Acetilcolinesterase, butirilcolinesterase, carboxilesterase e a resistência de peixes neotropicais aos pesticidas organofosforados
Autor(a) principal: | |
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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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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 |
format |
doctoralThesis |
status_str |
publishedVersion |
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 |
dc.language.iso.fl_str_mv |
por |
language |
por |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
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openAccess |
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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 |
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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 |
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reponame:Biblioteca Digital de Teses e Dissertações da UERJ instname:Universidade do Estado do Rio de Janeiro (UERJ) instacron:UERJ |
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Biblioteca Digital de Teses e Dissertações da UERJ |
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Biblioteca Digital de Teses e Dissertações da UERJ - Universidade do Estado do Rio de Janeiro (UERJ) |
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