Toxicity of malathion to nile tilapia, Oreochromis niloticus and modulation by other environmental contaminants

Aquatic Toxicology

Volumn 43, Issue 4, 1998, Pages 261-271

  Pathiratne, Asoka ^a   George, Stephen G ^b  

^a UNIVERSITY OF KELANIYA   (Sri Lanka)

^b UNIVERSITY OF STIRLING   (United Kingdom)

Author keywords

Acetylcholinesterase; Carboxylesterase; Cytochrome P 450; Enzyme induction; Glutathione S transferase; Insecticide toxicity; Malathion toxicity; Tilapia

Indexed keywords

16ALPHA CYANOPREGNENOLONE; 3 METHYLCHOLANTHRENE; CADMIUM CHLORIDE; CYTOCHROME P450; ENZYME; MALATHION; PIPERONYL BUTOXIDE; POLYCYCLIC AROMATIC HYDROCARBON; TRANS STILBENE OXIDE;

ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DRUG INTERACTION; DRUG METABOLISM; DRUG TOXICITY; ENZYME INDUCTION; NONHUMAN; PRIORITY JOURNAL; TILAPIA; WATER POLLUTION;

OREOCHROMIS NILOTICUS; TILAPIA;

EID: 0031791295     PISSN: 0166445X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-445X(98)00059-9     Document Type: Article

References (49)

1. Burke M.D., Mayer R.T. Ethoxyresorufin: direct fluorimetric assay of a microsomal O-dealkylation which is preferentially inducible by 3-methylcholanthrene. Drug Metab. Disp. 2:1974;583-588.
2. Celander M., Ronis M., Forlin L. Initial characterisation of a constitutive cytochrome P450 isoenzyme in rainbow trout liver. Mar. Environ. Res. 28:1989;9-13.
3. Celander M., Buhler D.R., Forlin L., Goksoyr A., Miranda C.L., Woodin B., Stegeman J.J. Immunochemical relationships of cytochrome P4503A-like proteins in teleost fish. Fish Physiol. Biochem. 15:1996;323-332.
4. Chambers, J.E., 1991. Bioactivation of Organophosphorus insecticides in mammalian target and non target tissue. In: Hodgson, E., Roe R.M., Motoyama, N. (Eds.), Pesticides and the Future: Toxicological Studies of Risks and Benefits. Reviews in Pesticide Toxicology I. North Carolina State University, NC, pp. 83-90.
5. Clarke, A.G., 1990. The glutathione S-transferases and resistance to insecticides. In: Hayes, J.D., Pickett, C.B., Mantle, T.J. (Eds.), Glutathione S-Transferase and Drug Resistance. Taylor and Francis, London, pp. 369-378.
6. Cohen S.D., Murphy S.D. Carboxylesterase inhibition as an indicator of malathion potentiation in mice. J. Pharmacol. Exp. Therap. 176:1971;733-742.
7. Cohen S.D. Mechanisms of toxicological interactions involving organophosphate insecticides. Fundam. Appl. Toxicol. 4:1980;315-324.
8. Dauterman W.C., Main A.R. Relationship between acute toxicity and in vitro inhibition and hydrolysis of a series of carbalkoxy homologues of malathion. Toxicol. Appl. Pharmacol. 9:1966;408-418.
9. Ellman G. L, Courtney K.D., Andreas V., Featherstone R.M. A new and rapid colorimetric determination of cholinesterase activity. Biochem. Pharmacol. 7:1961;88-95.
10. Erickson D.A., Goodrich M.S., Lech J.J. The effects of piperonyl butoxide on hepatic cytochrome P-450 dependent monooxygenase activity in rainbow trout (Salmo gairdneri). Toxicol. Appl. Pharmacol. 94:1988;1-10.
11. Fest, C., Schmidt, K.J., 1982. The Chemistry of organophosphorous pesticides. Springer-Verlag, Berlin, pp. 360.
12. Finney, D.J., 1971. Probit Analysis. Cambridge University Press, London, pp. 333.
13. Gantverg A.N., Rozengart V.I. The rate of malathion degradation in the liver of fish in vitro. J. Ichthyol. 24:1984;161-162.
14. George S.G., Young P. The time course of effects of cadmium and 3-methylcholanthrene on activities of enzymes of xenobiotic metabolism and metallothionein levels in the plaice Pleuronectes platessa. Comp. Biochem. Physiol. 83:1986;87-94.
15. George S., Buchanan G., Nimmo I., Hayes J. Fish and mammalian liver cytosolic glutathione S-transferases: substrate specificities and immunological comparison. Mar. Environ. Res. 28:1990;41-46.
16. George, S.G., 1994. Enzymology and molecular biology of phase II xenobiotic conjugating enzymes in fish. In: D.C. Malins, D.C., Ostrander, G.K. (Eds.), Aquatic Toxicology, Molecular Biochemical and Cellular Perspectives. Lewis Publishers, Boca Raton, pp. 37-85.
17. Habig W.H., Pabst M.J., Jackoby W.B. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249:1974;7130-7135.
18. Heymann E., Menthein R. Carboxylesterases-Amidases. Meth. Enzymology. 77:1981;333-345.
19. Hodgson E., Rose R.L., Goh D.K.S., George C.R., Roe R.M. Insect cytochrome P-450: metabolism and resistance to insecticides. Biochem. Soc. Trans. 21:1993;1060-1065.
20. Hollingworth, R.M., 1976. The biochemical and physiological basis of selective toxicity. In: Wilkinson, C.F. (Ed.), Pesticide Biochemistry and Physiology. Plenum Press, New York, p. 471-497.
21. Ketterer, B., Meyer, D., Clark, A., 1988. Soluble glutathione transferase isoenzymes. In: Sies, H. and Ketterer, B. (Ed.), Glutathione Conjugation. Academic Press, London, pp. 74-135.
22. Ketterman A.J., Pond S.M., Becker C.E. The effects of differential induction of cytochrome P-450 carboxylesterase and glutathione S-transferase activities on malathion toxicity in mice. Toxicol. Appl. Pharmacol. 87:1987;389-392.
23. Kleinow K., Haasch M.L., Williams D., Lech J.J. A comparison of hepatic P-450 induction in rat and trout (Onchorynchus mykiss): delineation of the site of resistance of fish to phenobarbital-type inducers. Comp. Biochem. Physiol. 96C:1990;259-270.
24. Kumar K., Ayyappan S., Murjani G. Eradication of the predatory insect Anisops sp. (Notonectidae) in freshwater fish ponds using malathion. J. Aquacult. Trop. 8:1993;245-248.
25. Leaver M.J., Pirrit L., George S.G. Cytochrome P450IA1 cDNA from plaice (Pleuronectes platessa) and induction of P450IA1 mRNA in various tissues by 3-methylcholanthrene and isosafrole. Mar. Mol. Biol. Biotech. 2:1993;338-345.
26. Leaver M.J., Scott K., George S.G. Cloning and characterisation of the major hepatic glutathione S-transferase from a marine teleost flatfish, the plaice (Pleuronectes platessa) with structural similarities to plant, insect and mammalian θ class isoenzymes. Biochem. J. 292:1993;189-195.
27. Leaver M.J., Wright J., George S.G. Structure and expression of a cluster of glutathione S-transferase genes from a marine fish, the plaice (Pleuronectes platessa). Biochem. J. 321:1997;405-412.
28. Lewis, D.F.V, 1996. Cytochromes P-450: Structure, Function, and Mechanism, Taylor and Francis, London, pp. 349.
29. Lowry O.H., Rosebrough A.L., Farr A.L., Randall R.J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:1951;265-267.
30. Mani V.G.T., Konar S.K. Acute toxicity of malathion to fish, plankton and worm. Environ. Ecol. 2:1984;248-250.
31. Mannervik B. The isoenzymes of glutathione S-transferase. Adv. Enzymol. 57:1985;357-417.
32. Meyer D., Coles B., Pemble S.E., Gilmore K.S., Fraser G.M., Ketterer B. θ, a new class of glutathione transferases purified from rat and man. Biochem. J. 274:1991;409-414.
33. Motoyama, N., Nishizawo, Y., Nagakura, A., Takemara, T., Dauterman, W.C., 1991. Selective inhibition of the cytochrome P-450 dependent monooxygenases from the rat liver and house fly abdomen. In: Hodgson, E., Roe, R.M., Motoyama, N. (Eds.), Reviews in Pesticide Toxicology I. North Carolina State University, NC.
34. Mouches C., Pasteur N., Berge J., Hyrien O., Raymond M., Saint Vincent B., Silvestri M., Giorghiou G. Amplification of an esterase gene is responsible for insecticide resistance in the California Culex mosquito. Science. 233:1986;778-780.
35. Mount D.I., Stephen C.E. A method for establishing acceptable toxicant limits for fish-malathion and butoxy-ethanol ester of 2,4-D. Trans. Am. Fish Soc. 21:1967;185-193.
36. Murphy S.D., Lauwery R.P., Cheever K.L. Comparative anticholinesterase action of organophosphorus insecticides in vertebrates. Toxicol Appl. Pharmacol. 12:1968;22-35.
37. Newman S.L., Guzelian P.S. Identification of the cyanopregnenolone inducible form of hepatic cytochrome P-450 as a catalyst of Aldrin epoxidation. Biochem. Pharmacol. 32:1983;1529-1531.
38. Omura T., Sato R. The carbon monoxide binding pigment of liver microsomes II: solubilisation, purification and properties. J. Biol. Chem. 239:1964;2379-2385.
39. Pathiratne A., George S.G. Comparison of xenobiotic metabolising enzymes of tilapia with those of other fish species and interspecies relationships between gene families. Mar. Environ. Res. 42:1996;293-296.
40. Reidy G.F., Rose H.A., Stacey N.H. Effect of length of exposure to malathion on xenobiotic biotransformation in male rat liver. Toxicol. Lett. 38:1987;193-199.
41. Reish D.J., Oshida P.S. Manual of methods in aquatic environment research. Part 10. Short term static Bioassays. FAO Fish Tech. Pap. 247:1986;62.
42. Scott K., Leaver M., George S. Regulation of glutathione S-transferase A expression in flounders. Mar. Environ. Res. 34:1992;233-236.
43. Seume F.W., O'Brien R.D. Metabolism of malathion by rat tissue preparations and its modification by EPN. J. Agr. Food Chem. 8:1960;36-41.
44. Shao-Nan L., De-Fang F. Correlation between biochemical parameters and susceptibility of freshwater fish to malathion. J. Toxicol. Environ. Health. 48:1996;413-418.
45. Stegeman, J.J., Hahn, M.E., 1994. Biochemistry and Molecular biology of monooxygenases, current perspectives on forms, functions and regulation of cytochrome P-450 in aquatic species. In: Malins, D.C., Ostrander, G.K. (Eds.), Aquatic Toxicology, Molecular, Biochemical and Cellular Perspectives. Lewis Publishers, Boca Raton, pp. 87-206.
46. Talcott R. Hepatic and extrahepatic malathion carboxylesterases assay, localization in the rat. Toxicol Appl. Pharmacol. 47:1979;145-150.
47. Townsend B.A., Carlson G.P. Effect of halogenated benzenes on the toxicity and metabolism of malathion, parathion and paraoxon in mice. Toxicol. Appl. Pharmacol. 60:1981;52-61.
48. Wang J.-Y., McCommas S., Syvanen M. Molecular cloning of a glutathione S-transferase overproduced in an insecticide resistant strain of the housefly (Musca domestica). Mol. Gen. Genet. 227:1991;260-266.
49. Wilkinson C.F., Murray M., Marcus C.B. Interactions of methylenedioxyphenyl compounds with cytochrome P-450 and effects of microsomal oxidation. Rev. Biochem. Toxicol. 6:1984;27-63.