Toxicology International (Formerly Indian Journal of Toxicology)

Open Access Open Access  Restricted Access Subscription Access
Open Access Open Access Open Access  Restricted Access Restricted Access Subscription Access

Evaluation of Aldrin-Induced Oxidative Stress and Apoptosis in J774 Macrophages


Affiliations
1 Department of Veterinary Pharmacology and Toxicology, College of Veterinary Science, Guru Angad Dev Veterinary and Animal Sciences University, Ludhiana-141004, India
     

   Subscribe/Renew Journal


The present study was carried out to evaluate the aldrin-induced oxidative stress and apoptosis in murine macrophage (J774A.1) cells. Acute exposure of aldrin for 2 hrs was given to the J774A.1 cells cultured in DMEM with 10% FBS at 37oC and 5% CO2 in air with 95% relative humidity under in vitro system. Lethal concentration-50 (LC50) was calculated after exposure period as 7.24 μg/ml. Further, cells were exposed with three different concentration of aldrin (1.81, 3.65 and 7.24 μg/ml) and 0.1% DMSO was used as negative control. The antioxidant enzymes and non-enzymes were determined along with G6pDH, LDH and ALP enzymes in J774A.1 cells. Cells were monitored for cell morphology and apoptosis. Exposure of aldrin to J774A.1cells resulted in increase in lipid peroxidation and decrease in antioxidant enzyme/ nonenzymes system. Further it caused decrease in G6PDH enzymes activity and excess leakage of LDH and ALP enzymes. The aldrin-treated cells showed higher number of apoptotic cells with alteration in cell morphology indicating apoptotic and necrotic changes. These effects were noticed in dose dependant manner. In conclusion, the result of in vitro study suggests that the aldrin can induced the process of apoptosis and cell death through the generation of ROS and thereof oxidative insult in J774A.1 cells.

Keywords

Aldrin, Apoptosis, Antioxidant Enzymes, J774A.1 Cells, Oxidative Stress.
User
Subscription Login to verify subscription
Notifications
Font Size

  • Chaiyarat R, Sookjam C, Eiam-Ampai K, Damrongphol P. Organochlorine pesticide levels in the food web in rice paddies of Bueng Boraphet wetland, Thailand. Environ Monit Assess. 2015; 187(5):4469.

  • Badr A, Elkington TT. Antimitotic and chromo, toxic effects of isoproturon in A. cepa and H. vulgare. Environ Exp Bot. 1982; 22:265–70.

  • Gui D, Yu R, He X, Tu Q, Wu Y. Tissue distribution and fate of persistent organic pollutants in Indo-Pacific humpback dolphins from the Pearl River Estuary, China. Mar Pollut Bull. 2014; 86(1-2):266–73.

  • Iyer P. Developmental and reproductive toxicology of pesticides. In: Krieger R editor. Handbook of Pesticide Toxicology, Academic Press, San Diego, 2010; 1:375–420.

  • Parron T, Requena M, Hernández AF, Alarcon R. Association between environmental exposure to pesticides and neurodegenerative diseases. Toxicol Appl Pharmacol 2011; 256: 379–85.

  • Hernandez AF, Lacasana M, Gil F, Rodriguez-Barranco M, Pla A, Lopez-Guarnido O. Evaluation of pesticide-induced oxidative stress from a gene–environment interaction perspective. Toxicol. 2013; 307:95–102.

  • Lonare M, Kumar M, Raut S, Badgujar P, Doltade S, Telang A. Evaluation of imidacloprid-induced neurotoxicity in male rats: A protective effect of curcumin. Neurochem Inter. 2014; 78:122–9

  • Bedia C, Dalmau N, Jaumot J, Tauler R. Phenotypic malignant changes and untargeted lipidomic analysis of longterm exposed prostate cancer cells to endocrine disruptors. Environ Res. 2015; 140:18–31.

  • Abdollahi M, Ranjbar A, Shadnia S, Nikfar S, Rezaiee A. Pesticides and oxidative stress: a review. Med Sci Monit. 2004; 10:RA141–7.

  • Raina R, Verma PK, Pankaj NK, Prawez S. Induction of oxidative stress and lipid peroxidation in rats chronically exposed to cypermethrin through dermal application. J Vet Sci. 2009; 10:257–9.

  • Gao LY, Abu Kwaik Y. Hijacking of apoptotic pathways by bacterial athogens. Microb Infect. 2000; 2:1705–19.

  • Sharma H, Zhang P, Barber DS, Liu B. Organochlorine pesticides dieldrin and lindane induce cooperative toxicity in dopaminergic neurons: Role of oxidative stress NeuroToxicol. 2010; 31(2):215–22

  • Tobiszewski M, Orlowski A. Multicriteria decision analysis in ranking of analytical procedures for aldrin determination in water. J Chromatogr A. 2015; 1387:116–22.

  • Wrobel MH, Grzeszczyk M, Mlynarczuk J, Kotwica J. The adverse effects of aldrin and dieldrin on both myometrial contractions and the secretory functions of bovine ovaries and uterus in vitro. Toxicol Appl Pharmacol. 2015; 85(1):23–31.

  • Koner BC, Banerjee BD, Ray A. Organochlorine pesticide-induced oxidative stress and immune suppression in rats. Indian J Exp Biol. 1998; 36(4):395–8.

  • Naqvi S, Samim M, Abdin MZ, Ahmed FJ, Maitra AN, Prashant CK, Dinda AK. Concentration-dependent toxicity of iron oxide nanoparticles mediated by increased oxidative stress; Inter J Nanomed. 2010; 5:983–9.

  • Mahajan S, Prashant CK, Koul V, Choudhary V, Dinda AK. Receptor specific macrophage targeting by mannose-conjugated gelatin nanoparticles: An in-vitro and in-vivo study. Curr Nanosci. 2010; 6(4):413–21.

  • Borenfreund E, Puerner J. Toxicity determined in vitro by morphological alterations and neutral red absorption. Toxicol Lett. 1985; 24:119–24.

  • Spector DL, Goldman RD, Leinwand LA. Morphological assessment of cell death. In: Spector DL, Goldman RD, Leinwand LA editors. Cells, a laboratory manual, in culture and biochemical analysis of cells. NY: Cold Spring Harbor Laboratory Press; 1997; 2:15.3–15.10.

  • Bergmeyer H. Methods of enzymatic analysis. New York: Academic Press. 1974.

  • Aebi H. Catalase in vitro. Methods Enzymol. 1984 ; 105:121–6.

  • Paglia DE, Valentine WN. Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J Lab Clin Med. 1967; 70:158–69.

  • Madesh J, Balasubramanian KA. Microtitre plate assay for superoxide dismutase using MTT reduction by superoxide. Indian J Biochem Biophys 1998; 35: 184–8.

  • Habig WH, Pabst MJ, Jakoby WB. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J Biol Chem. 1974; 249:7130–9.

  • Sedlak J, Lindsay RH. Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman’s reagent. Anal Biochem. 1968; 25:192–205.

  • Ohkawa H, Ohishi N, Yagi K. Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal Biochem. 1979; 95:351–8.

  • Lowry, OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with Folin- Phenol reagent. J Biol Chem. 1951; 193:265–75.

  • Bachowski S, Xu Y, Stevenson DE, Walborg EF Jr, Klaunig JE. Role of oxidative stress in the selective toxicity of dieldrin in the mouse liver. Toxicol Appl Pharmacol. 1998; 150(2):301–9.

  • Kitazawa M, Anantharam V, Kanthasamy AG. Dieldrin-induced oxidative stress and neurochemical changes contribute to apoptotic cell death in dopaminergic cells. Free Radic Biol Med. 2001; 31:1473–85.

  • Hincal F, Gurbay A, Giray, B. Induction of lipid peroxidation and alteration of glutathione redox status by endosulfan. Biol Trace Elem Res. 1995; 47(1-3):321–6.

  • Dorval J, Leblond VS, Hontela A. Oxidative stress and loss of cortisol secretion in adrenocortical cells of rainbow trout (Oncorhynchus mykiss) exposed in vitro to endosulfan, an organochlorine pesticide. Aquat Toxicol. 2002; 63(3):229–41.

  • Pandey S, Ahmad I, Parvez S, Bin-Hafeez B, Haque R, Raisuddin S. 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. 2001; 41(3):345–52.

  • Lonare M, Kumar M, Raut S, More A, Doltade S, Badgujar P, Telang A. Evaluation of ameliorative effect of curcumin on imidacloprid-induced male reproductive toxicity in wistar rats. Environ Toxicol. 2015. Doi: 10.1002/tox.22132.

  • Lopez O, Hernandez AF, Rodrigo L et al. Changes in antioxidant enzymes in humans with long-term exposure to pesticides. Toxicol Lett. 2007; 171:146–53.

  • Kannan K, Jain SK. Oxidative stress and apoptosis. Pathophysiology. 2000; 7(3):153–63.

  • Simon HU, Haj-Yehia A, Levi-Schaffer F. Role of reactive oxygen species (ROS) in apoptosis induction. Apoptosis. 2000; 5:415–8.

  • Junn E, Mouradian MM. Apoptotic signaling in dopamineinduced cell death: the role of oxidative stress, p38 mitogen-activated protein kinase, cytochrome c and caspases. J Neurochem. 2001; 78:374–83.

  • Akbarsha MA, Sivasamy P. Apoptosis in male germinal line cells of rat in vivo: caused by phosphamidon. Cytobios. 1997; 91:33–44.

  • Tian WN, Braunstein LD, Pang J, Stuhlmeier KM, Xi QC, Tian X, Stanton RC. Importance of glucose-6-phosphate dehydrogenase activity for cell growth. J Biol Chem. 1998; 273:10609–17.

  • Cho SW, Joshi JG. Inactivation of glucose-6-phosphate 11. dehydrogenase isozymes from human and pig brain by aluminum. J Neurochem. 1989; 53:616–21.

  • Manna S, Bhattacharyya D, Mandal TK, Das S. Sub-chronic toxicity study of alfa-cypermethrin in rats. Iranian J Pharmacol Therapeutics. 2006; 5:163–6.

  • Kale M, Rathore N, John S, Bhatnagar D. Lipid peroxidative damage on pyrethroid exposure and alterations in antioxidant status in rat erythrocytes: A possible involvement of reactive oxygen species. Toxicol Lett. 1999; 105(3):197–205.

  • Ranjbar A, Pasalar P, Sedighi A, Abdollahi M. Induction of oxidative stress in paraquat formulating workers. Toxicol Lett. 2002; 131:191–4.

  • Ronald WT, Malcolm RS, John WL. Mechanism of action and fate of the fungicide chlorothalonil (2,4,5,6-tetrachloroisophthalonitrile) in biological systems: I. Reactions with cells and subcellular components of Saccharomyces pastorianus. Pest Biochem Physiol. 2004; 3(2):160–7.

  • Kostaropoulos I, Papadopoulos AI, Metaxakis A et al. The role of glutathione S-transferases in the detoxification of some organophosphorus insecticides in larvae and pupae of the yellow mealworm, Tenebrio molitor (Coleoptera: Tenebrionidae). Pest Manag Sci. 2001; 57:501–8.

  • Vina J. Glutathione: Metabolism and Physiological Functions. CRC Press, Boston. 1990; 222–8.

  • Perez-Maldonado IN, Herrera C, Batres LE, Gonzalez-Amaroa R, Diaz-Barriga F, Yanez L. DDT-induced oxidative damage in human blood mononuclear cells. Environ Res. 2005; 98:177–84.

  • Kannan K, Holcombe RF, Jain SK, Alvarez-Hernandez X, Chervenak R, Wolf RE, Glass J. Evidence for the induction of apoptosis by endosulfan in a human T-cell leukemic line. Mol Cell Biochem. 2000; 205:53–66.

  • Slim R, Toborek M, Robertson LW, Lehmler HJ, Henning B. Cellular glutathione status modulates polychlorinated biphenyl-induced stress response and apoptosis in vascular endothelial cells. Toxicol Appl Pharmacol. 2000; 166:36–42.

  • Kitizawa M, Anantharam V, Kanthasamy AG. Dieldrininducedoxidative stress and neurochemical changes contribute to apoptotic cell death in dopaminergic cells. Free Radical Biol. Med. 2001; 31:1473–85.


Abstract Views: 486

PDF Views: 0




  • Evaluation of Aldrin-Induced Oxidative Stress and Apoptosis in J774 Macrophages

Abstract Views: 486  |  PDF Views: 0

Authors

Milindmitra K. Lonare
Department of Veterinary Pharmacology and Toxicology, College of Veterinary Science, Guru Angad Dev Veterinary and Animal Sciences University, Ludhiana-141004, India
Bhaskar Vemu
Department of Veterinary Pharmacology and Toxicology, College of Veterinary Science, Guru Angad Dev Veterinary and Animal Sciences University, Ludhiana-141004, India
Amit K. Singh
Department of Veterinary Pharmacology and Toxicology, College of Veterinary Science, Guru Angad Dev Veterinary and Animal Sciences University, Ludhiana-141004, India
Saloni Singla
Department of Veterinary Pharmacology and Toxicology, College of Veterinary Science, Guru Angad Dev Veterinary and Animal Sciences University, Ludhiana-141004, India
Suresh K. Sharma
Department of Veterinary Pharmacology and Toxicology, College of Veterinary Science, Guru Angad Dev Veterinary and Animal Sciences University, Ludhiana-141004, India

Abstract


The present study was carried out to evaluate the aldrin-induced oxidative stress and apoptosis in murine macrophage (J774A.1) cells. Acute exposure of aldrin for 2 hrs was given to the J774A.1 cells cultured in DMEM with 10% FBS at 37oC and 5% CO2 in air with 95% relative humidity under in vitro system. Lethal concentration-50 (LC50) was calculated after exposure period as 7.24 μg/ml. Further, cells were exposed with three different concentration of aldrin (1.81, 3.65 and 7.24 μg/ml) and 0.1% DMSO was used as negative control. The antioxidant enzymes and non-enzymes were determined along with G6pDH, LDH and ALP enzymes in J774A.1 cells. Cells were monitored for cell morphology and apoptosis. Exposure of aldrin to J774A.1cells resulted in increase in lipid peroxidation and decrease in antioxidant enzyme/ nonenzymes system. Further it caused decrease in G6PDH enzymes activity and excess leakage of LDH and ALP enzymes. The aldrin-treated cells showed higher number of apoptotic cells with alteration in cell morphology indicating apoptotic and necrotic changes. These effects were noticed in dose dependant manner. In conclusion, the result of in vitro study suggests that the aldrin can induced the process of apoptosis and cell death through the generation of ROS and thereof oxidative insult in J774A.1 cells.

Keywords


Aldrin, Apoptosis, Antioxidant Enzymes, J774A.1 Cells, Oxidative Stress.

References





DOI: https://doi.org/10.22506/ti%2F2015%2Fv22%2Fi2%2F137668