N-acetyl-β -d-glucosaminidase activity in feral Carcinus maenasexposed to cadmium

Bibliographic Details
Main Author: Mesquita, Sofia Raquel
Publication Date: 2015
Other Authors: Ergen, Şeyda Fikirdeşici, Rodrigues, Aurélie Pinto, Oliva-Teles, M. Teresa, Delerue-Matos, Cristina, Guimarães, Laura
Format: Article
Language: eng
Source: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Download full: http://hdl.handle.net/10400.22/7267
Summary: Cadmium is a priority hazardous substance, persistent in the aquatic environment, with the capacity to interfere with crustacean moulting. Moulting is a vital process dictating crustacean growth, reproduction and metamorphosis. However, for many organisms, moult disruption is difficult to evaluate in the short term, what limits its inclusion in monitoring programmes. N-acetyl-β-d-glucosaminidase (NAGase) is an enzyme acting in the final steps of the endocrine-regulated moulting cascade, allowing for the cast off of the old exoskeleton, with potential interest as a biomarker of moult disruption. This study investigated responses to waterborne cadmium of NAGase activity of Carcinus maenas originating from estuaries with different histories of anthropogenic contamination: a low impacted and a moderately polluted one. Crabs from both sites were individually exposed for seven days to cadmium concentrations ranging from 1.3 to 2000 μg/L. At the end of the assays, NAGase activity was assessed in the epidermis and digestive gland. Detoxification, antioxidant, energy production, and oxidative stress biomarkers implicated in cadmium metabolism and tolerance were also assessed to better understand differential NAGase responses: activity of glutathione S-transferases (GST), glutathione peroxidase (GPx) glutathione reductase (GR), levels of total glutathiones (TG), lipid peroxidation (LPO), lactate dehydrogenase (LDH), and NADP+-dependent isocitrate dehydrogenase (IDH). Animals from the moderately polluted estuary had lower NAGase activity both in the epidermis and digestive gland than in the low impacted site. NAGase activity in the epidermis and digestive gland of C. maenas from both estuaries was sensitive to cadmium exposure suggesting its usefulness for inclusion in monitoring programmes. However, in the digestive gland NAGase inhibition was found in crabs from the less impacted site but not in those from the moderately contaminated one. Altered glutathione levels were observed in cadmium-treated crabs from the contaminated site possibly conferring enhanced tolerance to these animals through its chelator action. Investigation of enhanced tolerance should thus be accounted for in monitoring programmes employing NAGase as biomarker to avoid data misinterpretation.
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spelling N-acetyl-β -d-glucosaminidase activity in feral Carcinus maenasexposed to cadmiumShore crabChitobiaseGlutathioneAnti-oxidant defencesEnvironmental monitoringCadmium is a priority hazardous substance, persistent in the aquatic environment, with the capacity to interfere with crustacean moulting. Moulting is a vital process dictating crustacean growth, reproduction and metamorphosis. However, for many organisms, moult disruption is difficult to evaluate in the short term, what limits its inclusion in monitoring programmes. N-acetyl-β-d-glucosaminidase (NAGase) is an enzyme acting in the final steps of the endocrine-regulated moulting cascade, allowing for the cast off of the old exoskeleton, with potential interest as a biomarker of moult disruption. This study investigated responses to waterborne cadmium of NAGase activity of Carcinus maenas originating from estuaries with different histories of anthropogenic contamination: a low impacted and a moderately polluted one. Crabs from both sites were individually exposed for seven days to cadmium concentrations ranging from 1.3 to 2000 μg/L. At the end of the assays, NAGase activity was assessed in the epidermis and digestive gland. Detoxification, antioxidant, energy production, and oxidative stress biomarkers implicated in cadmium metabolism and tolerance were also assessed to better understand differential NAGase responses: activity of glutathione S-transferases (GST), glutathione peroxidase (GPx) glutathione reductase (GR), levels of total glutathiones (TG), lipid peroxidation (LPO), lactate dehydrogenase (LDH), and NADP+-dependent isocitrate dehydrogenase (IDH). Animals from the moderately polluted estuary had lower NAGase activity both in the epidermis and digestive gland than in the low impacted site. NAGase activity in the epidermis and digestive gland of C. maenas from both estuaries was sensitive to cadmium exposure suggesting its usefulness for inclusion in monitoring programmes. However, in the digestive gland NAGase inhibition was found in crabs from the less impacted site but not in those from the moderately contaminated one. Altered glutathione levels were observed in cadmium-treated crabs from the contaminated site possibly conferring enhanced tolerance to these animals through its chelator action. Investigation of enhanced tolerance should thus be accounted for in monitoring programmes employing NAGase as biomarker to avoid data misinterpretation.ElsevierRepositório Científico do Instituto Politécnico do PortoMesquita, Sofia RaquelErgen, Şeyda FikirdeşiciRodrigues, Aurélie PintoOliva-Teles, M. TeresaDelerue-Matos, CristinaGuimarães, Laura2015-12-28T15:41:39Z2015-022015-02-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.22/7267eng10.1016/j.aquatox.2014.12.008metadata only accessinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-03-13T12:47:38Zoai:recipp.ipp.pt:10400.22/7267Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T17:27:44.978290Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv N-acetyl-β -d-glucosaminidase activity in feral Carcinus maenasexposed to cadmium
title N-acetyl-β -d-glucosaminidase activity in feral Carcinus maenasexposed to cadmium
spellingShingle N-acetyl-β -d-glucosaminidase activity in feral Carcinus maenasexposed to cadmium
Mesquita, Sofia Raquel
Shore crab
Chitobiase
Glutathione
Anti-oxidant defences
Environmental monitoring
title_short N-acetyl-β -d-glucosaminidase activity in feral Carcinus maenasexposed to cadmium
title_full N-acetyl-β -d-glucosaminidase activity in feral Carcinus maenasexposed to cadmium
title_fullStr N-acetyl-β -d-glucosaminidase activity in feral Carcinus maenasexposed to cadmium
title_full_unstemmed N-acetyl-β -d-glucosaminidase activity in feral Carcinus maenasexposed to cadmium
title_sort N-acetyl-β -d-glucosaminidase activity in feral Carcinus maenasexposed to cadmium
author Mesquita, Sofia Raquel
author_facet Mesquita, Sofia Raquel
Ergen, Şeyda Fikirdeşici
Rodrigues, Aurélie Pinto
Oliva-Teles, M. Teresa
Delerue-Matos, Cristina
Guimarães, Laura
author_role author
author2 Ergen, Şeyda Fikirdeşici
Rodrigues, Aurélie Pinto
Oliva-Teles, M. Teresa
Delerue-Matos, Cristina
Guimarães, Laura
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Repositório Científico do Instituto Politécnico do Porto
dc.contributor.author.fl_str_mv Mesquita, Sofia Raquel
Ergen, Şeyda Fikirdeşici
Rodrigues, Aurélie Pinto
Oliva-Teles, M. Teresa
Delerue-Matos, Cristina
Guimarães, Laura
dc.subject.por.fl_str_mv Shore crab
Chitobiase
Glutathione
Anti-oxidant defences
Environmental monitoring
topic Shore crab
Chitobiase
Glutathione
Anti-oxidant defences
Environmental monitoring
description Cadmium is a priority hazardous substance, persistent in the aquatic environment, with the capacity to interfere with crustacean moulting. Moulting is a vital process dictating crustacean growth, reproduction and metamorphosis. However, for many organisms, moult disruption is difficult to evaluate in the short term, what limits its inclusion in monitoring programmes. N-acetyl-β-d-glucosaminidase (NAGase) is an enzyme acting in the final steps of the endocrine-regulated moulting cascade, allowing for the cast off of the old exoskeleton, with potential interest as a biomarker of moult disruption. This study investigated responses to waterborne cadmium of NAGase activity of Carcinus maenas originating from estuaries with different histories of anthropogenic contamination: a low impacted and a moderately polluted one. Crabs from both sites were individually exposed for seven days to cadmium concentrations ranging from 1.3 to 2000 μg/L. At the end of the assays, NAGase activity was assessed in the epidermis and digestive gland. Detoxification, antioxidant, energy production, and oxidative stress biomarkers implicated in cadmium metabolism and tolerance were also assessed to better understand differential NAGase responses: activity of glutathione S-transferases (GST), glutathione peroxidase (GPx) glutathione reductase (GR), levels of total glutathiones (TG), lipid peroxidation (LPO), lactate dehydrogenase (LDH), and NADP+-dependent isocitrate dehydrogenase (IDH). Animals from the moderately polluted estuary had lower NAGase activity both in the epidermis and digestive gland than in the low impacted site. NAGase activity in the epidermis and digestive gland of C. maenas from both estuaries was sensitive to cadmium exposure suggesting its usefulness for inclusion in monitoring programmes. However, in the digestive gland NAGase inhibition was found in crabs from the less impacted site but not in those from the moderately contaminated one. Altered glutathione levels were observed in cadmium-treated crabs from the contaminated site possibly conferring enhanced tolerance to these animals through its chelator action. Investigation of enhanced tolerance should thus be accounted for in monitoring programmes employing NAGase as biomarker to avoid data misinterpretation.
publishDate 2015
dc.date.none.fl_str_mv 2015-12-28T15:41:39Z
2015-02
2015-02-01T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
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dc.identifier.uri.fl_str_mv http://hdl.handle.net/10400.22/7267
url http://hdl.handle.net/10400.22/7267
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1016/j.aquatox.2014.12.008
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dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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