementary mass action rate constants of P-gp transport for a confluent monolayer of MDCKII-hMDR1 cells
    • Tran, T. T., Mittal, A., Aldinger, T., Polli, J. W., Ayrton, A., and Bentz, J. (2005). The elementary mass action rate constants of P-gp transport for a confluent monolayer of MDCKII-hMDR1 cells. Biophys. J. 88, 715-738.
    • (2005) Biophys. J. , vol.88 , pp. 715-738
    • Tran, T.T.1    Mittal, A.2    Aldinger, T.3    Polli, J.W.4    Ayrton, A.5    Bentz, J.6
  • 37
    • 0032848316 scopus 로고    scopus 로고
    • P-glycoprotein system as a determinant of drug interactions: The case of digoxin-verapamil
    • Verschraagen, M., Koks, C. H., Schellens, J. H., and Beijnen, J. H. (1999). P-glycoprotein system as a determinant of drug interactions: The case of digoxin-verapamil. Pharmacol. Res. 40, 301-306.
    • (1999) Pharmacol. Res. , vol.40 , pp. 301-306
    • Verschraagen, M.1    Koks, C.H.2    Schellens, J.H.3    Beijnen, J.H.4
  • 40
    • 79959482544 scopus 로고    scopus 로고
    • Cannabinoid type 1 receptor antagonists modulate transport activity of multidrug resistance-associated proteins MRP1, MRP2, MRP3, and MRP4
    • Wittgen, H. G., van den Heuvel, J. J., van den Broek, P. H., Dinter-Heidorn, H., Koenderink, J. B., and Russel, F. G. (2011). Cannabinoid type 1 receptor antagonists modulate transport activity of multidrug resistance-associated proteins MRP1, MRP2, MRP3, and MRP4. Drug Metab. Dispos. 39, 1294-1302.
    • (2011) Drug Metab. Dispos. , vol.39 , pp. 1294-1302
    • Wittgen, H.G.1    van den Heuvel, J.J.2    van den Broek, P.H.3    Dinter-Heidorn, H.4    Koenderink, J.B.5    Russel, F.G.6
  • 41
    • 0031980141 scopus 로고    scopus 로고
    • A model for the prediction of digoxin-drug interactions at the renal tubular cell level
    • Woodland, C., Ito, S., and Koren, G. (1998). A model for the prediction of digoxin-drug interactions at the renal tubular cell level. Ther. Drug Monit. 20, 134-138.
    • (1998) Ther. Drug Monit. , vol.20 , pp. 134-138
    • Woodland, C.1    Ito, S.2    Koren, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.