In vivo alterations in glutathione-related processes, lipid peroxidation, and cholinesterase enzyme activities in the liver of diazinon-exposed Oreochromis niloticus

Toxicology Mechanisms and Methods

Volumn 17, Issue 6, 2007, Pages 317-324

  Üner, Nevin ^a   Sevgiler, Yusuf ^a   Durmaz, Hülya ^a   Piner, Petek ^a  

^a CUKUROVA UNIVERSITY   (Turkey)

Author keywords

Cholinesterase; Diazinon; Fish; Glutathione; Lipid Peroxidation; Liver

Indexed keywords

ACETYLCHOLINESTERASE; CHOLINESTERASE; DIMPYLATE; GLUTATHIONE; GLUTATHIONE REDUCTASE; GLUTATHIONE TRANSFERASE; MALONALDEHYDE;

ANALYTIC METHOD; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; ENZYME ACTIVITY; FEMALE; FRESHWATER FISH; LIPID PEROXIDATION; LIVER TOXICITY; MALE; NONHUMAN; OREOCHROMIS NILOTICUS; OXIDATIVE STRESS; PRIORITY JOURNAL; SPECTROPHOTOMETRY;

OREOCHROMIS NILOTICUS;

EID: 34547199626     PISSN: 15376516     EISSN: 15376524     Source Type: Journal    
DOI: 10.1080/15376510601031927     Document Type: Article

References (37)

1. Anderson, M. E. 1985. Determination of glutathione and glutathione disulfide in biological samples. Methods Enzymol. 113:548.
2. APHA, AWWA, and WPCF. 1981. Standard Methods, American Public Health Association, New York, p. 616.
3. Arteel, G. E., and Sies, H. 2001. The biochemistry of selenium and the glutathione system. Environ. Toxicol. Pharmacol. 10:153-158.
4. Banerjee, B. D., Seth, V., Bhattacharya, A., Pasha, S. T., and Chakraborty, A. K. 1999. Biochemical effects of some pesticides on lipid peroxidation and free-radical scavengers. Toxicol. Lett. 107:33-47.
5. Beutler, E. 1984. Red Cell Metabolism: A Manual of Biochemical Methods, 2nd reprint ed., Grune and Straton, New York, p. 133.
6. Carlberg, I., and Mannervik, B. 1975. Purification and characterization of the flavoenzyme glutathione reductase from rat liver. J. Biol. Chem. 250:5475-5480.
7. Chuiko, G. M. 2000. Comparative study of acetylcholinesterase and butyrylcholinesterase in brain and serum of several freshwater fish: specific activities and in vitro inhibition by DDVP, an organophosphorus pesticide. Comp. Biochem. Physiol. 127C:233-242.
8. Cnubben, N. H. P., Rietjens, I. M. C. M., Wortelboer, H., van Zenden, J., and van Bladeren, P. J. 2001. The interplay of glutathione-related processes in antioxidant defence. Environ. Toxicol. Pharmacol. 10:141-152.
9. Durmaz, H., Sevgiler, Y., and Üner, N. 2006. Tissue-specific antioxidative and neurotoxic responses to diazinon in Oreochromis niloticus. Pestic. Biochem. Physiol. 84:215-226.
10. El-Elaimy, I. A., El-Saadawy, M. M., Gabr, S. A., and Sakr, S. A. 1990. Pesticide-poisoning to fresh water teleost VIII. Ultrastructural alterations of the intestine of Tilapia nilotica under stress of exposure to diazinon and neopybuthrin. J. Egypt Ger. Soc. Zool. 1:223-236.
11. Elia, A. C., Waller, W. T., and Norton, S. J. 2002. Biochemical responses of bluegill sunfish (Lepomis macrochirus, Rafinesque) to atrazine induced oxidative stress. Bull. Environ. Contam. Toxicol. 68:809-816.
12. Ellman, G. L., Courtney, K. D., Andres, V., and Featherstone, R. M. 1961. A new and rapid colorimetric determination of acetycholinesterase activity. Biochem. Pharmacol. 7:88-95.
13. Environmental Protection Agency. 2004. Interim Reregistration Eligibility Decision, Diazinon. United States Environmental Protection Agency, Office of Prevention, Pesticides and Toxic Substances 7508 C.
14. Frasco, M. F., Fournier, D., Carvalho, F., and Guilhermino, L. 2006. Cholinesterase from the common prawn (Palaemon serratus) eyes: catalytic properties and sensitivity to organophosphate and carbamate compounds. Aquat. Toxicol. 77:412-421.
15. Griffith, O. W. 1999. Biologic and pharmacologic regulation of mammalian glutathione synthesis. Free Radic. Biol. Med. 27:922-935.
16. Habig, W. H., Pabst, M. J., and Jakoby, W. B. 1974. Glutathione S-transferases. The first enzymatic step in merkapturic acid formation. J. Biol. Chem. 249:7130-7139.
17. Hai, D. Q., Ilona Varga, Sz., and Matkovics, B. 1997. Organophosphate effects on antioxidant system of carp (Cyprinus carpio) and catfish (Ictalurus nebulosus). Comp. Biochem. Toxicol. 117C:83-88.
18. Halliwell, B., and Gutteridge, J. M. 2003. Free Radicals in Biology and Medicine, third ed., Oxford University Press, New York, p. 936.
19. Hanigan, M. H. 1998. γ-Glutamyl transpeptidase, a glutathionase: its expression and function in carcinogenesis. Chem. Biol. Interact 111-112:333-342.
20. Hazarika, A., Sarkar, S. N., Hajare, S., Kataria, M., and Malik, J. K. 2003. Influence of malathion pretreatment on the toxicity of anilofos in male rats: a biochemical interaction study. Toxicology 185:1-8.
21. Jefferies, H., Coster, J., Khalil, A., Bot, J., McCauley, R. D., and Hall, J. C. 2003. Glutathione. ANZ. J. Surg. 73:517-522.
22. Kwong, T. C. 2002. Organophosphate pesticides: biochemistry and clinical toxicology. Ther. Drug. Monit. 24:144-149.
23. Lemaire, P., Förlin, L., and Livingstone, D. R. 1996. Responses of hepatic biotransformation and antioxidant enzymes to CYPla-inducers (3-methylchloranthrene, β-naphtoflavone) in sea bass (Dicentrarchus labrax), dab (Limanda limanda) and rainbow trout (Onchorhynchus mykiss). Aquat. Toxicol. 36:141-160.
24. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. 1951. Protein measurement with folin phenol reagent. J. Biol. Chem. 193:265-275.
25. Ohkawa, H., Ohishi, N., and Tagi, K. 1979. Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal. Chem. 95:351-358.
26. Orlowski, M., and Meister, A. 1965. Isolation of γ-glutamyl transpeptidase from hog kidney. J. Biol. Chem. 240:338-347.
27. Pandey, S., Ahmad, I., Parvez, S., Bin-Hafeez, B., Haque, R., and Raisuddin, S. 2001. Effect of endosulfan on antioxidants of freshwater fish Channa punctatus Bloch: 1. Protection against lipid peroxidation in liver by copper preexposure. Arch. Environ. Contam. Toxicol. 41:345-352.
28. Pena-Llopis, S., Dolores Ferrando, M., and Pena, J. B. 2003. Fish tolerance to organophosphate-induced oxidative stress is dependent on the glutathione metabolism and enhanced by N-acetylcysteine. Aquat. Toxicol. 65:337-360.
29. Pena-Llopis, S., Pena, J. B., Sancho, E., Fernandez-Vega, C., and Ferrando, M. D. 2001. Glutathione-dependent resistance of the European eel Anguilla anguilla to the herbicide molinate. Chemosphere 45:671-681.
30. Sayeed, I., Parvez, S., Pandey, S., Bin-Hafeez, B., Haque, R., and Raisuddin, S. 2003. Oxidative stress biomarkers of exposure to deltamethrin in freshwater fish, Channa punctatus Bloch. Ecotox. Environ. Saf. 56:295-301.
31. Seelig, G. F., Simondsen, R. P., and Meister, A. 1984. Reversible dissociation of γ-glutamylcysteine synthetase into two subunits. J. Biol. Chem. 259:9345-9347.
32. Sen, C. K. 1997. Nutritional biochemistry of cellular glutathione. Nutr. Biochem. 8:660-672.
33. Stein, J. E., Collier, T. K., Reichert, W. L., Casillas, E., and Varanasi, U. 1992. Bioindicators of contaminant exposure and sublethal effects: studies with benthic fish in Puget Sound, Washington. Environ. Toxicol. Chem. 11:701-714.
34. Stephensen, E., Sturve, J., and Förlin, L. 2002. Effects of redox cycling compounds on glutathione content and activity of glutathione-related enzymes in rainbow trout liver. Comp. Biochem. Physiol. 133C:435-442.
35. Varo, I., Navarro, J. C., Amat, F., and Guilhermino, L. 2003. Effect of dichlorvos on cholinesterase activity of the European sea bass (Dicentrarchus labrax). Pestic. Biochem. Physiol. 75:61-72.
36. Yang, Z. P., and Dettbarn, W. D. 1996. Diisopropylphosphofluoridate- induced cholinergic hyperactivity and lipid peroxidation. Toxicol. Appl. Pharm. 138:48-53.
37. Zhang, J., Shen, H., Wang, X., Wu, J., and Xue, Y. 2004. Effects of chronic exposure of 2,4-dichlorophenol on the antioxidant system in liver of freshwater fish Carassius auratus. Chemosphere 55:167-174.