Abamectin affects the bioenergetics of liver mitochondria: A potential mechanism of hepatotoxicity
Autor(a) principal: | |
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Data de Publicação: | 2012 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1016/j.tiv.2011.10.007 http://hdl.handle.net/11449/42627 |
Resumo: | Abamectin (ABA) is a macrocyclic lactone of the avermectin family used worldwide as an antiparasitic agent in farm animals and pets and as the active ingredient of insecticides and nematicides. In this study, the effects of abamectin on the bioenergetics of mitochondria isolated from rat liver were evaluated. Mitochondria are responsible for converting the energy released by electron transport and stored as the binding energy molecule ATP. Xenobiotics that interfere with its synthesis or utilization can be acutely or chronically toxic. Abamectin (5-251 mu M) caused concentration-dependent inhibition of the respiratory chain without affecting the membrane potential or the activity of enzymes NADH dehydrogenase or succinate dehydrogenase. This behavior is similar to oligomycin and carboxyatractyloside and suggests direct action on F0F1-ATPase and/or the adenine nucleotide translocator (ANT). ABA more pronouncedly inhibited ATPase phosphohydrolase activity in intact, uncoupled mitochondria than in freeze-thawed disrupted mitochondria. ADP-stimulated depolarization of the mitochondrial membrane potential was also inhibited by ABA. Our results indicate that ABA interacts more specifically with the ANT, resulting in functional inhibition of the translocator with consequent impairment of mitochondria! bioenergetics. This effect could be involved in the ABA toxicity to hepatocytes. (C) 2011 Elsevier Ltd. All rights reserved. |
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Abamectin affects the bioenergetics of liver mitochondria: A potential mechanism of hepatotoxicityAbamectinMitochondriaF0F1-ATPaseOxidative phosphorylationAdenine nucleotide translocatorATP synthesisAbamectin (ABA) is a macrocyclic lactone of the avermectin family used worldwide as an antiparasitic agent in farm animals and pets and as the active ingredient of insecticides and nematicides. In this study, the effects of abamectin on the bioenergetics of mitochondria isolated from rat liver were evaluated. Mitochondria are responsible for converting the energy released by electron transport and stored as the binding energy molecule ATP. Xenobiotics that interfere with its synthesis or utilization can be acutely or chronically toxic. Abamectin (5-251 mu M) caused concentration-dependent inhibition of the respiratory chain without affecting the membrane potential or the activity of enzymes NADH dehydrogenase or succinate dehydrogenase. This behavior is similar to oligomycin and carboxyatractyloside and suggests direct action on F0F1-ATPase and/or the adenine nucleotide translocator (ANT). ABA more pronouncedly inhibited ATPase phosphohydrolase activity in intact, uncoupled mitochondria than in freeze-thawed disrupted mitochondria. ADP-stimulated depolarization of the mitochondrial membrane potential was also inhibited by ABA. Our results indicate that ABA interacts more specifically with the ANT, resulting in functional inhibition of the translocator with consequent impairment of mitochondria! bioenergetics. This effect could be involved in the ABA toxicity to hepatocytes. (C) 2011 Elsevier Ltd. All rights reserved.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Univ Estadual Paulista, UNESP, LaBMeT, BR-17900000 Dracena, SP, BrazilUniv Estadual Paulista, UNESP, LaBMeT, BR-17900000 Dracena, SP, BrazilPergamon-Elsevier B.V. LtdUniversidade Estadual Paulista (Unesp)Castanha Zanoli, Juliana C. [UNESP]Maioli, Marcos A. [UNESP]Medeiros, Hyllana C. D. [UNESP]Mingatto, Fábio Erminio [UNESP]2014-05-20T15:34:42Z2014-05-20T15:34:42Z2012-02-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article51-56application/pdfhttp://dx.doi.org/10.1016/j.tiv.2011.10.007Toxicology In Vitro. Oxford: Pergamon-Elsevier B.V. Ltd, v. 26, n. 1, p. 51-56, 2012.0887-2333http://hdl.handle.net/11449/4262710.1016/j.tiv.2011.10.007WOS:000299713100007WOS000299713100007.pdfWeb of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengToxicology in Vitro3.1050,931info:eu-repo/semantics/openAccess2024-05-07T13:48:06Zoai:repositorio.unesp.br:11449/42627Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-05-07T13:48:06Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Abamectin affects the bioenergetics of liver mitochondria: A potential mechanism of hepatotoxicity |
title |
Abamectin affects the bioenergetics of liver mitochondria: A potential mechanism of hepatotoxicity |
spellingShingle |
Abamectin affects the bioenergetics of liver mitochondria: A potential mechanism of hepatotoxicity Castanha Zanoli, Juliana C. [UNESP] Abamectin Mitochondria F0F1-ATPase Oxidative phosphorylation Adenine nucleotide translocator ATP synthesis |
title_short |
Abamectin affects the bioenergetics of liver mitochondria: A potential mechanism of hepatotoxicity |
title_full |
Abamectin affects the bioenergetics of liver mitochondria: A potential mechanism of hepatotoxicity |
title_fullStr |
Abamectin affects the bioenergetics of liver mitochondria: A potential mechanism of hepatotoxicity |
title_full_unstemmed |
Abamectin affects the bioenergetics of liver mitochondria: A potential mechanism of hepatotoxicity |
title_sort |
Abamectin affects the bioenergetics of liver mitochondria: A potential mechanism of hepatotoxicity |
author |
Castanha Zanoli, Juliana C. [UNESP] |
author_facet |
Castanha Zanoli, Juliana C. [UNESP] Maioli, Marcos A. [UNESP] Medeiros, Hyllana C. D. [UNESP] Mingatto, Fábio Erminio [UNESP] |
author_role |
author |
author2 |
Maioli, Marcos A. [UNESP] Medeiros, Hyllana C. D. [UNESP] Mingatto, Fábio Erminio [UNESP] |
author2_role |
author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) |
dc.contributor.author.fl_str_mv |
Castanha Zanoli, Juliana C. [UNESP] Maioli, Marcos A. [UNESP] Medeiros, Hyllana C. D. [UNESP] Mingatto, Fábio Erminio [UNESP] |
dc.subject.por.fl_str_mv |
Abamectin Mitochondria F0F1-ATPase Oxidative phosphorylation Adenine nucleotide translocator ATP synthesis |
topic |
Abamectin Mitochondria F0F1-ATPase Oxidative phosphorylation Adenine nucleotide translocator ATP synthesis |
description |
Abamectin (ABA) is a macrocyclic lactone of the avermectin family used worldwide as an antiparasitic agent in farm animals and pets and as the active ingredient of insecticides and nematicides. In this study, the effects of abamectin on the bioenergetics of mitochondria isolated from rat liver were evaluated. Mitochondria are responsible for converting the energy released by electron transport and stored as the binding energy molecule ATP. Xenobiotics that interfere with its synthesis or utilization can be acutely or chronically toxic. Abamectin (5-251 mu M) caused concentration-dependent inhibition of the respiratory chain without affecting the membrane potential or the activity of enzymes NADH dehydrogenase or succinate dehydrogenase. This behavior is similar to oligomycin and carboxyatractyloside and suggests direct action on F0F1-ATPase and/or the adenine nucleotide translocator (ANT). ABA more pronouncedly inhibited ATPase phosphohydrolase activity in intact, uncoupled mitochondria than in freeze-thawed disrupted mitochondria. ADP-stimulated depolarization of the mitochondrial membrane potential was also inhibited by ABA. Our results indicate that ABA interacts more specifically with the ANT, resulting in functional inhibition of the translocator with consequent impairment of mitochondria! bioenergetics. This effect could be involved in the ABA toxicity to hepatocytes. (C) 2011 Elsevier Ltd. All rights reserved. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-02-01 2014-05-20T15:34:42Z 2014-05-20T15:34:42Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1016/j.tiv.2011.10.007 Toxicology In Vitro. Oxford: Pergamon-Elsevier B.V. Ltd, v. 26, n. 1, p. 51-56, 2012. 0887-2333 http://hdl.handle.net/11449/42627 10.1016/j.tiv.2011.10.007 WOS:000299713100007 WOS000299713100007.pdf |
url |
http://dx.doi.org/10.1016/j.tiv.2011.10.007 http://hdl.handle.net/11449/42627 |
identifier_str_mv |
Toxicology In Vitro. Oxford: Pergamon-Elsevier B.V. Ltd, v. 26, n. 1, p. 51-56, 2012. 0887-2333 10.1016/j.tiv.2011.10.007 WOS:000299713100007 WOS000299713100007.pdf |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Toxicology in Vitro 3.105 0,931 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
51-56 application/pdf |
dc.publisher.none.fl_str_mv |
Pergamon-Elsevier B.V. Ltd |
publisher.none.fl_str_mv |
Pergamon-Elsevier B.V. Ltd |
dc.source.none.fl_str_mv |
Web of Science reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
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1799965621132197888 |