Investigation of the Effect of Acrylamide on Capoeta Capoeta (Guldensttead 1773) by Histopathological, Electrophoretic and Biochemical Methods

Year 2020, Volume: 7 Issue: 2, 153 - 166, 31.12.2020

Pinar Aksu Kılıçle , Evren Koç , Abdullah Doğan , Süleyman Gül , Ali Nazmi Can Doğan Yusuf Ersan

https://doi.org/10.48138/cjo.836674

Cited By: 2

Abstract

The aim of this study was to investigate the effects of acrylamide on Capoeta capoeta (Guldensttead 1773) by histopathological, electrophoretic and biochemical methods. Capoeta capoeta caught from Kars stream were used in the study. The fish were divided into 5 groups, each containing 10 pieces, and placed in 300 liter tanks with tap water. Group 1 was kept as a negative control. 20 mg / kg cyclophosphamide given to group 2 (i.p. positive control group), 10 mg / L acrylamide given to group 3, 20 mg / L acrylamide given to group 4 and 30 mg / L acrylamide given to group 5. After all groups were kept in tanks for 4 days, blood and tissue samples taken from fish were investigated by histopathological, electrophoretic and biochemical methods.
As a result of the analyzes serum AST and ALT levels were decreased in the other groups compared to the negative control group and serum TAS levels were significantly increased in the 30 mg / L acrylamide group compared to the negative control group (P < 0.01). Compared with the negative control group, TOS levels were increased in all groups. When the electropherogram obtained from SDS-PAGE was examined, it was determined increases and decreases at 21 kD, 27 kD, 36 kD, 42 kD, 48 kD, 54 kD protein expressions in groups with different concentrations compared to the negative control group. It was observed that protein expressions were inhibited especially in the group treated with 20 mg / L acrylamide. As a result of histopathological examinations; increased degenerations were detected in the gill and liver tissues of fish due to the concentration of acrylamide. As a result; acrylamide treatment caused toxic effects on C. capoeta after this varying time intervals and concentrations.

Keywords

Acrylamide, Capoeta capoeta, fish, protein expression, AST, ALT, histopathology

Supporting Institution

KAFKAS ÜNİVERSİTESİ BİLİMSEL ARAŞTIRMA PROJELERİ KOORDİNATÖRLÜĞÜ

Project Number

2015-FM-52

Thanks

This study was supported by the Scientific Research Projects Coordination Unit of Kafkas University (Project Number: 2015-FM-52).

References

• Referans1 International Agency for Research on Cancer, International Agency for Research on Cancer, eds. Some Industrial Chemicals: Views and Expert Opinions of an IARC Working Group on the Evaluation of Carcinogenesis Risks to Humans, Which Met in Lyon, Lyon; 1994.
• Referans2 Europäische Kommission, ed. European Union Risk Assessment Report. Vol. 24: Acrylamide: Risk Assessment ; [Final Report]. Luxembourg: Office for Official Publications of the European Communities; 2002.
• Referans3 Claeys W.L., De Vleeschouwer K., Hendrickx M.E. (2005). Quantifying the Formation of Carcinogens During Food Processing: Acrylamide. Trends in Food Science & Technology, 16 (5): 181-193.
• Referans4 Tritscher A. (2004). Human Health Risk Assessment of Processing-Related Compounds in Food. Toxicology Letters, 149 (1-3): 177-186.
• Referans5 http://www.acrylamide-food.org/index.htm,2012.http://www.acrylamide-food.org/.FAO/WHO, Acrylamide in food network. Acrylamide Infonet. Accessed February 6, 2020.
• Referans6 Zhang Y., Dong Y., Ren Y., Zhang Y. (2006). Rapid Determination of Acrylamide Contaminant in Conventional Fried Foods by Gas Chromatography with Electron Capture Detector. Journal of Chromatography, 1116 (1-2): 209-216.
• Referans7 Petersen D.W., Lech J.J. (1987). Hepatic Effects of Acrylamide in Rainbow Trout. Toxicology and Applied Pharmacology, 89 (2): 249-255.
• Referans8 Weideborg M., Källqvist T., Ødegård K.E., Sverdrup L.E., Vik E.A. (2001). Environmental Risk Assessment of Acrylamide and Methylolacrylamide from a Grouting Agent Used in the Tunnel Construction of Romeriksporten, Norway. Water Research, 35(11): 2645-2652.
• Referans9 Grisolia C.K., Cordeiro C.M.T. (2000). Variability in Micronucleus Induction with Different Mutagens Applied to Several Species of Fish. Genetics and Molecular Biology, 23 (1): 235-239.
• Referans10 Eisenthal R., Danson M.J. (1992). Enzyme Assays: A Practical Approach. Oxford [England]; New York: IRL Press at Oxford University Press.
• Referans11 Laemmli U.K. (1970). Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4. Nature, 227 (5259): 680-685.
• Referans12 O’Farrell P.H. (1975). High Resolution Two-Dimensional Electrophoresis of Proteins. The Journal of Biological Chemistry, 250 (10): 4007-4021.
• Referans13 Erel O. (2004). A Novel Automated Direct Measurement Method For Total Antioxidant Capacity Using A New Generation, More Stable Abts Radical Cation. Clinical Biochemistry, 37(4): 277-285.
• Referans14 Luna L.G. (1968). Manual of Histologic Staining Methods of the Armed Forces Institue of Pathology. 3rd ed. Place of publication not identified: McGraw-Hill. Book Co.New York.
• Referans15 Besaratinia A., Pfeifer G.P. (2005). DNA Adduction and Mutagenic Properties of Acrylamide. Mutation Research, 580 (1-2): 31-40.
• Referans16 Manière I., Godard T., Doerge D.R., Churchwell M.I., Guffroy M., Laurentie M., Poul J.M. (2005). DNA Damage and DNA Adduct Formation in Rat Tissues Following Oral Administration of Acrylamide. Mutation Research/Genetic Toxicology and Environmental Mutagenesis, 580 (1-2): 119-129.
• Referans17 Stadler R.H., Blank I., Varga N. Robert F., Hau J., Guy P.A., Robert M.C., Riediker S. (2002). Acrylamide from Maillard Reaction Products. Nature, 419(6906): 449-450.
• Referans18 Martins C., Oliveira N.G., Pingarilho M., Costa G.G., Martins V., Marques M.M., Beland F.A., Churchwell M.I., Doerge D.R., Ruef j., Gaspar J.F. (2006). Cytogenetic Damage Induced by Acrylamide and Glycidamide in Mammalian Cells: Correlation with Specific Glycidamide-DNA Adducts. Toxicological Sciences, 95 (2): 383-390.
• Referans19 Zareei S., Boojar M.M.A., Amanlou M. (2017). Inhibition of Liver Alanine Aminotransferase and Aspartate Aminotransferase by Hesperidin and its Aglycone Hesperetin: An in vitro and in Silico Study. Life Sciences, 178: 49-55.
• Referans20 Mayer J., Donnelly T.M., eds.(2013). Clinical Veterinary Advisor: Birds and Exotic Pets. St. Louis, Mo: Elsevier Saunders.
• Referans21 Nagi H.M., Amin W.S.M., and Zaki S.A. (2014). The Potential Effect of Fruits and Vegetables on Liver Functions and Liver Alterations Induced by Acrylamide in Mice. 3 rd International Conference on Nutrition and Food Sciences. IPCBEE [internet]. 5-9.
• Referans22 Mavri-Damelin D., Eaton S., Damelin L.H., Rees M., Hodgson H.J.F., Selden C. (2007). Ornithine Transcarbamylase and Arginase ı Deficiency are Responsible for Diminished Urea Cycle Function in the Human Hepatoblastoma Cell Line Hepg2. The International Journal of Biochemistry & Cell Biology, 39 (3): 555-564.
• Referans23 Jia Y., Lu L., Yuan C., Feng S., Zhu M. (2017). Aspartate Aminotransferase is Potently Inhibited by Copper Complexes: Exploring Copper Complex-Binding Proteome. Journal of Inorganic Biochemistry, 170: 46-54.
• Referans24 Larguinho M., Costa P.M., Sousa G., Costa M.H., Diniz M.S., Baptista P.V. (2014). Histopathological Findings on Carassius auratus Hepatopancreas Upon Exposure to Acrylamide: Correlation with Genotoxicity and Metabolic Alterations. Journal of Applied Toxicology, 34 (12): 1293-1302 (a).
• Referans25 Çınar K. (2010). Subchronic toxicity of acrylamide administered to rats, investigation of the effect of apricot at liver tissue glutathione S-Transferase P (GST-P) Gene Expression, GST, GSH-Px, GSH and MDA levels. Tıpta Uzmanlık Tezi, İnönü Üniversitesi, Sağlık Bilimleri Enstitüsü, Malatya.
• Referans26 Lakshmi D., Gopinath K., Jayanthy G., Anjum S., Prakash D., Sudhandiran G. (2012). Ameliorating Effect of Fish Oil on Acrylamide Induced Oxidative Stress and Neuronal Apoptosis in Cerebral Cortex. Neurochemical Research, 37 (9): 1859-1867.
• Referans27 El‐Beltagi H.S., Ahmed M.M. (2016). Assessment the Protective Role of Quercetin on Acrylamide-Induced Oxidative Stress in Rats. Journal of Food Biochemistry, 40 (6): 715-723.
• Referans28 El-Demerdash F.M., Yousef M.I., Elaswad F.A.M. (2006). Biochemical Study on the Protective Role of Folic Acid in Rabbits Treated with Chromium (VI). Journal of Environmental Science and Health, Part B, 41 (5): 731-746.
• Referans29 Larguinho M., Cordeiro A., Diniz M.S., Costa P.M., Baptista P.V. (2014). Metabolic and Histopathological Alterations in the Marine Bivalve Mytilus Galloprovincialis Induced by Chronic Exposure to Acrylamide. Environmental Research, 135: 55-62 (b).
• Referans30 Awad M.E., Abdel-Rahman M.S., Hassan S.A. (1998). Acrylamide Toxicity in Isolated Rat Hepatocytes. Toxicology in Vitro, 12 (6): 699-704.
• Referans31 Shwetha A., Hosetti B.B., Dube P.N. (2012). Toxic Effects of Zinc Cyanide on Some Protein Metabolites in Fresh Water Fish, Cirrhinus Mrigala (Hamilton). International Journal of Environmental Research, 6 (3): 769-778.
• Referans32 Naveed A., Venkateshwarlu P., Janaiah C. (2010). Impact of Sublethal Concentration of Triazophos on Regulation of Protein Metabolism in the Fish Channa Punctatus (Bloch). African Journal of Biotechnology, 9 (45): 7753-7758.
• Referans33 Altinoz E., Turkoz Y., Vardi N. (2015). The Protective Effect of N-Acetylcysteine Against Acrylamide Toxicity in Liver and Small and Large Intestine Tissues. Bratislavske lekarske listy, 116 (04): 252-258.
• Referans34 Petersen D.W., Cooper K.R., Friedman M.A., Lech J.J. (1987). Behavioral and Histological Effects of Acrylamide in Rainbow Trout. Toxicology and Applied Pharmacology, 87 (1) :177-184.