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Quinalphos Induced Oxidative Stress Biomarkers in Liver and Kidney of Common carp, Cyprinus carpio


Affiliations
1 Department of Aquatic Environment Management, Karnataka Veterinary, Animal & Fisheries Sciences University, College of Fisheries, Mangalore-575 002, Karnataka, India
2 Department of Veterinary Pharmacology and Toxicology, Karnataka Veterinary, Animal & Fisheries Sciences University, Veterinary College, Bangalore-560024, Karnataka, India
 

Oxidative stress responses were evaluated in liver and kidney of freshwater fish, Cyprinus carpio exposed to organophosphorus pesticide, quinalphos (25% emulsified concentration). Lipid peroxidation levels and antioxidant enzyme activities were measured spectrophotometrically in liver and kidney of fish, treated with two sub-lethal concentrations of quinalphos viz., 0.275 ppm and 0.55 ppm along with control as a reference for 4, 8, 16 and 32 days. The experimental concentration of quinalphos evoked different degrees of activity in both the tissues, the liver and the kidney. The significant increase in lipid peroxidation suggests quinalphosmediated free radical production; the increase in the activity of glutathione-S-transferase with corresponding increase in the activity of glutathione reductase indicates the glutathione conjugation of the pesticide; activity of superoxide dismutase, catalase and glutathione peroxidase decreased drastically after 32nd day exposure to sub-lethal concentrations of pesticide. Overall, the results demonstrate that alteration in the antioxidant enzymes, glutathione system and induction of lipid peroxidation reflects the toxicity of quinalphos which may cause oxidative stress in the experimental fish. The study, therefore, provides a rational use of biomarkers of oxidative stress in biomonitoring programs.

Keywords

Biomarkers, Chronic Toxicity, Cyprinus carpio, Oxidative Stress, Quinalphos.
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  • Aebi, H. 1974. Catalase. Methods in Enzymatic Analysis, 2: 673-678.

  • APHA, AWWA, WPCF. 1981. Standard Methods for the Examination of Water and Wastewater. Washington, DC: American Public Health Association, pp. 1134.

  • Bassi, A.M., Ledda, S., Penco, S., Menini, S., Muzio, G., Canuto, R. and Ferro, M. 2001. Changes in CYP1A1, GST, and ALDH3 enzymes in hepatoma cell lines undergoing enhanced lipid peroxidation. Free Radical Bio. Med., 29: 186-1196.

  • Cheung, C.C.C., Siu, W.H.L., Richardson, B.J., De Luca-Abbott, S.B. and Lam, P.K.S. 2004. Antioxidant responses to benzo[a]pyrene and aroclor 1254 exposure in the green-lipped mussel, Perna viridis. Environ. Pollut., 128: 393-403.

  • Das, B.K. and Mukherjee, S.C. 2000. Chronic toxic effects of quinalphos on some biochemical parameters in Labeo rohita (Ham.). Toxicol. Lett., 114: 11.

  • Dautremepuits, C., Paris-Palacios, S., Betoulle, S. and Vernet, G. 2004. Modulation in hepatic and head kidney parameters of carp (Cyprinus carpio L.) induced by copper and chitosan. Comp. Biochem. Physiol.C., 137(4): 325-333.

  • De Luca-Abbott, S.B., Richardson, B.J., McClellan, K.E., Zheng, G.J., Martin, M. and Lam, P.K.S. 2005. Field validation of antioxidant enzyme biomarkers in mussels (Perna viridis) and clams (Ruditapes philippinarum) transplanted in Hong Kong coastal waters. Mar. Pollut. Bull., 51: 694-707.

  • Di Giulio, R.T., Washburn, P.C., Wenning, R.J., Winston, G.W. and Jewell, C.S. 1989. Biochemical responses in aquatic animals: A review of determination of oxidative stress. Environ. Toxicol. Chem., 8: 1103-1123. .

  • Dimitrova, M.S.T., Tsinova, V. and Velcheva, V. 1994. Combined effects of zinc and lead on the hepatic superoxide dismutase-catalase system in carp (Cyprinus carpio). Comp. Biochem. Physiol. C., 108: 43-46.

  • Duncan, D.B.1955. Multiple range and multiple F-tests. Biometrics, 11: 142.

  • Durmaz, H., Sevgiler, Y. and Unes, N. 2006. Tissue specific antioxidative and neurotoxic responses to diazinon in Oreochromis niloticus. Pestic. Biochem. Physiol., 84: 215-226.

  • Gultekin, F., Ozturk, M. and Akdogan, M. 2000. The effects of organophosphate insecticide chlorpyrifos-ethyl on lipid peroxidation and antioxidant enzymes (in vitro). Arch. Toxicol., 74: 533-538.

  • Habig, W.H., Pabst, M.J. and Jakoby, W.B. 1974. Glutathione Stransferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem., 249: 7130-7139.

  • Leaver, M.J. and George, S.G. 1998. A piscidine glutathione S-transferase which efficiently conjugates the end-products of lipid peroxidation. Mar. Environ. Res., 46: 71-74.

  • Livingstone, D.R. 2001. Contaminant-stimulated reactive oxygen production and oxidative damage in aquatic organisms. Mar. Pollut. Bull., 42(8): 656-666.

  • Lopes, P.A., Pinheiro, T., Santos, M.C., Da Luz Mathias, M., CollaresPereira, M.J. and Viegas-Crespo, A.M. 2001. Response of antioxidant enzymes in freshwater fish populations (Leuciscus alburnoides complex) to inorganic pollutants exposure. Sci. Total Environ., 280: 153.

  • Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall, R.J. 1951. Protein measurement with the folin phenol reagent. J. Biol. Chem., 193: 265-275.

  • Massey, V. and Williams, C.H. 1965. On the reaction mechanism of yeast glutathione reductase. J. Biol. Chem., 240: 4470-4481.

  • Ohkawa, H., Ohisi, N. and Yagi, K. 1979. Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal. Biochem., 95: 351-358.

  • Oruc, E.Z., Sevgiler, Y. and Uner, N. 2004. Tissue-specific oxidative stress responses in fish exposed to 2, 4-D-Azinphosmethyl. Comp. Biochem. Physiol., 137: 43-51.

  • Paglia, D.E. and Valentine, W.N. 1967. Studies on quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J. Lab. Clin. Med., 70: 158-169.

  • Paoletti, F., Mocali, A. and Aldinucci, D. 1990. Superxide-driven NAD(P)H oxidation induced by EDTA-manganese complex and mercaptoethanol. Chem. Biol. Interact., 76: 3-18.

  • RodriGuez-Ariza, A., Peinado, J., Pueyo, C. and Lopez-Barea, J. 1993. Biochemical indicators of oxidative stress in fish from polluted littoral areas. Can. J. fish. Aquat. Sci., 50: 2568-2573.

  • Smith, G.J. and Litwack, G. 1980. Roles of ligandin and the glutathione Stranferases in binding steroid metabolites, carcinogens and other compounds. Rev. Biochem. Toxicol., 2: 1-47.

  • Snedecor, G.W. and Cochran, G.W. 1968. Statistical Methods. Oxford and IBH Publishing Company, Calcutta, India.

  • Stephensen, E., Sturve, J. and Forlin, L. 2002. Effects of redox cycling compounds on glutathione content and activity of glutathione-related enzymes in rainbow trout liver. Comp. Biochem. Physiol. C., 133: 435-442.

  • Triebskorn, R., Kohler, H.R., Honnen, W., Schramm, M. and Adams, S.M. 1997. Induction of heat shock proteins, changes in liver ultrastructure and alterations of fish behavior: Are these biomarkers related and are they useful to reflect the state of pollution in the field?. J. Aquatic Ecosystem Stress Recovery, 6: 57-73.

  • Wills, E.D. 1969. Lipid peroxide formation in microsomes: General considerations. Biochem. J., 113: 315-324.

  • Zhang, Z., Huasheng, H., Xinhong, W., Jianqing, L., Weiqi, C. and Li, X. 2002. Determination and load of organophosphorus and organochlorine pesticides at water from Jiulong River Estuary, China. Mar. Pollut. Bull., 45(1-12): 397-402.


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  • Quinalphos Induced Oxidative Stress Biomarkers in Liver and Kidney of Common carp, Cyprinus carpio

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Authors

A. Padmanabha
Department of Aquatic Environment Management, Karnataka Veterinary, Animal & Fisheries Sciences University, College of Fisheries, Mangalore-575 002, Karnataka, India
H. R. V. Reddy
Department of Aquatic Environment Management, Karnataka Veterinary, Animal & Fisheries Sciences University, College of Fisheries, Mangalore-575 002, Karnataka, India
Avinash Bhat
Department of Veterinary Pharmacology and Toxicology, Karnataka Veterinary, Animal & Fisheries Sciences University, Veterinary College, Bangalore-560024, Karnataka, India
Muttappa Khavi
Department of Aquatic Environment Management, Karnataka Veterinary, Animal & Fisheries Sciences University, College of Fisheries, Mangalore-575 002, Karnataka, India

Abstract


Oxidative stress responses were evaluated in liver and kidney of freshwater fish, Cyprinus carpio exposed to organophosphorus pesticide, quinalphos (25% emulsified concentration). Lipid peroxidation levels and antioxidant enzyme activities were measured spectrophotometrically in liver and kidney of fish, treated with two sub-lethal concentrations of quinalphos viz., 0.275 ppm and 0.55 ppm along with control as a reference for 4, 8, 16 and 32 days. The experimental concentration of quinalphos evoked different degrees of activity in both the tissues, the liver and the kidney. The significant increase in lipid peroxidation suggests quinalphosmediated free radical production; the increase in the activity of glutathione-S-transferase with corresponding increase in the activity of glutathione reductase indicates the glutathione conjugation of the pesticide; activity of superoxide dismutase, catalase and glutathione peroxidase decreased drastically after 32nd day exposure to sub-lethal concentrations of pesticide. Overall, the results demonstrate that alteration in the antioxidant enzymes, glutathione system and induction of lipid peroxidation reflects the toxicity of quinalphos which may cause oxidative stress in the experimental fish. The study, therefore, provides a rational use of biomarkers of oxidative stress in biomonitoring programs.

Keywords


Biomarkers, Chronic Toxicity, Cyprinus carpio, Oxidative Stress, Quinalphos.

References