Antioxidant enzymatic effects of diethylene glycol dibenzoate on zebrafish (Danio rerio)
DOI:
https://doi.org/10.25081/imrj.2026.v16.9904Keywords:
Diethylene glycol dibenzoate, Zebrafish, Catalase, Superoxide dismutase, Antioxidant defenseAbstract
Endocrine disrupting chemicals (EDCs) are known to disrupt normal metabolism and can influence the incidence of obesity in animals and humans. EDCs can exert adverse effects at low concentrations, oftenin a non-monotonic dose-related fashion. Among EDCs, diethylene glycol dibenzoate (DGB), an approved alternative to phthalates in the production of plastic and latex products, is less abundant and its effects are almost completely unknown. Potential EDCs can disrupt the normal hormonal level by inhibiting or stimulating the production of hormones or changing the way in which the hormones are transported to target tissues. In specific, the effect of DGB has expanded to include the deregulation of the antioxidant defense (AD) system of organisms dealing with oxidative stress and several enzymes metabolism. The present study focused on the changes elicited by DGB is on the enzyme activity catalase and superoxide dismutase of the various organs (muscle, gill, and liver) of zebrafish. The observation registered in this study reflects that antioxidant enzyme activities were significantly enhanced in all the tissues (muscle, gill, and liver) when compared to control (untreated DGB).This in turn induces some enzymatic variations that lead to the changes in hormonal secretion which is responsible for functioning of targeted organs and its generative activities. This could be due to the detoxification mechanism exhibited by the zebrafish on exposure of DGB. This finding provides a support for the hypothesis that DGB may be the environmental contaminant with stress property and in need to control of its exposure immediately and completely. Also this finding may help to initiate and follow the innovative methods, to control the use of DGB in our day today life.
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References
Aebi, H. E. (1984). Catalase. In H. U. Bergmeyer (Ed.), Methods of Enzymatic Analysis (Vol. 3, pp. 273-286). John Wiley & Sons, Inc.
Arun, S., & Subramanian, P. (2002). Antioxidant enzymes in freshwater prawn Macrobrachium malcolmsonii during embryonic and larval development. Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 121(3), 273-277. https://doi.org/10.1016/S0305-0491(98)10100-1
Chamorro-García, R., & Blumberg, B. (2014). Transgenerational effects of obesogens and the obesity epidemic. Current Opinion in Pharmacology, 19, 153-158. https://doi.org/10.1016/j.coph.2014.10.010
Chelikani, P., Fita, I., & Loewen, P. C. (2004). Diversity of structures and properties among catalases. Cellular and Molecular Life Sciences, 61, 192-208. https://doi.org/10.1007/s00018-003-3206-5
da Silva, C. A., Oba, E. T., Ramsdorf, W. A., Magalhães, V. F., Cestari, M. M., Ribeiro, C. A. O., de Assis, H. C. S. (2011). First report about saxitoxins in freshwater fish Hoplias malabaricus through trophic exposure. Toxicon, 57(1), 141-147. https://doi.org/10.1016/j.toxicon.2010.10.015
El-Naggar, A. M., Mahmoud, S. A., & Tayel, S. I. (2009). Bioaccumulation of some heavy metals and histopathological alterations in liver of Oreochromis niloticus in relation to water quality at different localities along the River Nile, Egypt. World Journal of Fish and Marine Sciences, 1(2), 105-114.
Filho, D. W. (1996). Fish antioxidant defenses - a comparative approach. Brazilian Journal of Medical and Biological Research, 29(12), 1735-1742.
Filho, D. W., Giulivi, C., & Boveris, A. (1993). Antioxidant defenses in marine fish: I. Teleosts. Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology, 106(2), 409-413. https://doi.org/10.1016/0742-8413(93)90154-D
Gardner, P. R., Raineri, I., Epstein, L. B., & White, C. W. (1995). Superoxide radical and iron modulate aconitase activity in mammalian cells. Journal of Biological Chemistry, 270(22), 13399-13405. https://doi.org/10.1074/jbc.270.22.13399
Grün, F., & Blumberg B, (2006). Environmental obesogens: Organotins and endocrine disruption via nuclear receptor signaling. Endocrinology, 147(6), 50-55. https://doi.org/10.1210/en.2005-1129
Hegazi, M. M., Attia, Z. I., & Ashour, O. A. (2010). Oxidative stress and antioxidant enzymes in liver and white muscle of Nile tilapia juveniles in chronic ammonia exposure. Aquatic Toxicology, 99(2), 118-125. https://doi.org/10.1016/j.aquatox.2010.04.007
Heindel, J. J., Blumberg, B., Cave, M., Machtinger, R., Mantovani, A., Mendez, M. A., Nadal, A., Palanza, P., Panzica, G., Sargis, R., Vandenberg, L. N., & vom Saal, F. (2017). Metabolism disrupting chemicals and metabolic disorders. Reproductive Toxicology, 68, 3-33. https://doi.org/10.1016/j.reprotox.2016.10.001
Hernández-Moreno, D., Soler, F., Míguez, M. P., & Pérez-López, M. (2010). Brain acetyl cholinesterase, malondialdehyde and reduced glutathione as biomarkers of continuous exposure of tench, Tinca tinca, to carbofuran or deltamethrin. Science of The Total Environment, 408(21), 4976-4983. https://doi.org/10.1016/j.scitotenv.2010.07.044
Kelly, K. A., Havrilla, C. M., Brady, T. C., Abramo, K. H., & Levin, E. D. (1998). Oxidative stress in toxicology: established mammalian and emerging picine model systems. Environmental Health Perspectives, 106(7), 375-384. https://doi.org/10.1289/ehp.98106375
Kermanshahi pour, A., Cooper, D. G., Mamer, O. A., Maric, M., Nicell, J. A. (2009). Mechanisms of biodegradation of dibenzoate plasticizers. Chemosphere, 77(2), 258-263. https://doi.org/10.1016/j.chemosphere.2009.06.048
Kuthan, H., Haussmann, H. J., & Werringloer, J. (1986). A spectrometric assay for superoxide dismutase activities in crude tissue fractions. Biochemical Journal, 237(1), 175-180. https://doi.org/10.1042/bj2370175
Lemaire, P., Berhaut, S., Lemaire-Gony, S., & Lafaurie, M. (1992). Ultrastructural changes induced by benzo[a]pyrene in sea bass (Dicentachus labrax) liver and intestine: Important of intoxication route. Environmental Research, 57(1), 59-72. https://doi.org/10.1016/S0013-9351(05)80019-2
Li, Z.-H., Zlabek, V., Velisek, J., Grabic, R., Machova, J., Kolarova, J., Li, P., & Randak, T. (2011). Acute toxicity of carbamazepine to juvenile rainbow trout (Oncorhynchus mykiss): Effects on antioxidant responses, hematological parameters and hepatic EROD. Ecotoxicology and Environmental Safety, 74(3), 319-327. https://doi.org/10.1016/j.ecoenv.2010.09.008
Lin, H. C., & Hwang, P. P. (1998). Acute and chronic effects of gallium chloride (GaCl3) on tilapia (Oreochromis mossambicus) larvae. Bulletin of Environmental Contamination and Toxicology, 60, 931-935. https://doi.org/10.1007/s001289900717
Livingstone, D. R., Forlin, L., & George, S. G. (1994). Molecular biomarkers and toxic consequences of impact by organic pollution in aquatic organism. D. Wsutcliffee, editor water quality and stress indicators in marine and fresh water ecosystem UK (pp. 154-171). Freshwater Biological Association.
Maradonna, F., & Carnevali, L. (2018). Lipid metabolism alteration by endocrine disruptors in animal models: An overview. Frontiers in Endocrinology, 9, 654. https://doi.org/10.3389/fendo.2018.00654
Marcon, J. M., & Filho, D. W. (1999). Antioxidant processes of the wild tambaqui, Colossoma macropomum (Osteichthyes, Serrasalmidae) from the Amazon. Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology, 123(3), 257-263. https://doi.org/10.1016/S0742-8413(99)00030-4
Marklund, S., & Marklund, G. (1974). Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. European Journal of Biochemistry, 47(3), 469-474. https://doi.org/10.1111/j.1432-1033.1974.tb03714.x
McCord, J. M., & Fridovich, I. (1969). Superoxide Dismutase: An enzymatic function for erythrocuprein (hemocuprein). Journal of Biological Chemistry, 244(22), 6049-6055. https://doi.org/10.1016/S0021-9258(18)63504-5
Michiels, C., Raes, M., Toussaint, O., & Remacle, J. (1994). Importance of SE-glutathione peroxidase, catalase, and Cu/Zn-SOD for cell survival against oxidative stress. Free Radical Biology and Medicine, 17(3), 235-248. https://doi.org/10.1016/0891-5849(94)90079-5
Neeraj Kumar, Antony Jesu Prabhu, P., Pal, A. K., Remya, S., Md. Aklakur, Rana, R. S., Subodh Gupta, Raman, R. P., & Jadhao, S. B. (2011). Anti-oxidative and immuno-hematological status of Tilapia (Oreochromis mossambicus) during acute toxicity test of endosulfan. Pesticide Biochemistry and Physiology, 99(1), 45-52. https://doi.org/10.1016/j.pestbp.2010.10.003
Pathan, T., Shinde, S. E., Thete, P., & Sonawane, L. D. (2010). Histopathology of liver and kidney of Rasbora daniconius exposed to study mill effluent. Research Journal of Biological Sciences, 5(5), 389-394.
Rudneva, I. I. (1997). Blood antioxidant system of Black Sea elasmobranch and teleosts. Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology, 118(2), 255-260. https://doi.org/10.1016/S0742-8413(97)00111-4
Xing, H., Li, S., Wang, Z., Gao, X., Xu, S., & Wang, X. (2012). Histopathological changes and antioxidant response in brain and kidney of common carp exposed to atrazine and chlorpyrifos. Chemosphere, 88(4), 377-383. https://doi.org/10.1016/j.chemosphere.2012.02.049
Zhao, X., Gao, Y., & Qi, M. (2014). Toxicity of phthalate esters exposure to carp (Cyprinus carpio) and antioxidant response by biomarker. Ecotoxicology, 23, 626-632. https://doi.org/10.1007/s10646-014-1194-x
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