Acetilcolinesterase, butirilcolinesterase, carboxilesterase e a resistência de peixes neotropicais aos pesticidas organofosforados

Detalhes bibliográficos
Autor(a) principal: Fraga, Aline Simões
Data de Publicação: 2010
Tipo de documento: Tese
Idioma: por
Título da fonte: Biblioteca Digital de Teses e Dissertações da UERJ
Texto Completo: http://www.bdtd.uerj.br/handle/1/16206
Resumo: Every human group who organizes to work together uses rivers, lakes or ponds as places in which undesirable substances are deposited for decomposition. Contamination of the aquatic environment with herbicides and pesticides derived from agricultural practices has become a problem of global importance since a long ago. We need detailed information on the biochemistry of the poisoning of native fish to assess the effects of pesticides on the biochemical processes that maintain fishes life cycle in waters of Brazil. Organophosphates, which are widely used pesticides, can interact with the B-esterases butyrylcholinesterase (EC 3.1.1.8) and carboxylesterase (EC 3.1.1.1) in plasma and liver. Butyrylcholinesterase (BChE) and carboxylesterase (CarbE) in relatively high concentrations act as stoichiometric scavengers by linking the phosphorus atom of the P=O group with the serine s hydroxyl they have in their active site. Our results show that the CarbE of curimbata plasma (IC50 74 ηm) is more sensitive to the organophosphate metilparaoxon than CarbE of pacu plasma (IC50 691 ηm). We isolated CarbE from curimbata and pacu s plasma. Piavussu does not have an expressive activity of CarbE in plasma, so we did not isolate it. The type and distribution of esterases in tissues are peculiar to a species. Curimbata has high CarbE activity in the liver (237.8 U.g-1) and blood (29.85 U.mL-1), pacu is equipped with high activities of BChE (134.0 U.g-1) and CarbE (149.6 U.g-1) in the liver and piavussu relies only on BChE of blood (17.87 U.g-1). This enzymatic arsenal was sufficient to protect AChE from brain, muscle and heart of the three species and protect them against mild intoxication by methylparathion (0.2 mg / L). The biochemical kinetic approach that allows understanding of the inhibition of the esterases in tissues of different fish species is a good tool capable of anticipating the harmful consequences of these drugs.
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spelling Bastos Neto, Jayme da Cunhahttp://lattes.cnpq.br/4733020887440354Waichmann, Andrea Vivianahttp://lattes.cnpq.br/0909284292846498Faria, Mauro Velho de Castrohttp://lattes.cnpq.br/3264626864573978Valente, Richard Hemmihttp://lattes.cnpq.br/2586326937843589Bastos, Wanderley Rodrigueshttp://lattes.cnpq.br/4028993334703256Sodré, Cátia Lacerdahttp://lattes.cnpq.br/2482175145348592http://lattes.cnpq.br/5569619171424831Fraga, Aline Simões2021-04-26T01:12:17Z2010-09-292010-03-04FRAGA, Aline Simões. Acetilcolinesterase, butirilcolinesterase, carboxilesterase e a resistência de peixes neotropicais aos pesticidas organofosforados. 2010. 98 f. Tese (Doutorado em Biociências) - Instituto de Biologia Roberto Alcantara Gomes, Universidade do Estado do Rio de Janeiro, Rio de Janeiro, 2010.http://www.bdtd.uerj.br/handle/1/16206Every human group who organizes to work together uses rivers, lakes or ponds as places in which undesirable substances are deposited for decomposition. Contamination of the aquatic environment with herbicides and pesticides derived from agricultural practices has become a problem of global importance since a long ago. We need detailed information on the biochemistry of the poisoning of native fish to assess the effects of pesticides on the biochemical processes that maintain fishes life cycle in waters of Brazil. Organophosphates, which are widely used pesticides, can interact with the B-esterases butyrylcholinesterase (EC 3.1.1.8) and carboxylesterase (EC 3.1.1.1) in plasma and liver. Butyrylcholinesterase (BChE) and carboxylesterase (CarbE) in relatively high concentrations act as stoichiometric scavengers by linking the phosphorus atom of the P=O group with the serine s hydroxyl they have in their active site. Our results show that the CarbE of curimbata plasma (IC50 74 ηm) is more sensitive to the organophosphate metilparaoxon than CarbE of pacu plasma (IC50 691 ηm). We isolated CarbE from curimbata and pacu s plasma. Piavussu does not have an expressive activity of CarbE in plasma, so we did not isolate it. The type and distribution of esterases in tissues are peculiar to a species. Curimbata has high CarbE activity in the liver (237.8 U.g-1) and blood (29.85 U.mL-1), pacu is equipped with high activities of BChE (134.0 U.g-1) and CarbE (149.6 U.g-1) in the liver and piavussu relies only on BChE of blood (17.87 U.g-1). This enzymatic arsenal was sufficient to protect AChE from brain, muscle and heart of the three species and protect them against mild intoxication by methylparathion (0.2 mg / L). The biochemical kinetic approach that allows understanding of the inhibition of the esterases in tissues of different fish species is a good tool capable of anticipating the harmful consequences of these drugs.Todos os agrupamentos humanos que se organizam para o trabalho usam rios, lagos ou lagoas como depósitos para a decomposição de matéria indesejável. A contaminação do meio aquático por herbicidas e agrotóxicos derivados de práticas agrícolas se tornou, faz tempo, um problema de importância mundial. Precisamos de informações detalhadas sobre a bioquímica da intoxicação de peixes nativos para avaliarmos quais os efeitos de agrotóxicos sobre os processos bioquímicos que mantêm o ciclo de vida dos peixes em águas do Brasil. Organofosfatos, que são agrotóxicos de uso disseminado, podem interagir com as B-esterases butirilcolinesterase (EC 3.1.1.8) e carboxilesterase (EC 3.1.1.1) presentes no fígado e no plasma. Tanto a butirilcolinesterase (BChE) como a carboxilesterase (CarbE), se presentes em concentrações relativamente elevadas, agem como limpadores estequiométricos ( scavengers moleculares) por ligarem o átomo de fósforo do grupo P=O com a hidroxila de uma serina presente nos seus sítios ativos. Em nossos resultados observamos que curimbatá possui a CarbE plasmática (IC50 74 ηM) mais sensível ao organofosfato metilparaoxon quando comparado ao pacu (IC50 691 ηM). Isolamos CarbE dos plasmas de curimbatá e pacu. Piavussu não possui uma atividade expressiva de CarbE no sangue, por isso não a isolamos. O tipo e a distribuição das esterases nos tecidos são particulares da espécie. Curimbatá tem alta atividade de CarbE no fígado (237,8 U.g-1) e no sangue (29,85 U.mL-1), pacu é dotado de alta atividade de BChE (134,0 U.g-1) e CarbE (149,6 U.g-1) no fígado, mas o piavussu conta apenas com a BChE do sangue (17,87 U.g-1). Este arsenal enzimático foi suficiente para proteger as AChE de cérebro, músculo e coração das três espécies e evitar a sua intoxicação leve por 0,2 mg metilparation/L. A abordagem cinético-bioquímica para conhecer a inibição das esterases presentes nos tecidos de diferentes espécies de peixes porSubmitted by Boris INFORMAT (boris@uerj.br) on 2021-04-26T01:12:17Z No. of bitstreams: 1 Tese Doutorado - Aline Simoes Fraga.pdf: 1430552 bytes, checksum: 0a4e11e5de980d226d4a5e98945ca980 (MD5)Made available in DSpace on 2021-04-26T01:12:17Z (GMT). No. of bitstreams: 1 Tese Doutorado - Aline Simoes Fraga.pdf: 1430552 bytes, checksum: 0a4e11e5de980d226d4a5e98945ca980 (MD5) Previous issue date: 2010-03-04application/pdfporUniversidade do Estado do Rio de JaneiroPrograma de Pós-Graduação em BiociênciasUERJBRCentro Biomédico::Instituto de Biologia Roberto Alcantara GomesAetylcholinesteraseButyrylcholinesteraseCarboxylesteraseCurimbataPiavussuPeixe - Efeito dos pesticidasCinéticaSangueAcetilcolinesteraseButirilcolinesteraseCarboxilesteraseCurimbatáPacu (Peixe)PiavussuCNPQ::CIENCIAS BIOLOGICAS::BIOQUIMICAAcetilcolinesterase, butirilcolinesterase, carboxilesterase e a resistência de peixes neotropicais aos pesticidas organofosforadosAcetylcholinesterase, butyrylcholinesterase, carboxylesterase and the resistenance of neotropical fishes to organophosphorus pesticidesinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/doctoralThesisinfo:eu-repo/semantics/openAccessreponame:Biblioteca Digital de Teses e Dissertações da UERJinstname:Universidade do Estado do Rio de Janeiro (UERJ)instacron:UERJORIGINALTese - Aline Simoes Fraga - 2010 - Completa.pdfapplication/pdf1430552http://www.bdtd.uerj.br/bitstream/1/16206/1/Tese+-+Aline+Simoes+Fraga+-+2010+-+Completa.pdf0a4e11e5de980d226d4a5e98945ca980MD511/162062024-02-26 11:25:02.187oai:www.bdtd.uerj.br:1/16206Biblioteca Digital de Teses e Dissertaçõeshttp://www.bdtd.uerj.br/PUBhttps://www.bdtd.uerj.br:8443/oai/requestbdtd.suporte@uerj.bropendoar:29032024-02-26T14:25:02Biblioteca Digital de Teses e Dissertações da UERJ - Universidade do Estado do Rio de Janeiro (UERJ)false
dc.title.por.fl_str_mv Acetilcolinesterase, butirilcolinesterase, carboxilesterase e a resistência de peixes neotropicais aos pesticidas organofosforados
dc.title.alternative.eng.fl_str_mv Acetylcholinesterase, butyrylcholinesterase, carboxylesterase and the resistenance of neotropical fishes to organophosphorus pesticides
title Acetilcolinesterase, butirilcolinesterase, carboxilesterase e a resistência de peixes neotropicais aos pesticidas organofosforados
spellingShingle Acetilcolinesterase, butirilcolinesterase, carboxilesterase e a resistência de peixes neotropicais aos pesticidas organofosforados
Fraga, Aline Simões
Aetylcholinesterase
Butyrylcholinesterase
Carboxylesterase
Curimbata
Piavussu
Peixe - Efeito dos pesticidas
Cinética
Sangue
Acetilcolinesterase
Butirilcolinesterase
Carboxilesterase
Curimbatá
Pacu (Peixe)
Piavussu
CNPQ::CIENCIAS BIOLOGICAS::BIOQUIMICA
title_short Acetilcolinesterase, butirilcolinesterase, carboxilesterase e a resistência de peixes neotropicais aos pesticidas organofosforados
title_full Acetilcolinesterase, butirilcolinesterase, carboxilesterase e a resistência de peixes neotropicais aos pesticidas organofosforados
title_fullStr Acetilcolinesterase, butirilcolinesterase, carboxilesterase e a resistência de peixes neotropicais aos pesticidas organofosforados
title_full_unstemmed Acetilcolinesterase, butirilcolinesterase, carboxilesterase e a resistência de peixes neotropicais aos pesticidas organofosforados
title_sort Acetilcolinesterase, butirilcolinesterase, carboxilesterase e a resistência de peixes neotropicais aos pesticidas organofosforados
author Fraga, Aline Simões
author_facet Fraga, Aline Simões
author_role author
dc.contributor.advisor1.fl_str_mv Bastos Neto, Jayme da Cunha
dc.contributor.advisor1Lattes.fl_str_mv http://lattes.cnpq.br/4733020887440354
dc.contributor.referee1.fl_str_mv Waichmann, Andrea Viviana
dc.contributor.referee1Lattes.fl_str_mv http://lattes.cnpq.br/0909284292846498
dc.contributor.referee2.fl_str_mv Faria, Mauro Velho de Castro
dc.contributor.referee2Lattes.fl_str_mv http://lattes.cnpq.br/3264626864573978
dc.contributor.referee3.fl_str_mv Valente, Richard Hemmi
dc.contributor.referee3Lattes.fl_str_mv http://lattes.cnpq.br/2586326937843589
dc.contributor.referee4.fl_str_mv Bastos, Wanderley Rodrigues
dc.contributor.referee4Lattes.fl_str_mv http://lattes.cnpq.br/4028993334703256
dc.contributor.referee5.fl_str_mv Sodré, Cátia Lacerda
dc.contributor.referee5Lattes.fl_str_mv http://lattes.cnpq.br/2482175145348592
dc.contributor.authorLattes.fl_str_mv http://lattes.cnpq.br/5569619171424831
dc.contributor.author.fl_str_mv Fraga, Aline Simões
contributor_str_mv Bastos Neto, Jayme da Cunha
Waichmann, Andrea Viviana
Faria, Mauro Velho de Castro
Valente, Richard Hemmi
Bastos, Wanderley Rodrigues
Sodré, Cátia Lacerda
dc.subject.eng.fl_str_mv Aetylcholinesterase
Butyrylcholinesterase
Carboxylesterase
Curimbata
Piavussu
topic Aetylcholinesterase
Butyrylcholinesterase
Carboxylesterase
Curimbata
Piavussu
Peixe - Efeito dos pesticidas
Cinética
Sangue
Acetilcolinesterase
Butirilcolinesterase
Carboxilesterase
Curimbatá
Pacu (Peixe)
Piavussu
CNPQ::CIENCIAS BIOLOGICAS::BIOQUIMICA
dc.subject.por.fl_str_mv Peixe - Efeito dos pesticidas
Cinética
Sangue
Acetilcolinesterase
Butirilcolinesterase
Carboxilesterase
Curimbatá
Pacu (Peixe)
Piavussu
dc.subject.cnpq.fl_str_mv CNPQ::CIENCIAS BIOLOGICAS::BIOQUIMICA
description Every human group who organizes to work together uses rivers, lakes or ponds as places in which undesirable substances are deposited for decomposition. Contamination of the aquatic environment with herbicides and pesticides derived from agricultural practices has become a problem of global importance since a long ago. We need detailed information on the biochemistry of the poisoning of native fish to assess the effects of pesticides on the biochemical processes that maintain fishes life cycle in waters of Brazil. Organophosphates, which are widely used pesticides, can interact with the B-esterases butyrylcholinesterase (EC 3.1.1.8) and carboxylesterase (EC 3.1.1.1) in plasma and liver. Butyrylcholinesterase (BChE) and carboxylesterase (CarbE) in relatively high concentrations act as stoichiometric scavengers by linking the phosphorus atom of the P=O group with the serine s hydroxyl they have in their active site. Our results show that the CarbE of curimbata plasma (IC50 74 ηm) is more sensitive to the organophosphate metilparaoxon than CarbE of pacu plasma (IC50 691 ηm). We isolated CarbE from curimbata and pacu s plasma. Piavussu does not have an expressive activity of CarbE in plasma, so we did not isolate it. The type and distribution of esterases in tissues are peculiar to a species. Curimbata has high CarbE activity in the liver (237.8 U.g-1) and blood (29.85 U.mL-1), pacu is equipped with high activities of BChE (134.0 U.g-1) and CarbE (149.6 U.g-1) in the liver and piavussu relies only on BChE of blood (17.87 U.g-1). This enzymatic arsenal was sufficient to protect AChE from brain, muscle and heart of the three species and protect them against mild intoxication by methylparathion (0.2 mg / L). The biochemical kinetic approach that allows understanding of the inhibition of the esterases in tissues of different fish species is a good tool capable of anticipating the harmful consequences of these drugs.
publishDate 2010
dc.date.available.fl_str_mv 2010-09-29
dc.date.issued.fl_str_mv 2010-03-04
dc.date.accessioned.fl_str_mv 2021-04-26T01:12:17Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/doctoralThesis
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dc.identifier.citation.fl_str_mv FRAGA, Aline Simões. Acetilcolinesterase, butirilcolinesterase, carboxilesterase e a resistência de peixes neotropicais aos pesticidas organofosforados. 2010. 98 f. Tese (Doutorado em Biociências) - Instituto de Biologia Roberto Alcantara Gomes, Universidade do Estado do Rio de Janeiro, Rio de Janeiro, 2010.
dc.identifier.uri.fl_str_mv http://www.bdtd.uerj.br/handle/1/16206
identifier_str_mv FRAGA, Aline Simões. Acetilcolinesterase, butirilcolinesterase, carboxilesterase e a resistência de peixes neotropicais aos pesticidas organofosforados. 2010. 98 f. Tese (Doutorado em Biociências) - Instituto de Biologia Roberto Alcantara Gomes, Universidade do Estado do Rio de Janeiro, Rio de Janeiro, 2010.
url http://www.bdtd.uerj.br/handle/1/16206
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dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Universidade do Estado do Rio de Janeiro
dc.publisher.program.fl_str_mv Programa de Pós-Graduação em Biociências
dc.publisher.initials.fl_str_mv UERJ
dc.publisher.country.fl_str_mv BR
dc.publisher.department.fl_str_mv Centro Biomédico::Instituto de Biologia Roberto Alcantara Gomes
publisher.none.fl_str_mv Universidade do Estado do Rio de Janeiro
dc.source.none.fl_str_mv reponame:Biblioteca Digital de Teses e Dissertações da UERJ
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