Hostname: page-component-78c5997874-4rdpn Total loading time: 0 Render date: 2024-11-02T20:00:40.377Z Has data issue: false hasContentIssue false
  • English
  • Français

Damage to malaria-infected erythrocytes following exposure to oxidant-generating systems

Published online by Cambridge University Press:  06 April 2009

Anne O. Wozencraft
Anne O. Wozencraft
Affiliation:
Department of Tropical Hygiene, London School of Hygiene and Tropical Medicine, Keppel Street, London WC1E 7HT
Get access Rights & Permissions [Opens in a new window]

Summary

A study has been made of the damage incurred by normal and Plasmodium falciparum-infected human erythrocytes following exposure to a variety of oxidant-generating systems. Hydrogen peroxide, produced by the glucose–glucose oxidase system, increased methaemoglobin formation within normal erythrocytes while normal levels of oxyhaemoglobin were maintained. Exposure to products of the xanthine–xanthine oxidase interaction did not have the same effect. Malondialdehyde measurements indicated that the host cell membranes of parasitized cells had undergone lipid peroxidation even before exposure to the oxidant-generating systems. Lipid peroxidation of normal and parasitized cell membranes was increased upon exposure to reagent-grade hydrogen peroxide and alloxan: this increase was not observed following exposure to the two enzyme–substrate systems that generated reactive oxygen intermediates. In addition, the effects of parasitism on intracellular levels of catalase and superoxide dismutase were assessed. Normal and parasitized erythrocytes were found to possess similar levels of these enzymes, which protect against oxidant-induced damage. It was therefore concluded that the increased susceptibility of infected cells to oxidant damage was probably not related to any decrease in the function of these enzymes.

Type
Research Article
Information
Parasitology , Volume 92 , Issue 3 , June 1986 , pp. 559 - 567
Copyright
Copyright © Cambridge University Press 1986

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Aebi, H. (1982). Catalase. In Methods of Enzymatic Analysis, vol.2, (eBergmeyer, d. H. N.) pp. 673–783. New York: Academic Press.Google Scholar
Beauchamp, C. & Fridovich, J. (1971). Superoxide dismutase: improved assays, and an assay applicable to acrylamide gels. Analytical Biochemistry 44, 276–87.CrossRefGoogle Scholar
Clark, I. A., Cowden, W. B. & Butcher, G. A. (1983). Free radical generates as antimalarial drugs. Lancet 1, 234.CrossRefGoogle ScholarPubMed
Clark, I. A., Cowden, W. B., Hunt, N. H., Maxwell, L. E. & Mackie, E. J. (1984 b). Activity of divicine in Plasmodium vinckei-infected mice has implications for treatment of favism and epidemiology of G6PD deficiency. British Journal of Haematology 57, 479–87.CrossRefGoogle Scholar
Clark, I. A. & Hunt, N. N. (1983). Evidence for reactive oxygen intermediates causing hemolysis and parasite death in malaria. Infection and Immunity 39, 1–6.CrossRefGoogle ScholarPubMed
Clark, I. A., Hunt, N. H., Cowden, W. B., Maxwell, L. E. & Mackie, E. J. (1984 a). Radical-mediated damage to parasites and erythrocytes in Plasmodium vinckei-infected mice after injection of t-butyl hydroperoxide. Clinical and Experimental Immunology. 56, 524–30.Google ScholarPubMed
Dockrell, H. M., De Souza, J. B. & Playfair, J. H. L. (1980). The role of the liver in immunity to blood-stage murine malaria. Immunology 41, 421–30.Google ScholarPubMed
Etkin, N. L. & Eaton, J. W. (1975). Malaria-induced erythrocyte oxidant sensitivity. In Erythrocyte Structure and Function, vol. 1. (ed. Brewer, G. J.), pp. 219–32. New York: A. R. Liss.Google Scholar
Fairfield, A. S., Meshnick, S. R. & Eaton, J. W. (1983). Malaria parasites adopt host cell superoxide dismutase. Science 221, 764–6.CrossRefGoogle ScholarPubMed
Fee, J. A., Bergamuri, R. & Briggs, R. G. (1975). Observations on the mechanisms of the oxygen/dialuric acid-induced haemolysis of Vit. E-deficient rat blood cells and the protective roles of catalase and superoxide dismutase. Archives of Biochemistry and Biophysics 169, 160–7.CrossRefGoogle Scholar
Friedman, M. J. (1979). Oxygen damage mediates variant red cell resistance to malaria. Nature, London 280, 245–7.CrossRefGoogle ScholarPubMed
Halliwell, B. & Gutteridge, J. M. C. (1984). Lipid peroxidation, oxygen radicals, cell damage and antioxidant therapy. Lancet 1, 1396–7.CrossRefGoogle ScholarPubMed
Hommel, M. (1985). Antigenic variation in malaria parasites. Immunology Today 6, 28–33.CrossRefGoogle ScholarPubMed
Kellogg, E. W. III & Fridovich, I. (1975). Superoxide, hydrogen peroxide and singlet oxygen in lipid peroxidation by a xanthine oxidase system. Journal of Biological Chemistry 250, 8812–17.CrossRefGoogle ScholarPubMed
Knight, A. & Sinden, R. E. (1982). The purification of gametocytes of Plasmodium falciparum and Plasmodium yoelii nigeriensis by colloidal silica gradient centrifugation. Transactions of the Royal Society of Tropical Medicine and Hygiene 76, 503–9.CrossRefGoogle Scholar
Ockenhouse, C. F., Schulman, S. & Shear, H. L. (1984). Induction of crisis forms in the human malaria parasite Plasmodium falciparum by γ-interferon-activated, monocyte-derived macrophages. Journal of Immunology 133, 1601–8.CrossRefGoogle ScholarPubMed
Picard-Maureau, A., Hempelmann, E., Krammer, G., Jackisch, R. & Jung, A. (1975). Glutathion Status in Plasmodium vinckei parasitienten Erythrozyten in Abhangigkeit vom intraerythrozytaren Entiockhingstadium des Parasiten. Tropenmedizin und Parasitologie 26, 405–16.Google Scholar
Schirmer, R. H., Lederbogen, F., Eisenbrand, G., Koniok, E. & Jung, A. (1984). Inhibitors of glutathione reductase as potential antimalarial drugs. Parasitology 89, i.Google Scholar
Sharma, O. P., Shukla, R. P., Singh, C. & Sew, A. B. (1979). Alterations in some biochemical parameters in mouse liver and spleen during infection with Plasmodium berghei. Indian Journal of Medical Research 69, 944–8.Google ScholarPubMed
Sherman, I. W. (1979). Biochemistry of Plasmodium (malarial parasites). Microbiological Reviews 43, 435–95.CrossRefGoogle ScholarPubMed
Sinnhuber, R. O. & Yu, T. C. (1958). 2-thiobarbituric acid method for the measurement of rancidity in fishery products. Food Technology 12, 9–14.Google Scholar
Van Kampen, E. J. & Zijlstra, W. G. (1961). Standardisation of hemoglobinometry. II. The hemoglobin-cyanide method. Clinica chimica acta 6, 538–45.CrossRefGoogle Scholar
Weiss, S. J. (1982). Neutrophil-mediated methemoglobin formation in the erythrocyte. Journal of Biological Chemistry 257, 2947–53.CrossRefGoogle ScholarPubMed
Winterbourn, C. C., Hawkins, R. E., Brian, M. & Carewell, R. W. (1975). The estimation of red cell superoxide dismutase activity. Journal of Laboratory and Clinical Medicine 85, 337–41.Google ScholarPubMed
Wozencraft, A. O., Dockrell, H. M., Taverne, J., Targett, G. A. T. & Playfair, J. H. L. (1984). Killing of human malaria parasites by macrophage secretory products. Infection and Immunity 43, 664–9.CrossRefGoogle ScholarPubMed