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Volumn 23, Issue 7, 2007, Pages 332-339

Is PfCRT a channel or a carrier? Two competing models explaining chloroquine resistance in Plasmodium falciparum

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; CELL PROTEIN; CHLOROQUINE; PFCRT PROTEIN; UNCLASSIFIED DRUG;

EID: 34250644012     PISSN: 14714922     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pt.2007.04.013     Document Type: Review
Times cited : (56)

References (45)
  • 2
    • 22744447610 scopus 로고    scopus 로고
    • A critical role for PfCRT K76T in Plasmodium falciparum verapamil-reversible chloroquine resistance
    • Lakshmanan V., et al. A critical role for PfCRT K76T in Plasmodium falciparum verapamil-reversible chloroquine resistance. EMBO J. 24 (2005) 2294-2305
    • (2005) EMBO J. , vol.24 , pp. 2294-2305
    • Lakshmanan, V.1
  • 3
    • 0037101785 scopus 로고    scopus 로고
    • Fate of haem iron in the malaria parasite Plasmodium falciparum
    • Egan T.J., et al. Fate of haem iron in the malaria parasite Plasmodium falciparum. Biochem. J. 365 (2002) 343-347
    • (2002) Biochem. J. , vol.365 , pp. 343-347
    • Egan, T.J.1
  • 4
    • 1142297431 scopus 로고    scopus 로고
    • Ferriprotoporphyrin IX, phospholipids, and the antimalarial actions of quinoline drugs
    • Fitch C.D. Ferriprotoporphyrin IX, phospholipids, and the antimalarial actions of quinoline drugs. Life Sci. 74 (2004) 1957-1972
    • (2004) Life Sci. , vol.74 , pp. 1957-1972
    • Fitch, C.D.1
  • 5
    • 0041696955 scopus 로고    scopus 로고
    • NMR studies of chloroquine-ferriprotoporphyrin IX complex
    • De Dios A.C., et al. NMR studies of chloroquine-ferriprotoporphyrin IX complex. J. Phys. Chem. A 107 (2003) 5821-5825
    • (2003) J. Phys. Chem. A , vol.107 , pp. 5821-5825
    • De Dios, A.C.1
  • 6
    • 0037072289 scopus 로고    scopus 로고
    • Solution structures of antimalarial drug-heme complexes
    • Leed A., et al. Solution structures of antimalarial drug-heme complexes. Biochemistry 41 (2002) 10245-10255
    • (2002) Biochemistry , vol.41 , pp. 10245-10255
    • Leed, A.1
  • 7
    • 0031818645 scopus 로고    scopus 로고
    • Access to hematin: the basis of chloroquine resistance
    • Bray P.G., et al. Access to hematin: the basis of chloroquine resistance. Mol. Pharmacol. 54 (1998) 170-179
    • (1998) Mol. Pharmacol. , vol.54 , pp. 170-179
    • Bray, P.G.1
  • 8
    • 0042573722 scopus 로고    scopus 로고
    • Trans stimulation provides evidence for a drug efflux carrier as the mechanism of chloroquine resistance in Plasmodium falciparum
    • Sanchez C.P., et al. Trans stimulation provides evidence for a drug efflux carrier as the mechanism of chloroquine resistance in Plasmodium falciparum. Biochemistry 42 (2003) 9383-9394
    • (2003) Biochemistry , vol.42 , pp. 9383-9394
    • Sanchez, C.P.1
  • 9
    • 0026580108 scopus 로고
    • Energy dependence of chloroquine accumulation and chloroquine efflux in Plasmodium falciparum
    • Krogstad D.J., et al. Energy dependence of chloroquine accumulation and chloroquine efflux in Plasmodium falciparum. Biochem. Pharmacol. 43 (1992) 57-62
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 57-62
    • Krogstad, D.J.1
  • 10
    • 33748645940 scopus 로고    scopus 로고
    • PfCRT and the trans-vacuolar proton electrochemical gradient: regulating the access of chloroquine to ferriprotoporphyrin IX
    • Bray P.G., et al. PfCRT and the trans-vacuolar proton electrochemical gradient: regulating the access of chloroquine to ferriprotoporphyrin IX. Mol. Microbiol. 62 (2006) 238-251
    • (2006) Mol. Microbiol. , vol.62 , pp. 238-251
    • Bray, P.G.1
  • 11
    • 0032562763 scopus 로고    scopus 로고
    • Transport and metabolism of the essential vitamin pantothenic acid in human erythrocytes infected with the malaria parasite Plasmodium falciparum
    • Saliba K.J., et al. Transport and metabolism of the essential vitamin pantothenic acid in human erythrocytes infected with the malaria parasite Plasmodium falciparum. J. Biol. Chem. 273 (1998) 10190-10195
    • (1998) J. Biol. Chem. , vol.273 , pp. 10190-10195
    • Saliba, K.J.1
  • 12
    • 0345652158 scopus 로고
    • Identification of the acidic compartment of Plasmodium falciparum-infected human erythrocytes as the target of the antimalarial drug chloroquine
    • Yayon A., et al. Identification of the acidic compartment of Plasmodium falciparum-infected human erythrocytes as the target of the antimalarial drug chloroquine. EMBO J. 3 (1984) 2695-2700
    • (1984) EMBO J. , vol.3 , pp. 2695-2700
    • Yayon, A.1
  • 13
    • 0344867895 scopus 로고    scopus 로고
    • Cellular uptake of chloroquine is dependent on binding to ferriprotoporphyrin IX and is independent of NHE activity in Plasmodium falciparum
    • Bray P.G., et al. Cellular uptake of chloroquine is dependent on binding to ferriprotoporphyrin IX and is independent of NHE activity in Plasmodium falciparum. J. Cell Biol. 145 (1999) 363-376
    • (1999) J. Cell Biol. , vol.145 , pp. 363-376
    • Bray, P.G.1
  • 14
    • 16044372680 scopus 로고    scopus 로고
    • On the molecular mechanism of chloroquine's antimalarial action
    • Sullivan Jr. D.J., et al. On the molecular mechanism of chloroquine's antimalarial action. Proc. Natl Acad. Sci. U. S. A. 93 (1996) 11865-11870
    • (1996) Proc. Natl Acad. Sci. U. S. A. , vol.93 , pp. 11865-11870
    • Sullivan Jr., D.J.1
  • 15
    • 0022347074 scopus 로고
    • Antimalarials increase vesicle pH in Plasmodium falciparum
    • Krogstad D.J., et al. Antimalarials increase vesicle pH in Plasmodium falciparum. J. Cell Biol. 101 (1985) 2302-2309
    • (1985) J. Cell Biol. , vol.101 , pp. 2302-2309
    • Krogstad, D.J.1
  • 16
    • 33645751112 scopus 로고    scopus 로고
    • The pH of the digestive vacuole of Plasmodium falciparum is not associated with chloroquine resistance
    • Hayward R., et al. The pH of the digestive vacuole of Plasmodium falciparum is not associated with chloroquine resistance. J. Cell Sci. 119 (2006) 1016-1025
    • (2006) J. Cell Sci. , vol.119 , pp. 1016-1025
    • Hayward, R.1
  • 17
    • 33947125517 scopus 로고    scopus 로고
    • Quantitative pH measurements in Plasmodium falciparum-infected erythrocytes using pHluorin
    • Kuhn Y., et al. Quantitative pH measurements in Plasmodium falciparum-infected erythrocytes using pHluorin. Cell. Microbiol. 9 (2007) 1004-1013
    • (2007) Cell. Microbiol. , vol.9 , pp. 1004-1013
    • Kuhn, Y.1
  • 18
    • 0007740769 scopus 로고
    • Susceptibility of human malaria parasites to chloroquine is pH dependent
    • Yayon A., et al. Susceptibility of human malaria parasites to chloroquine is pH dependent. Proc. Natl. Acad. Sci. U. S. A. 82 (1985) 2784-2788
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 2784-2788
    • Yayon, A.1
  • 19
    • 0025046280 scopus 로고
    • Kinetic modelling of the response of Plasmodium falciparum to chloroquine and its experimental testing in vitro. Implications for mechanism of action of and resistance to the drug
    • Geary T.G., et al. Kinetic modelling of the response of Plasmodium falciparum to chloroquine and its experimental testing in vitro. Implications for mechanism of action of and resistance to the drug. Biochem. Pharmacol. 40 (1990) 685-691
    • (1990) Biochem. Pharmacol. , vol.40 , pp. 685-691
    • Geary, T.G.1
  • 20
    • 0345528107 scopus 로고    scopus 로고
    • Drug resistance-associated PfCRT mutations confer decreased Plasmodium falciparum digestive vacuolar pH
    • Bennett T.N., et al. Drug resistance-associated PfCRT mutations confer decreased Plasmodium falciparum digestive vacuolar pH. Mol. Biochem. Parasitol. 133 (2004) 99-114
    • (2004) Mol. Biochem. Parasitol. , vol.133 , pp. 99-114
    • Bennett, T.N.1
  • 21
    • 0033827908 scopus 로고    scopus 로고
    • Digestive vacuolar pH of intact intraerythrocytic P. falciparum either sensitive or resistant to chloroquine
    • Dzekunov S.M., et al. Digestive vacuolar pH of intact intraerythrocytic P. falciparum either sensitive or resistant to chloroquine. Mol. Biochem. Parasitol. 110 (2000) 107-124
    • (2000) Mol. Biochem. Parasitol. , vol.110 , pp. 107-124
    • Dzekunov, S.M.1
  • 22
    • 0036155237 scopus 로고    scopus 로고
    • Distribution of acridine orange fluorescence in Plasmodium falciparum-infected erythrocytes and its implications for the evaluation of digestive vacuole pH
    • discussion 307-309, 311-313
    • Bray P.G., et al. Distribution of acridine orange fluorescence in Plasmodium falciparum-infected erythrocytes and its implications for the evaluation of digestive vacuole pH. Mol. Biochem. Parasitol. 119 (2002) 301-304 discussion 307-309, 311-313
    • (2002) Mol. Biochem. Parasitol. , vol.119 , pp. 301-304
    • Bray, P.G.1
  • 23
    • 0037020172 scopus 로고    scopus 로고
    • Illumination of the malaria parasite Plasmodium falciparum alters intracellular pH. Implications for live cell imaging
    • Wissing F., et al. Illumination of the malaria parasite Plasmodium falciparum alters intracellular pH. Implications for live cell imaging. J. Biol. Chem. 277 (2002) 37747-37755
    • (2002) J. Biol. Chem. , vol.277 , pp. 37747-37755
    • Wissing, F.1
  • 24
    • 0023666563 scopus 로고
    • Efflux of chloroquine from Plasmodium falciparum: mechanism of chloroquine resistance
    • Krogstad D.J., et al. Efflux of chloroquine from Plasmodium falciparum: mechanism of chloroquine resistance. Science 238 (1987) 1283-1285
    • (1987) Science , vol.238 , pp. 1283-1285
    • Krogstad, D.J.1
  • 25
    • 3142618432 scopus 로고    scopus 로고
    • The antimalarial drug resistance protein Plasmodium falciparum chloroquine resistance transporter binds chloroquine
    • Zhang H., et al. The antimalarial drug resistance protein Plasmodium falciparum chloroquine resistance transporter binds chloroquine. Biochemistry 43 (2004) 8290-8296
    • (2004) Biochemistry , vol.43 , pp. 8290-8296
    • Zhang, H.1
  • 26
    • 0037121251 scopus 로고    scopus 로고
    • Lysosomes and drug resistance in malaria
    • Warhurst D.C., et al. Lysosomes and drug resistance in malaria. Lancet 360 (2002) 1527-1529
    • (2002) Lancet , vol.360 , pp. 1527-1529
    • Warhurst, D.C.1
  • 27
    • 22744436592 scopus 로고    scopus 로고
    • Evidence for a pfcrt-associated chloroquine efflux system in the human malarial parasite Plasmodium falciparum
    • Sanchez C.P., et al. Evidence for a pfcrt-associated chloroquine efflux system in the human malarial parasite Plasmodium falciparum. Biochemistry 44 (2005) 9862-9870
    • (2005) Biochemistry , vol.44 , pp. 9862-9870
    • Sanchez, C.P.1
  • 28
    • 11144279334 scopus 로고    scopus 로고
    • Evidence for a substrate specific and inhibitable drug efflux system in chloroquine resistant Plasmodium falciparum strains
    • Sanchez C.P., et al. Evidence for a substrate specific and inhibitable drug efflux system in chloroquine resistant Plasmodium falciparum strains. Biochemistry 43 (2004) 16365-16373
    • (2004) Biochemistry , vol.43 , pp. 16365-16373
    • Sanchez, C.P.1
  • 29
    • 21844437088 scopus 로고    scopus 로고
    • Dictyostelium discoideum expresses a malaria chloroquine resistance mechanism upon transfection with mutant, but not wild-type, Plasmodium falciparum transporter PfCRT
    • Naude B., et al. Dictyostelium discoideum expresses a malaria chloroquine resistance mechanism upon transfection with mutant, but not wild-type, Plasmodium falciparum transporter PfCRT. J. Biol. Chem. 280 (2005) 25596-25603
    • (2005) J. Biol. Chem. , vol.280 , pp. 25596-25603
    • Naude, B.1
  • 30
    • 1642483495 scopus 로고    scopus 로고
    • The membrane potential of the intraerythrocytic malaria parasite Plasmodium falciparum
    • Allen R.J., and Kirk K. The membrane potential of the intraerythrocytic malaria parasite Plasmodium falciparum. J. Biol. Chem. 279 (2004) 11264-11272
    • (2004) J. Biol. Chem. , vol.279 , pp. 11264-11272
    • Allen, R.J.1    Kirk, K.2
  • 31
    • 34247364130 scopus 로고    scopus 로고
    • Differences in trans-stimulated chloroquine efflux kinetics are linked to PfCRT in Plasmodium falciparum
    • Sanchez C.P., et al. Differences in trans-stimulated chloroquine efflux kinetics are linked to PfCRT in Plasmodium falciparum. Mol. Microbiol. 64 (2007) 407-420
    • (2007) Mol. Microbiol. , vol.64 , pp. 407-420
    • Sanchez, C.P.1
  • 33
    • 0015829131 scopus 로고
    • The asymmetry of the facilitated transfer system for hexoses in human red cells and the simple kinetics of a two component model
    • Baker G.F., and Widdas W.F. The asymmetry of the facilitated transfer system for hexoses in human red cells and the simple kinetics of a two component model. J. Physiol. 231 (1973) 143-165
    • (1973) J. Physiol. , vol.231 , pp. 143-165
    • Baker, G.F.1    Widdas, W.F.2
  • 34
    • 18244396971 scopus 로고    scopus 로고
    • Alternative mutations at position 76 of the vacuolar transmembrane protein PfCRT are associated with chloroquine resistance and unique stereospecific quinine and quinidine responses in Plasmodium falciparum
    • Cooper R.A., et al. Alternative mutations at position 76 of the vacuolar transmembrane protein PfCRT are associated with chloroquine resistance and unique stereospecific quinine and quinidine responses in Plasmodium falciparum. Mol. Pharmacol. 61 (2002) 35-42
    • (2002) Mol. Pharmacol. , vol.61 , pp. 35-42
    • Cooper, R.A.1
  • 35
    • 0035945682 scopus 로고    scopus 로고
    • A molecular marker for chloroquine-resistant falciparum malaria
    • Djimde A., et al. A molecular marker for chloroquine-resistant falciparum malaria. N. Engl. J. Med. 344 (2001) 257-263
    • (2001) N. Engl. J. Med. , vol.344 , pp. 257-263
    • Djimde, A.1
  • 36
    • 0033636607 scopus 로고    scopus 로고
    • Mutations in the P. falciparum digestive vacuole transmembrane protein PfCRT and evidence for their role in chloroquine resistance
    • Fidock D.A., et al. Mutations in the P. falciparum digestive vacuole transmembrane protein PfCRT and evidence for their role in chloroquine resistance. Mol. Cell 6 (2000) 861-871
    • (2000) Mol. Cell , vol.6 , pp. 861-871
    • Fidock, D.A.1
  • 37
    • 0037020024 scopus 로고    scopus 로고
    • Chloroquine resistance in Plasmodium falciparum malaria parasites conferred by pfcrt mutations
    • Sidhu A.B., et al. Chloroquine resistance in Plasmodium falciparum malaria parasites conferred by pfcrt mutations. Science 298 (2002) 210-213
    • (2002) Science , vol.298 , pp. 210-213
    • Sidhu, A.B.1
  • 38
    • 4644251136 scopus 로고    scopus 로고
    • Evidence for a central role for PfCRT in conferring Plasmodium falciparum resistance to diverse antimalarial agents
    • Johnson D.J., et al. Evidence for a central role for PfCRT in conferring Plasmodium falciparum resistance to diverse antimalarial agents. Mol. Cell 15 (2004) 867-877
    • (2004) Mol. Cell , vol.15 , pp. 867-877
    • Johnson, D.J.1
  • 39
    • 3142772962 scopus 로고    scopus 로고
    • Dissecting the loci of low-level quinine resistance in malaria parasites
    • Ferdig M.T., et al. Dissecting the loci of low-level quinine resistance in malaria parasites. Mol. Microbiol. 52 (2004) 985-997
    • (2004) Mol. Microbiol. , vol.52 , pp. 985-997
    • Ferdig, M.T.1
  • 40
    • 4944253804 scopus 로고    scopus 로고
    • The malaria parasite's chloroquine resistance transporter is a member of the drug/metabolite transporter superfamily
    • Martin R.E., and Kirk K. The malaria parasite's chloroquine resistance transporter is a member of the drug/metabolite transporter superfamily. Mol. Biol. Evol. 21 (2004) 1938-1949
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 1938-1949
    • Martin, R.E.1    Kirk, K.2
  • 41
    • 1642473952 scopus 로고    scopus 로고
    • The principal chloroquine resistance protein of Plasmodium falciparum is a member of the drug/metabolite transporter superfamily
    • Tran C.V., and Saier Jr. M.H. The principal chloroquine resistance protein of Plasmodium falciparum is a member of the drug/metabolite transporter superfamily. Microbiology 150 (2004) 1-3
    • (2004) Microbiology , vol.150 , pp. 1-3
    • Tran, C.V.1    Saier Jr., M.H.2
  • 42
    • 33746805903 scopus 로고    scopus 로고
    • Functional reconstitution of purified chloroquine resistance membrane transporter expressed in yeast
    • Tan W., et al. Functional reconstitution of purified chloroquine resistance membrane transporter expressed in yeast. Arch. Biochem. Biophys. 452 (2006) 119-128
    • (2006) Arch. Biochem. Biophys. , vol.452 , pp. 119-128
    • Tan, W.1
  • 43
    • 1942501812 scopus 로고    scopus 로고
    • Site-directed mutation of arginine 282 to glutamate uncouples the movement of peptides and protons by the rabbit proton-peptide cotransporter PepT1
    • Meredith D. Site-directed mutation of arginine 282 to glutamate uncouples the movement of peptides and protons by the rabbit proton-peptide cotransporter PepT1. J. Biol. Chem. 279 (2004) 15795-15798
    • (2004) J. Biol. Chem. , vol.279 , pp. 15795-15798
    • Meredith, D.1
  • 44
    • 0039966984 scopus 로고    scopus 로고
    • +/proline transporter of Escherichia coli
    • +/proline transporter of Escherichia coli. Biochemistry 38 (1999) 13523-13529
    • (1999) Biochemistry , vol.38 , pp. 13523-13529
    • Quick, M.1
  • 45
    • 0343945299 scopus 로고
    • Facilitated transfer of hexoses across the human erythrocyte membrane
    • Widdas W.F. Facilitated transfer of hexoses across the human erythrocyte membrane. J. Physiol. 125 (1954) 163-180
    • (1954) J. Physiol. , vol.125 , pp. 163-180
    • Widdas, W.F.1


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