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Chlorothalonil induces oxidative stress and reduces enzymatic activities of Na(+)/K(+)-ATPase and acetylcholinesterase in gill tissues of marine bivalves

Chlorothalonil is a thiol-reactive antifoulant that disperses widely and has been found in the marine environment. However, there is limited information on the deleterious effects of chlorothalonil in marine mollusks. In this study, we evaluated the effects of chlorothalonil on the gill tissues of t...

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Autores principales: Haque, Md. Niamul, Eom, Hye-Jin, Nam, Sang-Eun, Shin, Yun Kyung, Rhee, Jae-Sung
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6456286/
https://www.ncbi.nlm.nih.gov/pubmed/30964867
http://dx.doi.org/10.1371/journal.pone.0214236
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author Haque, Md. Niamul
Eom, Hye-Jin
Nam, Sang-Eun
Shin, Yun Kyung
Rhee, Jae-Sung
author_facet Haque, Md. Niamul
Eom, Hye-Jin
Nam, Sang-Eun
Shin, Yun Kyung
Rhee, Jae-Sung
author_sort Haque, Md. Niamul
collection PubMed
description Chlorothalonil is a thiol-reactive antifoulant that disperses widely and has been found in the marine environment. However, there is limited information on the deleterious effects of chlorothalonil in marine mollusks. In this study, we evaluated the effects of chlorothalonil on the gill tissues of the Pacific oyster, Crassostrea gigas and the blue mussel, Mytilus edulis after exposure to different concentrations of chlorothalonil (0.1, 1, and 10 μg L(−1)) for 96 h. Following exposure to 1 and/or 10 μg L(−1) of chlorothalonil, malondialdehyde (MDA) levels significantly increased in the gill tissues of C. gigas and M. edulis compared to that in the control group at 96 h. Similarly, glutathione (GSH) levels were significantly affected in both bivalves after chlorothalonil exposure. The chlorothalonil treatment caused a significant time- and concentration-dependent increase in the activity of enzymes, such as catalase (CAT), superoxide dismutase (SOD), glutathione peroxidase (GPx), and glutathione reductase (GR), in the antioxidant defense system. Furthermore, 10 μg L(−1) of chlorothalonil resulted in significant inhibitions in the enzymatic activity of Na(+)/K(+)-ATPase and acetylcholinesterase (AChE). These results suggest that chlorothalonil induces potential oxidative stress and changes in osmoregulation and the cholinergic system in bivalve gill tissues. This information will be a useful reference for the potential toxicity of chlorothalonil in marine bivalves.
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spelling pubmed-64562862019-05-03 Chlorothalonil induces oxidative stress and reduces enzymatic activities of Na(+)/K(+)-ATPase and acetylcholinesterase in gill tissues of marine bivalves Haque, Md. Niamul Eom, Hye-Jin Nam, Sang-Eun Shin, Yun Kyung Rhee, Jae-Sung PLoS One Research Article Chlorothalonil is a thiol-reactive antifoulant that disperses widely and has been found in the marine environment. However, there is limited information on the deleterious effects of chlorothalonil in marine mollusks. In this study, we evaluated the effects of chlorothalonil on the gill tissues of the Pacific oyster, Crassostrea gigas and the blue mussel, Mytilus edulis after exposure to different concentrations of chlorothalonil (0.1, 1, and 10 μg L(−1)) for 96 h. Following exposure to 1 and/or 10 μg L(−1) of chlorothalonil, malondialdehyde (MDA) levels significantly increased in the gill tissues of C. gigas and M. edulis compared to that in the control group at 96 h. Similarly, glutathione (GSH) levels were significantly affected in both bivalves after chlorothalonil exposure. The chlorothalonil treatment caused a significant time- and concentration-dependent increase in the activity of enzymes, such as catalase (CAT), superoxide dismutase (SOD), glutathione peroxidase (GPx), and glutathione reductase (GR), in the antioxidant defense system. Furthermore, 10 μg L(−1) of chlorothalonil resulted in significant inhibitions in the enzymatic activity of Na(+)/K(+)-ATPase and acetylcholinesterase (AChE). These results suggest that chlorothalonil induces potential oxidative stress and changes in osmoregulation and the cholinergic system in bivalve gill tissues. This information will be a useful reference for the potential toxicity of chlorothalonil in marine bivalves. Public Library of Science 2019-04-09 /pmc/articles/PMC6456286/ /pubmed/30964867 http://dx.doi.org/10.1371/journal.pone.0214236 Text en © 2019 Haque et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Haque, Md. Niamul
Eom, Hye-Jin
Nam, Sang-Eun
Shin, Yun Kyung
Rhee, Jae-Sung
Chlorothalonil induces oxidative stress and reduces enzymatic activities of Na(+)/K(+)-ATPase and acetylcholinesterase in gill tissues of marine bivalves
title Chlorothalonil induces oxidative stress and reduces enzymatic activities of Na(+)/K(+)-ATPase and acetylcholinesterase in gill tissues of marine bivalves
title_full Chlorothalonil induces oxidative stress and reduces enzymatic activities of Na(+)/K(+)-ATPase and acetylcholinesterase in gill tissues of marine bivalves
title_fullStr Chlorothalonil induces oxidative stress and reduces enzymatic activities of Na(+)/K(+)-ATPase and acetylcholinesterase in gill tissues of marine bivalves
title_full_unstemmed Chlorothalonil induces oxidative stress and reduces enzymatic activities of Na(+)/K(+)-ATPase and acetylcholinesterase in gill tissues of marine bivalves
title_short Chlorothalonil induces oxidative stress and reduces enzymatic activities of Na(+)/K(+)-ATPase and acetylcholinesterase in gill tissues of marine bivalves
title_sort chlorothalonil induces oxidative stress and reduces enzymatic activities of na(+)/k(+)-atpase and acetylcholinesterase in gill tissues of marine bivalves
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6456286/
https://www.ncbi.nlm.nih.gov/pubmed/30964867
http://dx.doi.org/10.1371/journal.pone.0214236
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