Pollutants, Snails, Oxidative-Stress, Organophosphates, Metals
Affiliation(s)
Department of Applied Biology and Biochemistry, National University of Science and Technology, Bulawayo, Zimbabwe.
Department of Applied Biology and Biochemistry, National University of Science and Technology, Bulawayo, Zimbabwe.
ABSTRACT
Aquatic reservoirs remain the ultimate sink of chemical pollutants emanating from anthropogenic activities such as agriculture, mining and industry. Freshwater biota undoubtedly is at risk from the adverse effects of these water pollutants and there is therefore, a need to monitor effects of these chemical pollutants in order to safeguard the health of aquatic biota. We investigated the oxidative stress effects of chlorpyrifos and lead on the freshwater snail Helisoma duryi to assess the potential of using this enzyme system as a biondicator of exposure to environmental pollutants. Groups of snails were exposed to 5 ppb lead acetate and 25 ppb chlorpyrifos for 7 days after which half of the snails were sacrificed and the other half were allowed to recover in clean water and sacrificed after another 7 days. Post mitochondrial fractions were used to measure the activities of the following antioxidant enzymes: superoxide dismutase, catalase, glutathione peroxidase, glutathione S-transferase and diphosphotriphosphodiaphorase. Both pollutants enhanced the activities of all the antioxidant enzymes suggesting a defensive mechanism by the snail to combat the oxidative stress due to the organophosphate chlopryrifos and metal pollutant lead. There was a significant recovery of the antioxidant defense system of the snails allowed to recover in clean water shown by the reduced alteration of the antioxidant enzyme activities of the snails allowed to recover for 7 days. This suggests the need to minimize exposure of aquatic biota to chemical pollutants and remediate the polluted water reservoirs in order to safeguard the health of aquatic life.
Aquatic reservoirs remain the ultimate sink of chemical pollutants emanating from anthropogenic activities such as agriculture, mining and industry. Freshwater biota undoubtedly is at risk from the adverse effects of these water pollutants and there is therefore, a need to monitor effects of these chemical pollutants in order to safeguard the health of aquatic biota. We investigated the oxidative stress effects of chlorpyrifos and lead on the freshwater snail Helisoma duryi to assess the potential of using this enzyme system as a biondicator of exposure to environmental pollutants. Groups of snails were exposed to 5 ppb lead acetate and 25 ppb chlorpyrifos for 7 days after which half of the snails were sacrificed and the other half were allowed to recover in clean water and sacrificed after another 7 days. Post mitochondrial fractions were used to measure the activities of the following antioxidant enzymes: superoxide dismutase, catalase, glutathione peroxidase, glutathione S-transferase and diphosphotriphosphodiaphorase. Both pollutants enhanced the activities of all the antioxidant enzymes suggesting a defensive mechanism by the snail to combat the oxidative stress due to the organophosphate chlopryrifos and metal pollutant lead. There was a significant recovery of the antioxidant defense system of the snails allowed to recover in clean water shown by the reduced alteration of the antioxidant enzyme activities of the snails allowed to recover for 7 days. This suggests the need to minimize exposure of aquatic biota to chemical pollutants and remediate the polluted water reservoirs in order to safeguard the health of aquatic life.
Cite this paper
Basopo, N. and Ngabaza, T. (2015) Pollutants, Snails, Oxidative-Stress, Organophosphates, Metals. Advances in Biological Chemistry, 5, 225-233. doi: 10.4236/abc.2015.56019.
Basopo, N. and Ngabaza, T. (2015) Pollutants, Snails, Oxidative-Stress, Organophosphates, Metals. Advances in Biological Chemistry, 5, 225-233. doi: 10.4236/abc.2015.56019.
References
[1] Testai, E., Buratti, F.M. and Consiglio, E.D. (2010) Chlorpyrifos. In: Krieger, R.I., Doull, J., van Hemmen, J.J., Hodgson, E., Maibach, H.I., Ritter, L., Ross, J. and Slikker, W., Eds., Handbook of Pesticide Toxicology, Vol. 2, Elsevier, Burlington, 1505-1526.
http://dx.doi.org/10.1016/b978-0-12-374367-1.00070-7 [2] Nunes, B. (2011) The Use of Cholinesterases in Ecotoxicology. Reviews of Environmental Contamination and Toxicology, 212, 29-59.
http://dx.doi.org/10.1007/978-1-4419-8453-1_2 [3] Wang, C., Lu, G. and Cui, J. (2012) Responses of AChE and GST Activities to Insecticide Coexposure in Carassius auratus. Environmental Toxicology, 27, 50-57.
http://dx.doi.org/10.1002/tox.20612 [4] Ferrari, A., Lascano, C., Pechen de D’Angelo, A.M. and Venturino, A. (2011) Effects of Azinphos Methyl and Carbaryl on Rhinella arenarum Larvae Esterases and Antioxidant Enzymes. Comparative Biochemistry Physiology C and Toxicological Pharmacology, 153, 34-39.
http://dx.doi.org/10.1016/j.cbpc.2010.08.003 [5] Netpae, T., Phalaraksh, C. and Wongkham, W. (2012) Antioxidant Enzyme Activities and DNA Damage as Biomarker of Copper Effect on Corbicula fluminea. Electronic Journal of Biology, 8, 19-23. [6] Company, R., Serafim, A., Bebianno, M.J., Cosson, R., Shillito, B. and Fiala-Médioni, A. (2004) Effect of Cadmium, Copper and Mercury on Antioxidant Enzyme Activities and Lipid Peroxidation in the Gills of the Hydrothermal Vent Mussel Bathymodiolus azoricus. Marine Environmental Research, 58, 377-381.
http://dx.doi.org/10.1016/j.marenvres.2004.03.083 [7] Guidi, P., Frenzilli, G., Benedetti, M., Bernardeshi, M., Falleni, A., Fattorini, D., Reooli, F., Scarcelli, V. and Nigro, M. (2010) Antioxidant, Genotoxic and Lysosomal Biomarkers in the Freshwater Bivalve (Uni pictorum) Transplanted in a Metal Polluted River Basin. Aquatic Toxicology, 100, 75-83.
http://dx.doi.org/10.1016/j.aquatox.2010.07.009 [8] Bianco, K., Yusseppone, M.S., Otero, S., Luquet, C., Rios de Molina, M.C. and Kristoff, G. (2013) Cholinesterase and Neurotoxicity as Highly Sensitive Biomarkers for an Arganophos-phate Insecticide in a Freshwater Gastropod (Chilina gibbosa) with Low Sensitivity Carboxylesterases. Aquatic Toxicology, 26-35, 144-145.
http://dx.doi.org/10.1016/j.aquatox.2013.09.025 [9] Naik, Y.S. and Hasler, J.A. (2002) An Economical Method for the Maintenance of Schistosome Life-Cycle Using Outdoor Facilities. Discovery Innovation, 14, 221-224. [10] Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall, R.J. (1951) Protein Measurement with Folin Phenol Reagent. Journal of Biological Chemistry, 193, 265-275. [11] Sun, Y., Larry, W.O. and Ying, L. (1988) A Simple Method for Clinical Assay of Superoxide Dismutase. Clinical Chemistry, 34, 497-500. [12] Claiborne, A. (1989) Catalase Activity. In: Greeenwald, A.R., Ed., Handbook of Methods for Methods for Oxygen Radical Research, CRC Press Inc., Boca Raton, 283-284. [13] Flohe, L. and Gunzler, W.A. (1984) Assays of Glutathione Peroxidase. Methods in Enzymology, 105, 114-121.
http://dx.doi.org/10.1016/S0076-6879(84)05015-1 [14] Habig, W.H., Pabst, M.J. and Jakoby, W.B. (1974) Glutathione S-Transferases. Journal of Biological Chemistry, 349, 7130-7139. [15] Lind, C., Cadenas, E., Hochstein, P. and Ernster, L. (1990) DT Diaphorase: Purification, Properties and Function. Methods in Enzymology, 186, 287-301.
http://dx.doi.org/10.1016/0076-6879(90)86122-C [16] Pimentel, D. and Burgess, M. (2012) Small Amounts of Pesticides Reaching Target Insects. Environment Development and Sustainability Journal, 14, 1-2. http://dx.doi.org/10.1007/s10668-011-9325-5 [17] Patra, R.C., Rautray, A.K. and Swarup, D. (2011) Oxidative Stress in Lead and Cadmium Toxicity and Its Amelioration. Veterinary Medicine International Journal, 2011, Article ID: 457327.
http://dx.doi.org/10.4061/2011/457327 [18] Radwan, M.A., El-Gendy, K.S. and Gad, A.F. (2010) Oxidative Stress Biomarkers in the Digestive Gland of Theba pisana Exposed to Heavy Metals. Archives of Environmental Contamination Toxicology, 58, 828-835.
http://dx.doi.org/10.1007/s00244-009-9380-1 [19] Rajkumar, J.S.I. and Milton, M.C.J. (2011) Biochemical Changes Induced by Cadmium, Copper, Lead and Zinc Exposure to Perna Viridis under Long Term Toxicity Test. International Journal of Pharmacology and Biosciences, 2. [20] Nowakowska, A., Laciak, M. and Capula, M. (2011) Organ Profile of the Antioxidant Defense System and Accumulation of Metals in Helix aspersa Snails. Polish Journal of Environmental Studies, 21, 1369-1375. [21] Alhifi, M.A., Khan, M.Z. and Gholem V.S. (2005) Effect of Dimethoate 30% EC on Antioxidant Enzymes in Chick Embryo Brain, Liver and Heart. International Medical Journal, 4. [22] El-Gendy, K.S., Radwan, M.A. and Gad, A.F. (2009) In Vivo Evaluation of Oxidative Stress Biomarkers in the Land Snail, Theba pisana Exposed to Copper-Based Pesticides. Chemosphere, 77, 339-344.
http://dx.doi.org/10.1016/j.chemosphere.2009.07.015 [23] El-Shenawy, N. and Amaal, M. (2012) Using En-zymatic and Nonenzyamatic Antioxidant Defense Systems of the Land Snail Eobonia vermiculata as Biomarkers of Terrestrial Heavy Metal Pollution. Ecotoxicology and Environmental Safety, 84, 347-354.
http://dx.doi.org/10.1016/j.ecoenv.2012.08.014 [24] Verlecar, X.N., Jena, K.B. and Chainy, G.B.N. (2008) Modulation of Antioxidant Defences in Digestive Gland of Perna viridis on Mercury Exposures. Chemosphere, 71, 1977-1985. [25] Leveelahti, L., Rytkonen, K.T., Renshaw, G.M.C. and Nikinmaa, M. (2013) Revisiting Redox-Active Antioxidant Defenses in Response to Hypoxic Challenge in Both Hypoxia-Tolerant and Hypoxia-Sensitive. Fish Species Fish Physiology and Biochemistry, 40, 183-191.
http://dx.doi.org/10.1007/s10695-013-9835-1 [26] Vontas, J.G., Small, G.J. and Hemingway, J. (2001) Glutathione S-Transferases as Antioxidant Defense Agents Confer Pyrethroid Resistance in Nilaparvata lugens. Biochemical Journal, 357, 65-72.
http://dx.doi.org/10.1042/bj3570065 [27] Porte, C.S., Albaiges, M.J. and Livingstone, D.R. (1991) Responses of Mixed Function Oxygenase and Antioxidase Enzyme System of Mytilus sp. to Organic Pollution. Comparative Biochemistry and Physiology, 100C, 183-186. [28] U.S. EPA (U.S. Environmental Protection Agency) (1999) Chlorpyrifos: HED Preliminary Risk Assessment for the Reregistration Eligibility Decision (RED) Document. Chemical No. 059101. Barcode: D260163, Case: 818975, Submission: S568580. [29] Valavanidis, A., Vlahogianni, T., Dassenakis, M. and Scoullos, M. (2006) Molecular Biomarkers of Oxidative Stress in Aquatic Organisms in Relation to Toxic Environmental Pollutants. Ecotoxicology and Environmental Safety, 64, 178- 189.
http://dx.doi.org/10.1016/j.ecoenv.2005.03.013 [30] Salama, A.K., Khaled, A.O., Nabia, A., Saber, Salim S.A. (2005) Oxidative Stress Induced by Different Pesticides in Land Snails Helix aspersa. Pakistan Journal of Biological Sciences, 8, 92-96.
http://dx.doi.org/10.3923/pjbs.2005.92.96 [31] Leomanni, A., Schettino, T., Calisi, A., Gorbi, S., Mezzelani, M., Regoli, F. and Lionetto, M.G. (2015) Antioxidant and Oxidative Stress Related Responses in the Mediterranean Land Snail Cantareus apertus Exposed to the Carbamate Pesticide Carbaryl. Comparative Biochemistry and Physiology C, 168, 20-27.
http://dx.doi.org/10.1016/j.cbpc.2014.11.003 [32] Khalil, A.M. (2015) Toxicological Effects and Oxidative Stress Responses in Freshwater Snail Lanistes carinatus Following Exposure to Chlorpyrifos. Ecotoxicology and Environmental Safety Volume, 116, 137-142.
http://dx.doi.org/10.1016/j.ecoenv.2015.03.010 [33] Ma, J., Zhou, C., Li, Y. and Li, X. (2014) Biochemical Responses to the Toxicity of the Biocide Abamectin on the Freshwater Snail Physa acuta. Ecotoxicology and Environmental Safety, 101, 31-33.
http://dx.doi.org/10.1016/j.ecoenv.2013.12.009 [34] Kavitha, P. and Venkateswara Rao, J. (2009) Sub-Lethal Effects of Profenofos on Tissue-Specific Antioxidative Responses in a Euryhyaline Fish, Oreochromis mossambicus. Ecotoxicology and Environmental Safety, 72, 1727-1733.
http://dx.doi.org/10.1016/j.ecoenv.2009.05.010 [35] Siegel, D., Gustafson, D.L., Dehn, D.L., Han, J.Y., Boonchoong, P., Berliner, L.J. and Ross, D. (2004) NAD(P)H: Quinone Oxidoreductase 1: Role as a Superoxide Scavenger. Molecular Pharmacology, 65, 1238-1247.
http://dx.doi.org/10.1124/mol.65.5.1238
[1] Testai, E., Buratti, F.M. and Consiglio, E.D. (2010) Chlorpyrifos. In: Krieger, R.I., Doull, J., van Hemmen, J.J., Hodgson, E., Maibach, H.I., Ritter, L., Ross, J. and Slikker, W., Eds., Handbook of Pesticide Toxicology, Vol. 2, Elsevier, Burlington, 1505-1526.
http://dx.doi.org/10.1016/b978-0-12-374367-1.00070-7 [2] Nunes, B. (2011) The Use of Cholinesterases in Ecotoxicology. Reviews of Environmental Contamination and Toxicology, 212, 29-59.
http://dx.doi.org/10.1007/978-1-4419-8453-1_2 [3] Wang, C., Lu, G. and Cui, J. (2012) Responses of AChE and GST Activities to Insecticide Coexposure in Carassius auratus. Environmental Toxicology, 27, 50-57.
http://dx.doi.org/10.1002/tox.20612 [4] Ferrari, A., Lascano, C., Pechen de D’Angelo, A.M. and Venturino, A. (2011) Effects of Azinphos Methyl and Carbaryl on Rhinella arenarum Larvae Esterases and Antioxidant Enzymes. Comparative Biochemistry Physiology C and Toxicological Pharmacology, 153, 34-39.
http://dx.doi.org/10.1016/j.cbpc.2010.08.003 [5] Netpae, T., Phalaraksh, C. and Wongkham, W. (2012) Antioxidant Enzyme Activities and DNA Damage as Biomarker of Copper Effect on Corbicula fluminea. Electronic Journal of Biology, 8, 19-23. [6] Company, R., Serafim, A., Bebianno, M.J., Cosson, R., Shillito, B. and Fiala-Médioni, A. (2004) Effect of Cadmium, Copper and Mercury on Antioxidant Enzyme Activities and Lipid Peroxidation in the Gills of the Hydrothermal Vent Mussel Bathymodiolus azoricus. Marine Environmental Research, 58, 377-381.
http://dx.doi.org/10.1016/j.marenvres.2004.03.083 [7] Guidi, P., Frenzilli, G., Benedetti, M., Bernardeshi, M., Falleni, A., Fattorini, D., Reooli, F., Scarcelli, V. and Nigro, M. (2010) Antioxidant, Genotoxic and Lysosomal Biomarkers in the Freshwater Bivalve (Uni pictorum) Transplanted in a Metal Polluted River Basin. Aquatic Toxicology, 100, 75-83.
http://dx.doi.org/10.1016/j.aquatox.2010.07.009 [8] Bianco, K., Yusseppone, M.S., Otero, S., Luquet, C., Rios de Molina, M.C. and Kristoff, G. (2013) Cholinesterase and Neurotoxicity as Highly Sensitive Biomarkers for an Arganophos-phate Insecticide in a Freshwater Gastropod (Chilina gibbosa) with Low Sensitivity Carboxylesterases. Aquatic Toxicology, 26-35, 144-145.
http://dx.doi.org/10.1016/j.aquatox.2013.09.025 [9] Naik, Y.S. and Hasler, J.A. (2002) An Economical Method for the Maintenance of Schistosome Life-Cycle Using Outdoor Facilities. Discovery Innovation, 14, 221-224. [10] Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall, R.J. (1951) Protein Measurement with Folin Phenol Reagent. Journal of Biological Chemistry, 193, 265-275. [11] Sun, Y., Larry, W.O. and Ying, L. (1988) A Simple Method for Clinical Assay of Superoxide Dismutase. Clinical Chemistry, 34, 497-500. [12] Claiborne, A. (1989) Catalase Activity. In: Greeenwald, A.R., Ed., Handbook of Methods for Methods for Oxygen Radical Research, CRC Press Inc., Boca Raton, 283-284. [13] Flohe, L. and Gunzler, W.A. (1984) Assays of Glutathione Peroxidase. Methods in Enzymology, 105, 114-121.
http://dx.doi.org/10.1016/S0076-6879(84)05015-1 [14] Habig, W.H., Pabst, M.J. and Jakoby, W.B. (1974) Glutathione S-Transferases. Journal of Biological Chemistry, 349, 7130-7139. [15] Lind, C., Cadenas, E., Hochstein, P. and Ernster, L. (1990) DT Diaphorase: Purification, Properties and Function. Methods in Enzymology, 186, 287-301.
http://dx.doi.org/10.1016/0076-6879(90)86122-C [16] Pimentel, D. and Burgess, M. (2012) Small Amounts of Pesticides Reaching Target Insects. Environment Development and Sustainability Journal, 14, 1-2. http://dx.doi.org/10.1007/s10668-011-9325-5 [17] Patra, R.C., Rautray, A.K. and Swarup, D. (2011) Oxidative Stress in Lead and Cadmium Toxicity and Its Amelioration. Veterinary Medicine International Journal, 2011, Article ID: 457327.
http://dx.doi.org/10.4061/2011/457327 [18] Radwan, M.A., El-Gendy, K.S. and Gad, A.F. (2010) Oxidative Stress Biomarkers in the Digestive Gland of Theba pisana Exposed to Heavy Metals. Archives of Environmental Contamination Toxicology, 58, 828-835.
http://dx.doi.org/10.1007/s00244-009-9380-1 [19] Rajkumar, J.S.I. and Milton, M.C.J. (2011) Biochemical Changes Induced by Cadmium, Copper, Lead and Zinc Exposure to Perna Viridis under Long Term Toxicity Test. International Journal of Pharmacology and Biosciences, 2. [20] Nowakowska, A., Laciak, M. and Capula, M. (2011) Organ Profile of the Antioxidant Defense System and Accumulation of Metals in Helix aspersa Snails. Polish Journal of Environmental Studies, 21, 1369-1375. [21] Alhifi, M.A., Khan, M.Z. and Gholem V.S. (2005) Effect of Dimethoate 30% EC on Antioxidant Enzymes in Chick Embryo Brain, Liver and Heart. International Medical Journal, 4. [22] El-Gendy, K.S., Radwan, M.A. and Gad, A.F. (2009) In Vivo Evaluation of Oxidative Stress Biomarkers in the Land Snail, Theba pisana Exposed to Copper-Based Pesticides. Chemosphere, 77, 339-344.
http://dx.doi.org/10.1016/j.chemosphere.2009.07.015 [23] El-Shenawy, N. and Amaal, M. (2012) Using En-zymatic and Nonenzyamatic Antioxidant Defense Systems of the Land Snail Eobonia vermiculata as Biomarkers of Terrestrial Heavy Metal Pollution. Ecotoxicology and Environmental Safety, 84, 347-354.
http://dx.doi.org/10.1016/j.ecoenv.2012.08.014 [24] Verlecar, X.N., Jena, K.B. and Chainy, G.B.N. (2008) Modulation of Antioxidant Defences in Digestive Gland of Perna viridis on Mercury Exposures. Chemosphere, 71, 1977-1985. [25] Leveelahti, L., Rytkonen, K.T., Renshaw, G.M.C. and Nikinmaa, M. (2013) Revisiting Redox-Active Antioxidant Defenses in Response to Hypoxic Challenge in Both Hypoxia-Tolerant and Hypoxia-Sensitive. Fish Species Fish Physiology and Biochemistry, 40, 183-191.
http://dx.doi.org/10.1007/s10695-013-9835-1 [26] Vontas, J.G., Small, G.J. and Hemingway, J. (2001) Glutathione S-Transferases as Antioxidant Defense Agents Confer Pyrethroid Resistance in Nilaparvata lugens. Biochemical Journal, 357, 65-72.
http://dx.doi.org/10.1042/bj3570065 [27] Porte, C.S., Albaiges, M.J. and Livingstone, D.R. (1991) Responses of Mixed Function Oxygenase and Antioxidase Enzyme System of Mytilus sp. to Organic Pollution. Comparative Biochemistry and Physiology, 100C, 183-186. [28] U.S. EPA (U.S. Environmental Protection Agency) (1999) Chlorpyrifos: HED Preliminary Risk Assessment for the Reregistration Eligibility Decision (RED) Document. Chemical No. 059101. Barcode: D260163, Case: 818975, Submission: S568580. [29] Valavanidis, A., Vlahogianni, T., Dassenakis, M. and Scoullos, M. (2006) Molecular Biomarkers of Oxidative Stress in Aquatic Organisms in Relation to Toxic Environmental Pollutants. Ecotoxicology and Environmental Safety, 64, 178- 189.
http://dx.doi.org/10.1016/j.ecoenv.2005.03.013 [30] Salama, A.K., Khaled, A.O., Nabia, A., Saber, Salim S.A. (2005) Oxidative Stress Induced by Different Pesticides in Land Snails Helix aspersa. Pakistan Journal of Biological Sciences, 8, 92-96.
http://dx.doi.org/10.3923/pjbs.2005.92.96 [31] Leomanni, A., Schettino, T., Calisi, A., Gorbi, S., Mezzelani, M., Regoli, F. and Lionetto, M.G. (2015) Antioxidant and Oxidative Stress Related Responses in the Mediterranean Land Snail Cantareus apertus Exposed to the Carbamate Pesticide Carbaryl. Comparative Biochemistry and Physiology C, 168, 20-27.
http://dx.doi.org/10.1016/j.cbpc.2014.11.003 [32] Khalil, A.M. (2015) Toxicological Effects and Oxidative Stress Responses in Freshwater Snail Lanistes carinatus Following Exposure to Chlorpyrifos. Ecotoxicology and Environmental Safety Volume, 116, 137-142.
http://dx.doi.org/10.1016/j.ecoenv.2015.03.010 [33] Ma, J., Zhou, C., Li, Y. and Li, X. (2014) Biochemical Responses to the Toxicity of the Biocide Abamectin on the Freshwater Snail Physa acuta. Ecotoxicology and Environmental Safety, 101, 31-33.
http://dx.doi.org/10.1016/j.ecoenv.2013.12.009 [34] Kavitha, P. and Venkateswara Rao, J. (2009) Sub-Lethal Effects of Profenofos on Tissue-Specific Antioxidative Responses in a Euryhyaline Fish, Oreochromis mossambicus. Ecotoxicology and Environmental Safety, 72, 1727-1733.
http://dx.doi.org/10.1016/j.ecoenv.2009.05.010 [35] Siegel, D., Gustafson, D.L., Dehn, D.L., Han, J.Y., Boonchoong, P., Berliner, L.J. and Ross, D. (2004) NAD(P)H: Quinone Oxidoreductase 1: Role as a Superoxide Scavenger. Molecular Pharmacology, 65, 1238-1247.
http://dx.doi.org/10.1124/mol.65.5.1238