Abstract
Biochemical changes produced by luxabendazole in muscle-stageTrichinella spiralis larvae consisted of a decrease in free glucose and glycogen levels (46.71% and 35.66%, respectively) after in vivo treatment, slight in vitro inhibition of fumarate reductase activity (24.15%) and, finally, inhibition of [3H]-colchicine-tubulin binding, which was found to be of a competitive nature, with an inhibition constant (Ki) of 0.9×10−7 M. In a parallel study, luxabendazole did not appear to be inhibitory to [3H]-colchicine binding to pig-brain tubulin.
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References
Barrett J (1978) Activation of succinate dehydrogenase from adultFasciola hepatica (Trematoda). Parasitology 76:269–275
Borgers M, Nollin A de, Verheyen A, Brabander M de, Thienpont D (1975) Effects of new anthelmintics on the microtubular system of parasites. In: Microtubules and microtubule inhibitors. North Holland. Amsterdam, pp 497–508
Bossche H van den (1972) Biochemical effects of the anthelmintic drug mebendazole. In: Bossche H van den (ed) Comparative Biochemistry of parasites. Academic Press, New York London, pp 139–158
Bryant C, Bennet E (1983) Observations on the fumarate reductase system inHaemonchus contortus and their relevance to anthelmintic resistance and to strain variations of energy metabolism. Mol Biochem Parasitol 7:281–292
Comley JCW, Wright DJW (1981) Succinate dehydrogenase and fumarate reductase activity inAspiculuris tetraptera andAscaris suum and the effects of the anthelmintics cambendazole, thiabendazole and levamisole. Int J Parasitol 11:79–84
Corba J, Hovorka J, Spaldonova R, Stoffa P, Legeny J, Andrasko H (1987) Efficacy of luxabendazole (Hoe 216 V) susp. 5% in sheep naturally infected with the most important helminths. Helminthologia 24:227–235
Criado A, Rodriguez E, Jimenez A (1987) The mode of action of some benzimidazole drugs onTrichinella spiralis. Parasitology 95:61–70
Friedman PA, Platzer EG (1980) Interaction of anthelmintic benzimidazoles withAscaris suum embryonic tubulin. Biochim Biophys Acta 630:271–278
Friedman PA, Platzer EC, Carrol EJ (1980) Tubulin characterization during embryogenesis ofAscaris suum. Biochem Pharmacol 28:2680–2682
Grzywinski L, Karmanska K (1988) Efficacy of luxabendazole against different stages ofTrichinella spiralis. Proceedings of the 7th International Conference on Trichinellosis. Alicante, Spain, October 2–6, pp 144
Kassai T, Takats C, Fok E, Redl P (1988) Activity of luxabendazole against liver flukes, gastrointestinal roundworm and lungworms in naturally infected sheep. Parasitol Res 75:14–18
Köhler P, Bachmann R (1978) The effects of antiparasitic drugs levamisole, thiabendazole, praziquantel and chloroquine on mitochondrial electron transport in muscle tissue fromAscaris suum. Mol Pharmacol 14:155–163
Köhler P, Bachmann R (1984) Helminth tubulin and the action of benzimidazole carbamate drugs. Zentralbl Bakteriol Mikrobiol Hyg [A] 258:426–427
Lacey E (1988) The role of the cytoskeletal protein, tubulin, in the mode of action and mechanism of drug resistance to benzimidazoles. Int J Parasitol 18:885–936
Lowry O, Rosebrough N, Farr A, Randall R (1951) Protein measurement with the folin phenol reagent. J Biol Chem 193:265–275
Nollin S de, Bossche H van den (1973) Biochemical effects of mebendazole onTrichinella spiralis larvae. J Parasitol 59:970–976
Prichard RK (1973) The fumarate reductase reaction ofHacmonchus contortus and the mode of action of some anthelmintics. Int J Parasitol 3:409–417
Rodriguez F, Criado A, Jimenez A (1985) A comparative study of the succinate dehydrogenase-fumarate reductase complex in the genusTrichinella. Parasitology 91:577–583
Sangster NC, Prichard RK (1984) Uptake of thiabendazole and its effects on glucose uptake and carbohydrate levels in the thiabendazole-resistant and-susceptibleTrichostrongylus colubriformis. Int J Parasitol 14:121–126
Shelanski ML, Gaskin F, Contor CR (1973) Microtubule assembly in the absence of added nucleotides. Proc Natl Acad Sci USA 70:765–768
Sherline P, Bodwin C, Kipnis DM (1974) A new colchiome binding assay for tubulin. Anal Biochem 52:400–407
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Criado-Fornelio, A., de Armas-Serra, C., Jimenez-Gonzalez, A. et al. Biochemical effects of luxabendazole onTrichinella spiralis . Parasitol Res 76, 518–520 (1990). https://doi.org/10.1007/BF00931057
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DOI: https://doi.org/10.1007/BF00931057