CYP1A gene expression and antioxidant enzymes in green scat (Scatophagus argus) as PAHs biomarker

Document Type : Research Paper

Authors

1 Assistant Professor in Department of Biotechnology, Persian Gulf Institute, Persian Gulf University, Bushehr, Iran

2 M.Sc. Student in Fisheries, Department of Fisheries, Faculty of Fisheries and Environmental Sciences, Gorgan University of Agricultural Sciences and Natural Resources, Gorgan, Iran

10.22124/japb.2022.21777.1458

Abstract

Monitoring of the pollutant effects in the biological environment requires the identification of a suitable biomarker. In this study, the efficacy of the expression of the CYP1 gene and the antioxidant enzymes in the Scatophagus argus were studied as biomarker of oil pollutants at three stations (Bandargah, Solhabad and Jofreh) and the control samples. CYP1A gene expression in liver was significantly different from control samples in all regions. The highest CYP1 gene expression was measured in Solhabad station. CYP1A gene expression in the gills of green scat fish showed a significant increase compared to control samples. The highest and lowest CYP1A gene expression was observed in the gills in Solhabad and Bandargah samples, respectively. The amount of superoxide dismutase and catalase of liver tissue in Jofrah and Solhabad stations were significantly lower than the control (P<0.05). In contrast, the rate of lipid peroxidation and GST were directly correlated with the amount of polycyclic aromatic hydrocarbons (P<0.05, R=0.96). Due to the relationship between CYP1A gene expression and antioxidant markers and the level of contamination, CYP1A gene expression and antioxidant markers can be used as a suitable biomarker for PAH contaminants in this species.

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References

قاسمی ا. 1392. بررسی امکان استفاده از میزان بیان ژن سیتوکروم P450 به عنوان شاخص آلاینده‌های نفتی. گزارش نهایی طرح مرکز مطالعات و همکاری‌های علمی بین‌المللی. 136ص.
Abele D., Vazquez-Medina J.P. and Zenteno-Savin T. 2017. Introduction to oxidative stress in aquatic ecosystems. P: 1–5. In: Abele D., Vazquez-Medina J.P. and Zenteno-Savin T. (Eds.). Oxidative Stress in Aquatic Ecosystems. John Wiley and Sons, UK.
Agrahari S., Pandey K.C. and Gopal K. 2007. Biochemical alteration induced by monocrotophos in the blood plasma of fish, Channa punctatus (Bloch). Pesticide Biochemistry and Physiology, 88(3): 268–272.
Almeida J.R., Oliveira C. and Gravato C. 2010. Linking behavioural alterations with biomarkers responses in the European seabass Dicentrarchus labrax L. exposed to the organophosphate pesticide fenitrothion. Ecotoxicology, 19: 1369–1381.
An L., Hu J., Yang M., Zheng B., Wei A., Shang J. and Zhao X. 2011. CYP1A mRNA expression in redeye mullets (Liza haematocheila) from Bohai Bay, China. Marine Pollution Bulletin, 62: 718–725.
Bagheri D., Amiri B., Poorbagher H., Farahmand H. and Bargahi A. 2014. Antioxidant responses, lipid peroxidation and blood aminotransferase activity in Liza persicus in the northern Persians Gulf (Case study: The Boushehr Province). Journal of Fisheries, 67(3): 329–345.
Chitra K.C. and Maiby S. 2014. Oxidative stress of bisphenol-A and its adverse effects on liver of freshwater fish Oreochromis mossambicus. International Journal of Scientific Research, 3(7): 221–224.
Chitra K.C. and Sajitha R. 2014. Effect of bisphenol-A on the antioxidant defense system and its impact on the activity of succinate dehydrogenase in the gill of freshwater fish, Oreochromis mossambicus. Cell and Tissue Research, 14(2): 4219–4226.
Dorrington T., Zanette J., Zacchi F.L., Stegeman J.J. and Bainy A.C.D. 2012. Basal and 3-methylcholanthrene-induced expression of cytochrome P450 1A, 1B and 1C genes in the Brazilian guppy, Poecilia vivipara. Aquatic Toxicology, 124-125: 106–113.
Faheem M. and Lone K.P. 2018. Oxidative stress and histopathologic biomarkers of exposure to bisphenol-A in the freshwater fish Ctenopharyngodon idella. Brazilian Journal of Pharmaceutical Sciences, 53: 1–9.
Faheem M., Sulehria A. Q. K., Tariq M., Khadija I. and Saeed M. 2012. Effect of sub-lethal dose of cadmium chloride on biochemical profle and catalase activity in freshwater fish Oreochromis niloticus. Biologia (Pakistan), 58(1-2): 73–78.
Goth L. 1991. A simple method for determination of serum catalase activity and revision of reference range. Clinical Chemical Acta, 196(2-3): 143–151.
Habig W.H., Pabst M.J. and Jakoby W.B. 1974. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. Journal of Biological Chemistry, 249(22): 7130–7139.
Hassanin A.A.I., Kaminishi Y., Funahashi A. and Itakura T. 2012. Cytochrome P450 1C1 complementary DNA cloning, sequence analysis and constitutive expression induced by benzo-a-pyrene in Nile tilapia (Oreochromis niloticus). Aquatic Toxicology, 109: 17–24.
Hellou J., Ross N.W. and Moon T.W. 2012. Glutathione, glutathione S-transferase and glutathione conjugates, complementary markers of oxidative stress in aquatic biota. Environmental Science and Pollution Research, 19: 2007–2023.
Jonsson M.E., Gao K., Olsson J.A., Goldstone J.V. and Brandt I. 2010. Induction patterns of new CYP1 genes in environmentally exposed rainbow trout. Aquatic Toxicology, 98: 311–321.
Livak K.J. and Schmittgen T.D. 2001. Analysis of relative gene expression data using real-time quantitative PCR and the 2−ΔΔCT method. Methods, 25(4): 402–408.
Livingstone D.R. 1998. The fate of organic xenobiotics in aquatic ecosystems: Quantitative and qualitative differences in biotransformation by invertebrates and fish. Comparative Biochemistry and Physiology (A), 120(1): 43–49.
McCord J.M. and Fridovich I. 1969. Superoxide dismutase an enzymic function for erythrocuprein (hemocuprein). Journal of Biological Chemistry, 244(22): 6049–6055.
Oliveira M., Ahmad I., Maria V., Pacheco M. and Santos M. 2010. Antioxidant responses versus DNA damage and lipid peroxidation in golden grey mullet liver: A field study at Ria de Aveiro (Portugal). Archives of Environmental Contamination and Toxicology, 59(3): 454–463.
Pigeolet E., Corbisier P., Houbion A., Lambert D., Michiels C., Raes M., Zachary M.D. and Remacle J. 1990. Glutathione peroxidase, superoxide dismutase and catalase inactivation by peroxides and oxygen derived free radicals. Mechanisms of Ageing and Development, 51(3): 283–297.
Quiros L., Pina B., Sole M., Blasco J., Lopez M.A., Riva M. C., Barcelo D. and Raldua D. 2007. Environmental monitoring by gene expression biomarkers in Barbus graellsii: Laboratory and field studies. Chemosphere, 67: 1144–1154.
Regoli F., Bocchetti R. and Filho D.W. 2011. Spectrophotometric assays of antioxidants, in oxidative stress in aquatic ecosystems. P: 367–380. In: Abele D., Vazquez-Medina J.P. and Zenteno-Savin T. (Eds.). Oxidative Stress in Aquatic Ecosystems. John Wiley and Sons, UK.
Ringwood A., Hoguet J., Keppler C., Gielazyn M., Ward B. and Rourk A. 2003. Cellular biomarkers (lysosomal destabilization, glutathione and lipid peroxidation) in three common estuarine species: A methods handbook. Marine Resources Research Institute, USA. 46P.
Santana M.S., Sandrini-Neto L., Neto F.F., Oliveira Ribeiro C.A., Di Domenico M. and Prodocimo M.M. 2018. Biomarker responses in fish exposed to polycyclic aromatic hydrocarbons (PAHs): Systematic review and meta-analysis. Environmental Pollution, 242: 449–461.
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. Ecotoxicology and Environmental Safety, 56(2): 295–301.
Smolowitz R.M., Schultz M.E. and Stegeman J.J. 1992. Cytochrome P4501a induction in tissues, including olfactory epithelium, of topminnows (Poeciliopsis spp) by waterborne benzo[a]pyrene. Carcinogenesis, 13: 2395–2402.
Van der Oost R., Beyer J. and Vermeulen N.P.E. 2003. Fish bioaccumulation and biomarkers in environmental risk assessment: a review. Environmental Toxicology and Pharmacology, 13: 57–149.
 
Aquatic Physiology and Biotechnology
Volume 11, Issue 1
June 2023
Pages 41-57

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