메뉴 건너뛰기




Volumn 101, Issue 1-2, 1999, Pages 43-59

Chelation of iron within the erythrocytic Plasmodium falciparum parasite by iron chelators

Author keywords

Antimalarial iron chelators; Calcein; Plasmodia

Indexed keywords

AMINOPHENOL; AMINOPHENOL DERIVATIVE; ANTIMALARIAL AGENT; BIPYRIDINE; CALCEIN; CALCIUM; DEFEROXAMINE; HEMATIN; HEMOGLOBIN; IRON CHELATING AGENT;

EID: 0032998958     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(99)00053-5     Document Type: Article
Times cited : (47)

References (52)
  • 2
    • 0025088403 scopus 로고
    • Stage-dependent effect of desferrioxamine on growth of Plasmodium falciparum in vitro
    • Whitehead S., Peto T.E.A. Stage-dependent effect of desferrioxamine on growth of Plasmodium falciparum in vitro. Blood. 76:1990;1250-1255.
    • (1990) Blood , vol.76 , pp. 1250-1255
    • Whitehead, S.1    Peto, T.E.A.2
  • 3
    • 0024366384 scopus 로고
    • Antimalarial activity of selected aromatic chelators V: localization of 59Fe in plasmodium falciparum in the presence of oxines
    • In: Eaton JW, Meshnik SR, Brewer GJ, editors Ann Arbor, Michigan, October 24 New York: Alan R. Liss
    • Scheibel LW, Rodriguez S, Antimalarial activity of selected aromatic chelators V: localization of 59Fe in plasmodium falciparum in the presence of oxines. In: Eaton JW, Meshnik SR, Brewer GJ, editors. Malaria and the Red Cell 2. Proceedings of the Second Workshop on Malaria and the Red Cell, Ann Arbor, Michigan, October 24, 1988. New York: Alan R. Liss, 1989: 119-149.
    • (1988) Malaria and the Red Cell 2. Proceedings of the Second Workshop on Malaria and the Red Cell , pp. 119-149
    • Scheibel, L.W.1    Rodriguez, S.2
  • 5
    • 0027153445 scopus 로고
    • In vivo antimalarial action of a lipophilic Fe(III) chelator: Suppression of Plasmodium vinckei infection by reversed siderophore
    • Lytton S.L., Loyevsky M., Mester B., Libman J., Landau I., Shanzer A., Cabantchik Z.I. In vivo antimalarial action of a lipophilic Fe(III) chelator: suppression of Plasmodium vinckei infection by reversed siderophore. Am. J. Hematol. 43:1993;217-220.
    • (1993) Am. J. Hematol. , vol.43 , pp. 217-220
    • Lytton, S.L.1    Loyevsky, M.2    Mester, B.3    Libman, J.4    Landau, I.5    Shanzer, A.6    Cabantchik, Z.I.7
  • 8
    • 0027488985 scopus 로고
    • Cloning, sequence determination, and regulation of the ribonucleotide reductase subunits from Plasmodium falciparum. A target for antimalarial therapy
    • Rubin H., Salem J.S., Li L.S., Jang F.D., Mama S. et al. Cloning, sequence determination, and regulation of the ribonucleotide reductase subunits from Plasmodium falciparum. A target for antimalarial therapy. Proc. Natl. Acad. Sci. USA. 90:1993;9280-9284.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9280-9284
    • Rubin, H.1    Salem, J.S.2    Li, L.S.3    Jang, F.D.4    Mama, S.5
  • 9
    • 0026785410 scopus 로고
    • De novo biosynthesis of heme offers a new chemotherapeutic target in the human malarial parasite
    • Surolia N., Padmanaban G. De novo biosynthesis of heme offers a new chemotherapeutic target in the human malarial parasite. Biochem. Biophys. Res. Commun. 187:1992;744-750.
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 744-750
    • Surolia, N.1    Padmanaban, G.2
  • 11
    • 0001402353 scopus 로고    scopus 로고
    • Cysteine proteinase inhibitors block early steps in hemoglobin degradation by cultured malaria parasites
    • Gamboa de Dominguez N., Rosenthal P.J. Cysteine proteinase inhibitors block early steps in hemoglobin degradation by cultured malaria parasites. Blood. 87:1996;4448-4454.
    • (1996) Blood , vol.87 , pp. 4448-4454
    • Gamboa De Dominguez, N.1    Rosenthal, P.J.2
  • 12
    • 0026726309 scopus 로고
    • A transferrin-independent Fe uptake activity in Plasmodium falciparum-infected and uninfected erythrocytes
    • Sanchez-Lopez R., Haldar K. A transferrin-independent Fe uptake activity in Plasmodium falciparum-infected and uninfected erythrocytes. Mol. Biochem. Parasitol. 55:1992;9-20.
    • (1992) Mol. Biochem. Parasitol. , vol.55 , pp. 9-20
    • Sanchez-Lopez, R.1    Haldar, K.2
  • 13
    • 0022967464 scopus 로고
    • A protein on Plasmodium falciparum-infected erythrocytes functions as a transferrin receptor
    • Rodriguez M.H., Jungery M. A protein on Plasmodium falciparum-infected erythrocytes functions as a transferrin receptor. Nature. 234:1986;388-391.
    • (1986) Nature , vol.234 , pp. 388-391
    • Rodriguez, M.H.1    Jungery, M.2
  • 14
    • 0000505513 scopus 로고
    • Identification of the parasite transferrin receptor of Plasmodium falciparum-infected erythrocytes and its acylation via 1,2-diacyl-sn-glycerol
    • Haldar K., Henderson C.L., Cross G.A.M. Identification of the parasite transferrin receptor of Plasmodium falciparum-infected erythrocytes and its acylation via 1,2-diacyl-sn-glycerol. Proc. Natl. Acad. Sci. USA. 83:1986;8565-8569.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8565-8569
    • Haldar, K.1    Henderson, C.L.2    Cross, G.A.M.3
  • 15
    • 0021163466 scopus 로고
    • Plasmodium falciparum takes up Fe from transferrin
    • Pollack S., Fleming J. Plasmodium falciparum takes up Fe from transferrin. B. J. Haematol. 58:1984;289-293.
    • (1984) B. J. Haematol. , vol.58 , pp. 289-293
    • Pollack, S.1    Fleming, J.2
  • 16
    • 0027379252 scopus 로고
    • Hemoglobin denaturation and Fe release in acidified red blood cell lysate-a possible source of Fe for intraerythrocytic malaria parasites
    • Gabay T., Ginsburg H. Hemoglobin denaturation and Fe release in acidified red blood cell lysate-a possible source of Fe for intraerythrocytic malaria parasites. Exp. Parasitol. 77:1993;261-272.
    • (1993) Exp. Parasitol. , vol.77 , pp. 261-272
    • Gabay, T.1    Ginsburg, H.2
  • 17
    • 0023740339 scopus 로고
    • Deferoxamine inhibition of malaria is independent of host Fe status
    • Hershko H., Peto T.E.A. Deferoxamine inhibition of malaria is independent of host Fe status. J. Exp. Med. 168:1988;375-387.
    • (1988) J. Exp. Med. , vol.168 , pp. 375-387
    • Hershko, H.1    Peto, T.E.A.2
  • 18
    • 0028243344 scopus 로고
    • Inhibition by anti-malarial drugs of hemoglobin denaturation and Fe release in acidified red blood cell lysates - A possible mechanism of their anti-malarial effect
    • Gabay T., Krugliak M., Shalmiev G., Ginsburg H. Inhibition by anti-malarial drugs of hemoglobin denaturation and Fe release in acidified red blood cell lysates - a possible mechanism of their anti-malarial effect. Parasitology. 108:1994;371-381.
    • (1994) Parasitology , vol.108 , pp. 371-381
    • Gabay, T.1    Krugliak, M.2    Shalmiev, G.3    Ginsburg, H.4
  • 19
    • 0023930872 scopus 로고
    • Inability to detect transferrin receptors on P. falciparum parasitized red cells
    • Pollack S., Schnelle V. Inability to detect transferrin receptors on P. falciparum parasitized red cells. Br. J. Haematol. 68:1988;125-129.
    • (1988) Br. J. Haematol. , vol.68 , pp. 125-129
    • Pollack, S.1    Schnelle, V.2
  • 20
    • 0025102616 scopus 로고
    • Parasite uptake of desferrioxamine: A prerequisite for antimalarial activity
    • Scott M.D., Ranz A., Kuypers F.A., Lubin B.H., Meshnik S.R. Parasite uptake of desferrioxamine: a prerequisite for antimalarial activity. Br. J. Haematol. 75:1990;598-602.
    • (1990) Br. J. Haematol. , vol.75 , pp. 598-602
    • Scott, M.D.1    Ranz, A.2    Kuypers, F.A.3    Lubin, B.H.4    Meshnik, S.R.5
  • 21
    • 0027392073 scopus 로고
    • The antimalarial action of desferal involves a direct access route to erythrocytic (Plasmodium falciparum) parasites
    • Loyevsky M., Lytton S., Mester B., Libman J., Shanzer A., Cabantchik Z.I. The antimalarial action of desferal involves a direct access route to erythrocytic (Plasmodium falciparum) parasites. J. Clin. Invest. 91:1993;218-224.
    • (1993) J. Clin. Invest. , vol.91 , pp. 218-224
    • Loyevsky, M.1    Lytton, S.2    Mester, B.3    Libman, J.4    Shanzer, A.5    Cabantchik, Z.I.6
  • 22
    • 0026514177 scopus 로고
    • Inhibition by chloroquine of a novel haem polymerase enzyme activity in malaria trophozoites
    • Slater A.F., Cerami A. Inhibition by chloroquine of a novel haem polymerase enzyme activity in malaria trophozoites. Nature. 355:1992;167-169.
    • (1992) Nature , vol.355 , pp. 167-169
    • Slater, A.F.1    Cerami, A.2
  • 23
    • 0027948987 scopus 로고
    • The biochemical basis for the selective antimalarial action of iron chelators on Plasmodium falciparum parasitized cells
    • In: Hershko C, Konijn AM, Aisen P, editors, New York: Plenum Press
    • Lytton SD, Loyevsky M, Libman J, Mester B, Shanzer A, Cabantchik ZI. The biochemical basis for the selective antimalarial action of iron chelators on Plasmodium falciparum parasitized cells. In: Hershko C, Konijn AM, Aisen P, editors, Progress in iron Research. New York: Plenum Press, 1994: 385-397.
    • (1994) Progress in Iron Research , pp. 385-397
    • Lytton, S.D.1    Loyevsky, M.2    Libman, J.3    Mester, B.4    Shanzer, A.5    Cabantchik, Z.I.6
  • 26
  • 27
    • 0031413254 scopus 로고    scopus 로고
    • Role of the mitochondrial permeability transition in salicylate toxicity to cultured rat hepatocytes: Implications for the pathogenesis of Reye's Syndrome
    • Trost L.C., Lemasters J.J. Role of the mitochondrial permeability transition in salicylate toxicity to cultured rat hepatocytes: implications for the pathogenesis of Reye's Syndrome. Toxicol. Appl. Pharmacol. 147:1997;431-441.
    • (1997) Toxicol. Appl. Pharmacol. , vol.147 , pp. 431-441
    • Trost, L.C.1    Lemasters, J.J.2
  • 29
    • 0028817755 scopus 로고
    • High-performance liquid chromatographic analysis of biological and chemical heme polymerization
    • Berger B.J., Bendrat K., Cerami A. High-performance liquid chromatographic analysis of biological and chemical heme polymerization. Anal. Biochem. 231:1995;151-156.
    • (1995) Anal. Biochem. , vol.231 , pp. 151-156
    • Berger, B.J.1    Bendrat, K.2    Cerami, A.3
  • 31
    • 0002684580 scopus 로고
    • Oxo-bis-oxo dinuclear complexes of technetium (V) with amine phenol ligands: Synthesis, characterization and X-ray crystal structures
    • Pillai M.R.A., John C.S., Lo J.M., Schlemper E.O., Troutner D.E. Oxo-bis-oxo dinuclear complexes of technetium (V) with amine phenol ligands: synthesis, characterization and X-ray crystal structures. Inorg. Chem. 29:1990;1850-1861.
    • (1990) Inorg. Chem. , vol.29 , pp. 1850-1861
    • Pillai, M.R.A.1    John, C.S.2    Lo, J.M.3    Schlemper, E.O.4    Troutner, D.E.5
  • 33
    • 0001101920 scopus 로고
    • Chelation of ferrous sulfate solutions by desferrioxamine B
    • Goodwin J.F., Whitten C.F. Chelation of ferrous sulfate solutions by desferrioxamine B. Nature. 205:1965;281-283.
    • (1965) Nature , vol.205 , pp. 281-283
    • Goodwin, J.F.1    Whitten, C.F.2
  • 34
    • 0023704559 scopus 로고
    • Use of chelating agents to inhibit enzymes
    • Auld D.S. Use of chelating agents to inhibit enzymes. Meth. Enzymol. 158:1988;110-114.
    • (1988) Meth. Enzymol. , vol.158 , pp. 110-114
    • Auld, D.S.1
  • 35
    • 0017311840 scopus 로고
    • Continuous culture of human malaria parasites
    • Trager W., Jensen J.B. Continuous culture of human malaria parasites. Science (Washington, D.C.). 193:1976;673-675.
    • (1976) Science (Washington, D.C.) , vol.193 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 36
    • 0018704491 scopus 로고
    • Synchronization of Plasmodium falciparum erythrocytic stages in culture
    • Lambros C., Vanderberg J.P. Synchronization of Plasmodium falciparum erythrocytic stages in culture. J. Parasitol. 65:1979;418-420.
    • (1979) J. Parasitol. , vol.65 , pp. 418-420
    • Lambros, C.1    Vanderberg, J.P.2
  • 37
    • 0027323244 scopus 로고
    • Hemozoin production by Plasmodium falciparum: Variation with strain and exposure to chloroquine
    • Orjih A.U., Fitch C.D. Hemozoin production by Plasmodium falciparum: variation with strain and exposure to chloroquine. Biochim. Biophys. Acta. 1157:1993;270-274.
    • (1993) Biochim. Biophys. Acta , vol.1157 , pp. 270-274
    • Orjih, A.U.1    Fitch, C.D.2
  • 39
    • 0020313839 scopus 로고
    • Calcium transport of Plasmodium chabaudi-infected erythrocytes
    • Tanabe K., Mikkelsen R.B., Wallach D.F.H. Calcium transport of Plasmodium chabaudi-infected erythrocytes. J. Cell Biol. 93:1982;680-684.
    • (1982) J. Cell Biol. , vol.93 , pp. 680-684
    • Tanabe, K.1    Mikkelsen, R.B.2    Wallach, D.F.H.3
  • 41
    • 0345652158 scopus 로고
    • Identification of the acidic compartment of Plasmodium falciparum-infected human erythrocytes as the target of the antimalarial drug chloroquine
    • Yayon A., Cabantchik Z.I., Ginsburg H. 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    Cabantchik, Z.I.2    Ginsburg, H.3
  • 42
    • 0018237740 scopus 로고
    • Concentration from continuous culture of erythrocytes infected with trophozoites and schizonts of Plasmodium falciparum
    • Jensen J.B. Concentration from continuous culture of erythrocytes infected with trophozoites and schizonts of Plasmodium falciparum. Am. J. Trop. Med. Hyg. 27:1978;1274-1276.
    • (1978) Am. J. Trop. Med. Hyg. , vol.27 , pp. 1274-1276
    • Jensen, J.B.1
  • 43
    • 0030030821 scopus 로고    scopus 로고
    • A fluorescence assay for assessing chelation of intracellular iron in a membrane model system and in mammalian cells
    • Cabantchik Z.I., Glickstein H., Milgram P., Breuer W. A fluorescence assay for assessing chelation of intracellular iron in a membrane model system and in mammalian cells. Anal. Biochem. 233:1996;221-227.
    • (1996) Anal. Biochem. , vol.233 , pp. 221-227
    • Cabantchik, Z.I.1    Glickstein, H.2    Milgram, P.3    Breuer, W.4
  • 44
    • 0027521831 scopus 로고
    • Role of ribonucleotide reductase in inhibition of mammalian cell growth by potent iron chelators
    • Nyholm S, Mann GI, Johanson AG, Bergeron RJ, Graslund A, Thelander L. Role of ribonucleotide reductase in inhibition of mammalian cell growth by potent iron chelators. J. Biol. Chem. 1993;268:26200-5.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26200-26205
    • Nyholm, S.1    Mann, G.I.2    Johanson, A.G.3    Bergeron, R.J.4    Graslund, A.5    Thelander, L.6
  • 46
    • 0026680709 scopus 로고
    • Iron release and membrane damage in erythrocytes exposed to oxidizing agents, phenylhydrazine, divicine and isouramil
    • Ferrali M., Signorini C., Ciccoli L., Comporti M. Iron release and membrane damage in erythrocytes exposed to oxidizing agents, phenylhydrazine, divicine and isouramil. Biochem. J. 285:1992;293-301.
    • (1992) Biochem. J. , vol.285 , pp. 293-301
    • Ferrali, M.1    Signorini, C.2    Ciccoli, L.3    Comporti, M.4
  • 47
    • 0025251655 scopus 로고
    • Properties of permeation pathways induced in the human red cell membrane by malaria parasites
    • Cabantchik Z.I. Properties of permeation pathways induced in the human red cell membrane by malaria parasites. Blood Cells. 16:1990;421-432.
    • (1990) Blood Cells , vol.16 , pp. 421-432
    • Cabantchik, Z.I.1
  • 49
    • 0027430639 scopus 로고
    • Origin of reactive oxygen species in erythrocytes infected with Plasmodium falciparum
    • Atamna H., Ginsburg H. Origin of reactive oxygen species in erythrocytes infected with Plasmodium falciparum. Mol. Biochem. Parasitol. 61:1993;231-242.
    • (1993) Mol. Biochem. Parasitol. , vol.61 , pp. 231-242
    • Atamna, H.1    Ginsburg, H.2
  • 50
    • 0017578794 scopus 로고
    • 2+ binding to the sarcoplasmic reticulum. Use of a high-affinity fluorescent calcium indicator
    • 2+ binding to the sarcoplasmic reticulum. Use of a high-affinity fluorescent calcium indicator. Biophys. J. 18:1977;3-22.
    • (1977) Biophys. J. , vol.18 , pp. 3-22
    • Chiu, V.C.K.1    Haynes, D.H.2
  • 51
    • 0028852090 scopus 로고
    • Natural resistance to infection with intracellular parasites: Molecular genetics identifies Nramp1 as the Bcg/Ity/Lsh locus
    • Vidal S., Gros P., Skamene E. Natural resistance to infection with intracellular parasites: molecular genetics identifies Nramp1 as the Bcg/Ity/Lsh locus. J. Leukoc. Biol. 58:1995;382-390.
    • (1995) J. Leukoc. Biol. , vol.58 , pp. 382-390
    • Vidal, S.1    Gros, P.2    Skamene, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.