Hostname: page-component-78c5997874-m6dg7 Total loading time: 0 Render date: 2024-11-18T17:48:58.437Z Has data issue: false hasContentIssue false
  • English
  • Français

Glutathione peroxidase (EC 1.11.1.9) and superoxide dismutase (EC 1.15.1.1) activities in riboflavin-deficient rats infected with Plasmodium berghei malaria

Published online by Cambridge University Press:  09 March 2007

D. A. Adelekan  and
D. I. Thurnham
D. A. Adelekan*
Affiliation:
Department of Community Health, Faculty of Clinical Sciences, College of Health Sciences, Obafemi Awolowo University, Ile-lfe, Nigeria
D. I. Thurnham
Affiliation:
Northern Ireland Centre for Diet and Health, School of Biomedical Sciences, University of Ulster, Coleraine BT52 1SA, UK
*
*Corresponding author:Dr D. A. Adelekan, email adel@chs.oauife.edu.ng and dadeleka@oauife.edu.ng
Rights & Permissions [Opens in a new window]

Abstract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

Riboflavin deficiency interferes with the growth and multiplication of malaria parasites as well as the host response to malaria. The objective of the present work was to determine the effects of riboflavin deficiency on erythrocyte glutathione peroxidase (EC 1.11.1.9; GPx) and superoxide dismutase (EC 1.15.1.1; SOD) in rats infected with Plasmodium berghei malaria. Riboflavin in its co-enzyme form, FAD, is required by glutathione reductase (EC 1.6.4.1) to regenerate GSH and GSH is an important cellular antioxidant both in its own right and also as a substrate for the enzyme GPx. Weanling rats were deprived of riboflavin for 8 weeks before intraperitoneal injection of 1 × 106P. berghei parasites. Control animals were weight-matched to the respective riboflavin-deficient group. At 10d post-infection, parasite counts were higher in the weight-matched control group than the riboflavin-deficient group (P = 0.004). GPx activity was higher in erythrocytes of rats parasitized with P. berghei than comparable non-infected rats regardless of riboflavin status (P < 0.05). As mature erythrocytes do not synthesize new protein, the higher GPx activities were probably due to the presence of the parasite protein. In erythrocytes from riboflavin-deficient rats, GPx activity tended to be lower than in those rats fed on diets adequate in riboflavin (weight-matched controls) whether parasitized or not, but the difference was not significant. Neither riboflavin deficiency nor malaria had any effect on erythrocyte SOD activity. It was concluded that riboflavin deficiency has no marked effect on erythrocyte GPx or SOD activity in the rat.

Keywords

RiboflavinMalariaGlutathione peroxidaseSuperoxide dismutase
Type
Research Article
Information
British Journal of Nutrition , Volume 79 , Issue 3 , March 1998 , pp. 305 - 309
Copyright
Copyright © The Nutrition Society 1998

References

Adelekan, DA & Thurnham, DI (1986) Effects of combined riboflavin and iron deficiency on the haematological status and tissue iron concentrations of the rat. Journal of Nutrition 116, 1257–1265.CrossRefGoogle ScholarPubMed
Anon. (1984) Riboflavin deficiency inhibits multiplication of malarial parasites. Nutrition Reviews 42, 195–196.Google Scholar
Areekul, S & Boonme, Y (1987) Superoxide dismutase and catalase activities in red cells of patients with Plasmodium falciparum. Journal of the Medical Association of Thailand 70, 127–130.Google ScholarPubMed
Bates, CJ (1987) Human riboflavin requirements, and metabolic consequences of deficiency in man and animals. World Review of Nutrition and Dietetics 50, 215–265.CrossRefGoogle Scholar
Clark, IA, Cowden, WB & Butcher, GA (1983) Free oxygen radicals in malaria. Lancet i, 234.CrossRefGoogle Scholar
Clark, IA, Cowden, WB, Hunt, NH, Maxwell, LE & Mackie, PJ (1984) Activity of divicine in Plasmodium vinkei-infected mice has implications for treatment of favism and epidemiology of G-6-PD deficiency. British Journal of Haematology 57, 479–487.CrossRefGoogle ScholarPubMed
Clark, IA & Hunt, NH (1983) Evidence for reactive oxygen intermediates causing haemolysis and parasite death in malaria. Infection and Immunity 39, 1–6.CrossRefGoogle ScholarPubMed
Clark, IA, Hunt, NH & Cowden, WB (1986) Oxygen-derived free radicals in the pathogenesis of parasitic disease. Advances in Parasitology 25, 1–44.CrossRefGoogle ScholarPubMed
Das, BS, Das, DB, Satpathy, RN, Patnaik, JK & Bose, TK (1988) Riboflavin deficiency and severity of malaria. European Journal of Clinical Nutrition 42, 277–283.Google ScholarPubMed
Das, BS, Thurnham, DI, Patnaik, JK, Das, DB, Satpathy, RN & Bose, TK (1990) Increased plasma lipid peroxidation in riboflavin-deficient malaria-infected children. American Journal of Clinical Nutrition 51, 859–863.CrossRefGoogle ScholarPubMed
DiSilvestro, RA & Marten, JT (1990) Effects of inflammation and copper intake on rat liver and erythrocyte Cu-Zn superoxide dismutase activity levels. Journal of Nutrition 120, 1223–1227.CrossRefGoogle Scholar
Dutta, P, Pinto, J & Rivlin, S (1985) Antimalarial effects of riboflavin deficiency. Lancet i, 1043–1046.Google Scholar
Fairfield, AS, Aboseh, A, Ranz, A, Eaton, JW & Meshick, SR (1988) Oxidant defense enzymes of Plasmodium falciparum. Molecular and Biochemical Parasitology 30, 77–82.CrossRefGoogle ScholarPubMed
Fairfield, AS, Meshnick, SR & Eaton, JW (1983) Malaria parasites adopt host cell superoxide dismutase. Science 221, 764–766.CrossRefGoogle ScholarPubMed
Fritsch, B, Dieckmann, A, Menze, B, Hempelmann, E, Fritsch, K-G, Fritsch, G & Jung, A (1987) Glutathione and peroxide metabolism in malaria-parasitized erythrocytes. Parasitological Research 73, 515–517.CrossRefGoogle ScholarPubMed
Ganzoni, AM, Barras, JP & Marti, HR (1976) Red cell ageing and death. Vox Sanguinis 30, 161–174.CrossRefGoogle ScholarPubMed
Hassan, FM & Thurnham, DI (1977) Effect of riboflavin deficiency on the metabolism of the red blood cell. International Journal of Vitamin and Nutrition Research 47, 349–355.Google Scholar
Jones, KR, Cottrell, BJ, Targett, GAT & Playfair, JHL (1989) Killing of Plasmodium falciparum by human monocyte derived macrophages. Parasite Immunology 11, 585–592.CrossRefGoogle ScholarPubMed
Kaikai, P & Thurnham, DI (1983) The influence of riboflavin deficiency on Plasmodium berghei infection in rats. Transactions of the Royal Society of Tropical Medicine and Hygiene 77, 680–686.CrossRefGoogle ScholarPubMed
Kelman, SN, Sullivan, SG & Stern, A (1982) Primaquine-mediated oxidative metabolism in the human red cell. Lack of dependency on oxyhemoglobin, H2O2 formation or glutathione turnover. Biochemical Pharmacology 31, 2409–2414.CrossRefGoogle ScholarPubMed
Medical Research Council (1977) Dietary Standards for Laboratory Animals. Surrey, UK: Medical Research Council.Google Scholar
Nagel, RL & Roth, EF Jr (1989) Malaria and red cell genetic defects. Blood 74, 1213–1221.CrossRefGoogle ScholarPubMed
National Research Council (1985) Guide for the Care and Use of Laboratory Animals. Publication no. 85–23 (Rev). Washington, DC: National Institute of Health.Google Scholar
Phillips, RE, Looareesuwan, S, Warrell, DA, Lee, SH, Karbwang, J, Warrell, MJ, White, NJ, Swasdichai, C & Weatherall, DJ (1976) The importance of anaemia in cerebral and uncomplicated falciparum malaria: role of complications, dyserythropoiesis and iron sequestration. Quartery Journal of Medicine 58, 305–323.Google Scholar
Pollack, S, George, JN & Crosby, WH (1966) Effect of agents simulating the abnormalities of the glucose-6-phosphate dehydrogenase-deficient red cell on Plasmodium berghei malaria. Nature 210, 33–35.CrossRefGoogle ScholarPubMed
Seth, RK, Saini, AS & Jaswal, TS (1985) Plasmodium berghei: oxidant defense systems. Experimental Parasitology 60, 414–416.CrossRefGoogle Scholar
Spooner, RJ, Percy, RA & Rumley, AG (1979) The effect of erythrocyte ageing on some vitamin and mineral-dependent enzymes. Clinical Biochemistry 12, 289–290.CrossRefGoogle ScholarPubMed
Stocker, R, Hunt, NH, Buffington, GD, Weidemann, MJ, Lewis-Hughes, PH & Clark, IA (1985) Oxidative stress protective mechanisms in erythrocytes in relation to P. vinckei load. Proceedings of the National Academy of Sciences, USA 82, 548–551.CrossRefGoogle Scholar
Suthipark, U, Krungkrai, J, Jearnpipatkul, A, Yuthavong, Y & Panijpan, B (1982) Superoxide dismutase (SOD) in mouse red blood cells infected with Plasmodium berghei. Journal of Parasitology 68, 337–339.CrossRefGoogle ScholarPubMed
Thurnham, DI, Oppenheimer, SJ & Bull, R (1983) Riboflavin status and malaria in infants in Papua New Guinea. Transactions of the Royal Society of Tropical Medicine and Hygiene 77, 423–424.CrossRefGoogle ScholarPubMed
Wendel, A (1981) Glutathione peroxidase. Methods in Enzymology 77, 325–333.CrossRefGoogle ScholarPubMed
Winterbourn, CC, Hawkins, RE, Brian, M & Carrell, RW (1975) The estimation of red cell superoxide dismutase activity. Journal of Laboratory and Clinical Medicine 85, 337–341.Google ScholarPubMed
Wozencraft, AO, Dockrell, HM, Taverne, J, Targett, GAT & Playfair, JHL (1984) Killing of human macrophage secretory products. Infection and Immunity 43, 664–669.CrossRefGoogle ScholarPubMed