Role of glutathione in the detoxification of ferriprotoporphyrin IX in chloroquine resistant Plasmodium berghei

Molecular and Biochemical Parasitology

Volumn 98, Issue 2, 1999, Pages 215-223

  Platel, D F N ^a   Mangou, F ^a   Tribouley Duret, J ^a  

^a UNIVERSITÉ DE BORDEAUX   (France)

Author keywords

Chloroquine resistance; Glutathione; Glutathione S transferase; Hemozoin; Plasmodium berghei; Reticulocytes

Indexed keywords

BUTHIONINE SULFOXIMINE; CHLOROQUINE; GLUTATHIONE; GLUTATHIONE DISULFIDE; GLUTATHIONE TRANSFERASE; HEMATIN; HEMOZOIN;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; DETOXIFICATION; DRUG RESISTANCE; ERYTHROCYTE; HOST RESISTANCE; MALE; MOUSE; NONHUMAN; PLASMODIUM BERGHEI; POLYMERIZATION; PRIORITY JOURNAL; RETICULOCYTE; TROPHOZOITE;

ANIMALS; ANTIMALARIALS; BUTHIONINE SULFOXIMINE; CHLOROQUINE; DRUG RESISTANCE; GLUTATHIONE; GLUTATHIONE TRANSFERASE; HEMEPROTEINS; HEMIN; MALARIA; METABOLIC DETOXICATION, DRUG; MICE; PLASMODIUM BERGHEI; VACUOLES;

PLASMODIUM BERGHEI;

EID: 0033056373     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(98)00170-4     Document Type: Article

References (37)

1. Goldberg D.E., Slater A.F.G., Cerami A., Henderson G.B. Hemoglobin degradation in the malaria parasite Plasmodium falciparum: an ordered process in a unique organelle. Proc. Natl. Acad. Sci. USA. 87:1990;2931-2935.
2. Slater A.F.G., Swiggard W.J., Orton B.R. et al. An iron-carboxylate bond links the heme units of malaria pigment. Proc. Natl. Acad. Sci. USA. 88:1991;325-329.
3. Dorn A., Stoffel R., Matile H., Budendorf A., Ridley R.G. Malarial haemozoin/β-haematin supports haem polymerization in the absence of protein. Nature. 374:1995;269-271.
4. Chou A.C., Chevli R., Fitch C.D. Ferriprotoporphyrin IX fulfills the criteria for identification as the chloroquine receptor of malaria parasites. Biochemistry. 19:1980;1543-1549.
5. Fitch C.D., Chevli R. Sequestration of the chloroquine receptor in cell-free preparations of erythrocytes infected with Plasmodium berghei. Antimicrob. Agents Chemother. 19:1981;589-592.
6. Constantinidis I., Satterlee J.D. UV-visible and carbon NMR studies of chloroquine binding to urohemin I chloride and uroporphyrin I in aqueous solutions. J. Am. Chem. Soc. 110:1988;4391-4395.
7. Constantinidis I., Satterlee J.D. UV-visible and carbon NMR studies of quinine binding to urohemin I chloride and uroporphyrin I in aqueous solution. J. Am. Chem. Soc. 110:1988;927-932.
8. Blauer G. Interaction of ferriprotoporphyrin IX with the antimalarials amodiaquine and halofantrine. Biochem. Int. 17:1988;729-734.
9. Sullivan D.J., Gluzman I.Y., Russel D.G., Goldberg D.E. On the molecular mechanism of chloroquine's antimalarial action. Proc. Natl. Acad. Sci. USA. 93:1996;11865-11870.
10. Chou A.C., Fitch C.D. Control of heme polymerase by chloroquine and other quinoline derivatives. Biochem. Biophys. Res. Comm. 195:1993;422-427.
11. Vander Jagt D.L., Hunsaker L.A., Campos N.M. Characterization of a hemoglobin-degrading, low molecular weight protease from Plasmodium falciparum. Mol. Biochem. Parasitol. 18:1986;389-400.
12. Sugioka Y., Suzuki M., Sugioka K., Nakano M. A ferriprotoporphyrin IX-chloroquine complex promotes membrane phospholipid peroxidation. FEBS. Lett. 223:1987;251-254.
13. Sugioka Y., Suzuki M. The chemical basis for the ferriprotoporphyrin IX-chloroquine complex induced lipid peroxidation. Biochim. Biophys. Acta. 1074:1991;19-24.
14. Orjih A.U. Heme polymerase activity and the stage specificity of antimalarial action of chloroquine. J. Pharmacol. Exp. Ther. 282:1997;108-112.
15. Dubois V.L., Platel D.F.N., Pauly G., Tribouley-Duret J. Plasmodium berghei: implication of intracellular glutathione and its related enzymes in chloroquine resistance in vivo. Exp. Parasitol. 81:1995;117-124.
16. Platel D.F.N., Mangou F., Tribouley-Duret J. High-level chloroquine resistance of Plasmodium berghei is associated with multiple drug resistance and loss of reversal by calcium antagonists. Int. J. Parasitol. 28:1998;641-651.
17. Peters W. The chemotherapy of rodent malaria-II-Host-parasite relationship, part 2. The relationship between chloroquine sensitivity and the age of the host cell. Ann. Trop. Med. Parasitol. 62:1968;246-251.
18. Peters W. The chemotherapy of rodent malaria-V-Dynamics of drug resistance, part 1. Methods for studying the acquisition and loss of resistance to chloroquine by Plasmodium berghei. Ann. Trop. Med. Parasitol. 62:1968;277-287.
19. Hunt N.H., Stocker R. Oxidative stress and the redox status of malaria-infected erythrocytes. Blood Cells. 16:1990;499-526.
20. Atamna H., Ginsburg H. Heme degradation in the presence of glutathione. J. Biol. Chem. 270:1995;24876-24883.
21. Ellman G.L., Courtney K.D., Andres V., Featherstone R.M. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol. 7:1961;88-95.
22. Brehe J.E., Burch M.B. Enzymatic assay for glutathione. Anal. Biochem. 74:1976;189-197.
23. Habig W.H., Pabst M.J., Jakoby W.B. Glutathione-S-transferase: the first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249:1974;7130-7139.
24. 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.
25. Egan T.J., Ross D.C., Adams P.A. Quinoline anti-malarial drugs inhibit spontaneous formation of β-haematin (malaria pigment). FEBS. Lett. 352:1994;54-57.
26. Ferrari V., Cutler D.J. Simulation of kinetic data on the influx and efflux of chloroquine by erythrocytes infected with Plasmodium falciparum-Evidence for a drug-importer in chloroquine-sensitive strains. Biochem. Pharmacol. 1991;42, suppl S167-S179.
27. Howells R.E., Peters W., Thomas E.A. The chemotherapy of rodent malaria-III: Host-parasite relationship, part 3. The relationship between haemozoin formation and the age of the host cell. Ann. Trop. Med. Parasitol. 62:1968;267-269.
28. Dei-Cas E., Slomianny C., Prensier G. Action préférentielle de la chloroquine sur les Plasmodium hébergés dans des hématies matures. Pathol. Biol. 32:1984;1019-1023.
29. Charet P., Dei-Cas E., Prensier G., Moreau S., Slomianny C., Vernes A. Plasmodium resistance to chloroquine: a new hypothesis. Trans. Roy. Soc. Trop. Med. Hyg. 79:1985;140.
30. Harvey J.W., Beutler E. Binding of heme by glutathione S-transferase: a possible role of the erythrocyte enzyme. Blood. 60:1982;1227-1230.
31. Sugiyama Y., Sugimoto M., Stolz A., Kaplowitz N. Comparison of the binding affinities of five forms of rat glutathione S-transferases for bilirubin, sulfobromophtalein and hematin. Biochem. Pharmacol. 33:1984;3511-3513.
32. Takikawa H., Sugiyama Y., Stolz Y., Sugimoto M., Kaplowitz N. Organic anion-binding by human hepatic GSH S-transferase. Biochem. Pharmacol. 35:1986;354-356.
33. Shviro Y., Shaklai N. Glutathione as a scavenger of free hemin-A mechanism of preventing red cell membrane damage. Biochem. Pharmacol. 36:1987;3801-3807.
34. Wood P., Rock L.M., Eaton J.W. Chloroquine resistance and host cell hemoglobin catabolism in Plasmodium berghei. Prog. Clin. Biol. Res. 155:1984;159-169.
35. Fitch D.C., Chou A.C. Regulation of polymerizing activity and the antimalarial action of chloroquine. Antimicrob. Agents Chemother. 41:1997;2461-2465.
36. Srivastava P., Pandey V.C. Heme oxygenase and related indices in chloroquine-resistant and -sensitive strains of Plasmodium berghei. Int. J. Parasitol. 25:1995;1061-1064.
37. Atamna H., Ginsburg H. The malaria parasite supplies glutathione to its host cell. Eur. J. Biochem. 250:1997;670-679.