Fate of haem iron in the malaria parasite Plasmodium falciparum

Biochemical Journal

Volumn 365, Issue 2, 2002, Pages 343-347

  Egan, Timothy J ^a   Combrinck, Jill M ^a   Egan, Joanne ^a   Hearne, Giovanni R ^b   Marques, Helder M ^b   Ntenteni, Skhumbuzo ^b   Sewell, B Trevor ^a   Smith, Peter J ^a   Taylor, Dale ^a   Van Schalkwyk, Donelly A ^a   Walden, Jason C ^a  

^a UNIVERSITY OF CAPE TOWN   (South Africa)

^b UNIVERSITY OF THE WITWATERSRAND   (South Africa)

Author keywords

Electron spectroscopic imaging; Haemozoin; M ssbauer spectroscopy

Indexed keywords

CHEMICAL ANALYSIS; ELECTRON SPECTROSCOPY; IRON;

MALARIAL PARASITE;

BIOCHEMISTRY;

HEME; HEMOZOIN; IRON;

ARTICLE; CHEMICAL ANALYSIS; CONTROLLED STUDY; ERYTHROCYTE; MALARIA; MOSSBAUER SPECTROSCOPY; NONHUMAN; PLASMODIUM FALCIPARUM; PRIORITY JOURNAL; TRANSMISSION ELECTRON MICROSCOPY; TROPHOZOITE;

ANIMALS; HEME; HEMEPROTEINS; IRON; PLASMODIUM FALCIPARUM; SPECTROSCOPY, MOSSBAUER;

PLASMODIUM FALCIPARUM; PROTOZOA;

EID: 0037101785     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20020793     Document Type: Article

References (28)

1. Aikawa, M., Hepler, P. K., Huff, C. G. and Sprinz, H. (1966) Feeding mechanisms of avian malarial parasites. J. Cell Biol. 28, 355-373
2. Banerjee, R., Liu, J., Beatty, W., Pelosof, L., Klemba, M. and Goldberg, D. E. (2002) Four plasmepsins are active in the Plasmodium falciparum food vacuole, including a protease with an active-site histidine. Proc. Natl. Acad. Sci. U.S.A. 99, 990-995
3. Brown, W. H. (1911) Malarial pigment (so-called melanin): its nature and mode of production. J. Exp. Med. 13, 290-299
4. Pagola, S., Stephens, P. W., Bohle, D. S., Kosar, A. D. and Madsen, S. K. (2000) The structure of malaria pigment (β-haematin). Nature (London) 404, 307-310
5. Ginsburg, H., Famin, O., Zhang, J. and Krugliak, M. (1998) Inhibition of glutathione-dependent degradation of heme by chloroquine and amodiaquine as a possible basis for their antimalarial mode of action. Biochem. Pharmacol. 56, 1305-1313
6. Loria, P., Miller, S., Foley, M. and Tilley, L. (1999) Inhibition of the peroxidative degradation of haem as the basis of action of chloroquine and other quinoline antimalarials. Biochem. J. 339, 363-370
7. Mungthin, M., Bray, P. G., Ridley, R. G. and Ward, S. A. (1998) Central role of hemoglobin degradation in mechanisms of action of 4-aminoquinolines, quinoline methanols, and phenanthrene methanols. Antimicrob. Agents Chemother. 42, 2973-2977
8. Bray, P. G., Mungthin, M., Ridley, R. G. and Ward, S. A. (1998) Access to hematin: the basis of chloroquine resistance. Mol. Pharmacol. 54, 170-179
9. Slater, A. F. G. and Cerami, A. (1992) Inhibition by chloroquine of a novel haem polymerase enzyme activity in malaria trophozoites. Nature (London) 355, 167-169
10. Egan, T. J., Ross, D. C. and Adams, P. A. (1994) Quinoline anti-malarial drugs inhibit spontaneous formation of β-haematin (malaria pigment). FEBS Lett. 352, 54-57
11. Dorn, A., Stoffel, R., Matile, H., Bubendorf, A. and Ridley, R. G. (1995) Malarial haemozoin/β-haematin supports haem polymerization in the absence of protein. Nature (London) 374, 269-271
12. Sullivan, D. J., Gluzman, I. Y., Russell, D. G. and Goldberg, D. E. (1996) On the molecular mechanism of chloroquine's antimalarial action. Proc. Natl. Acad. Sci. U.S.A. 93, 11865-11870
13. Trager, W. and Jensen, J. B. (1976) Human malaria parasites in continuous culture. Science 193, 673-675
14. Lambros, C. and Vanderberg, J. P. (1979) Synchronisation of Plasmodium falciparum erythrocyte stages in culture. J. Parasitol. 65, 418-420
15. Aley, S. B., Sherwood, J. A., Marsh, K., Eidelman, O. and Howard, R. J. (1986) Identification of isolate-specific proteins on sorbitol-enriched Plasmodium falciparum infected erythrocytes from Gambian patients. Parasitology 92, 511-525
16. Saliba, K. J., Folb, P. I. and Smith, P. J. (1998) Role for the Plasmodium falciparum digestive vacuole in chloroquine resistance. Biochem. Pharmacol. 56, 313-320
17. Carter, P. (1971) Spectrophotometric determination of serum iron at the submicrogram level with a new reagent (ferrozine). Anal. Biochem. 40, 450-458
18. Blume, M. (1967) Temperature-dependent spin-spin relaxation times: Application to the Mössbauer spectra of ferric hemin. Phys. Rev. Lett. 18, 350-358
19. Egerton, R. F. (1996) Electron Energy-Loss Spectroscopy in the Electron Microscope, 2nd edn, Plenum Press, New York, NY
20. Greendyke, R. M., Meriwether, W. A., Thomas, E. T., Flintjer, J. D. and Bayliss, M. W. (1962) Suggested revision of normal values for haemoglobin, haematocrit, and erythrocyte count in healthy adult men. Am. J. Clin. Pathol. 37, 429-436
21. Krugliak, M., Zhang, J. and Ginsburg, H. (2002) Intraeryrthrocytic Plasmodium falciparum utilises only a fraction of the amino acids derived from digestion of host cell cytosol for the biosynthesis of its proteins. Mol. Biochem. Parasitol. 119, 249-256
22. Adams, P. A., Egan, T. J., Ross, D. C., Silver, J. and Marsh, P. J. (1996) The chemical mechanism of β-haematin formation studied by Mössbauer spectroscopy. Biochem. J. 318, 25-27
23. 57Fe: metal, alloys, and inorganic compounds. In Chemical Applications of Mössbauer Spectroscopy (Goldanskii, V. I. and Herber, R. H., eds.), pp. 159-267, Academic Press, New York, NY
24. Moshkovskii, Y. S. (1968) Applications of the Mössbauer effect in biology. In Chemical Applications of Mössbauer Spectroscopy (Goldanskii, V. I. and Herber, R. H., eds.), pp. 524-547, Academic Press, New York, NY
25. Beckers, A. L. D., De Bruijn, W. C., Gelsema, E. S., Cleton-Soeteman, M. I. and Van Eijk, H. G. (1994) Quantitative electron spectroscopic imaging in bio-medicine: methods for image acquisition, correction and analysis. J. Microsc. 174, 171-182
26. O'Keeffe, D. H., Barlow, C. H., Smythe, G. A., Fuchsman, W. H., Moss, T. H., Lilienthal, H. R. and Caughey, W. S. (1975) Magnetic and spectroscopic probes for FeOFe linkages in hemin systems. Bioinorg. Chem. 5, 125-147
27. Marques, H. M., Munro, O. Q., Munro, T., de Wet, M. and Vashi, P. R. (1999) Coordination of N-donor ligands by the monomeric ferric porphyrin N-acetylmicroperoxidase-8. Inorg. Chem. 38, 2312-2319
28. Bauminger, E. R., Akkawi, M. and Blauer, G. (1999) Mössbauer studies of different types of hematin. Inorg. Chim. Acta 286, 229-232