Thioredoxin-linked metabolism in Entamoeba histolytica
- Autores
- Arias, Diego Gustavo; Gutierrez, Pablo Cesar; Iglesias, Alberto Alvaro; Guerrero, Sergio Adrian
- Año de publicación
- 2007
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Entamoeba histolytica, an intestinal protozoan that is the causative agent of amoebiasis, is exposed to elevated amounts of highly toxic reactive oxygen species during tissue invasion. In this work, we report the molecular cloning, from E. histolytica genomic DNA, of the genes ehtrxr and ehtrx41, respectively coding for thioredoxin reductase (EhTRXR) and thioredoxin (EhTRX41). The genes were expressed in Escherichia coli cells, and the corresponding recombinant proteins were purified and characterized. EhTRXR catalyzed the NADPH (Km = 4.5 μM)-dependent reduction of 5,5′-dithiobis-(2-nitrobenzoic) acid (Km = 1.7 mM), EhTRX41 (Km = 3.6 μM), and E. coli TRX (Km = 4.6 μM). EhTRXR and EhTRX41 could be assayed as a functional redox pair that, together with peroxiredoxin, mediate the NADPH-dependent reduction of hydrogen peroxide and tert-butyl hydroperoxide. It is proposed that this detoxifying system could be operative in vivo. Results add value to the genome project information and advise reconsideration of key metabolic pathways operating in E. histolytica.
Fil: Arias, Diego Gustavo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina
Fil: Gutierrez, Pablo Cesar. Universidad Nacional del Litoral; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina
Fil: Guerrero, Sergio Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina - Materia
-
ENTAMOEBA HISTOLYTICA
FREE RADICALS
REDOX METABOLISM
STRUCTURAL AND FUNCTIONAL CHARACTERIZATION
THIOREDOXIN SYSTEM - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/84788
Ver los metadatos del registro completo
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spelling |
Thioredoxin-linked metabolism in Entamoeba histolyticaArias, Diego GustavoGutierrez, Pablo CesarIglesias, Alberto AlvaroGuerrero, Sergio AdrianENTAMOEBA HISTOLYTICAFREE RADICALSREDOX METABOLISMSTRUCTURAL AND FUNCTIONAL CHARACTERIZATIONTHIOREDOXIN SYSTEMhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Entamoeba histolytica, an intestinal protozoan that is the causative agent of amoebiasis, is exposed to elevated amounts of highly toxic reactive oxygen species during tissue invasion. In this work, we report the molecular cloning, from E. histolytica genomic DNA, of the genes ehtrxr and ehtrx41, respectively coding for thioredoxin reductase (EhTRXR) and thioredoxin (EhTRX41). The genes were expressed in Escherichia coli cells, and the corresponding recombinant proteins were purified and characterized. EhTRXR catalyzed the NADPH (Km = 4.5 μM)-dependent reduction of 5,5′-dithiobis-(2-nitrobenzoic) acid (Km = 1.7 mM), EhTRX41 (Km = 3.6 μM), and E. coli TRX (Km = 4.6 μM). EhTRXR and EhTRX41 could be assayed as a functional redox pair that, together with peroxiredoxin, mediate the NADPH-dependent reduction of hydrogen peroxide and tert-butyl hydroperoxide. It is proposed that this detoxifying system could be operative in vivo. Results add value to the genome project information and advise reconsideration of key metabolic pathways operating in E. histolytica.Fil: Arias, Diego Gustavo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; ArgentinaFil: Gutierrez, Pablo Cesar. Universidad Nacional del Litoral; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; ArgentinaFil: Guerrero, Sergio Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; ArgentinaElsevier Science Inc2007-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/84788Arias, Diego Gustavo; Gutierrez, Pablo Cesar; Iglesias, Alberto Alvaro; Guerrero, Sergio Adrian; Thioredoxin-linked metabolism in Entamoeba histolytica; Elsevier Science Inc; Free Radical Biology and Medicine; 42; 10; 5-2007; 1496-15050891-5849CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.freeradbiomed.2007.02.012info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0891584907001177info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:37:11Zoai:ri.conicet.gov.ar:11336/84788instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 15:37:11.905CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Thioredoxin-linked metabolism in Entamoeba histolytica |
title |
Thioredoxin-linked metabolism in Entamoeba histolytica |
spellingShingle |
Thioredoxin-linked metabolism in Entamoeba histolytica Arias, Diego Gustavo ENTAMOEBA HISTOLYTICA FREE RADICALS REDOX METABOLISM STRUCTURAL AND FUNCTIONAL CHARACTERIZATION THIOREDOXIN SYSTEM |
title_short |
Thioredoxin-linked metabolism in Entamoeba histolytica |
title_full |
Thioredoxin-linked metabolism in Entamoeba histolytica |
title_fullStr |
Thioredoxin-linked metabolism in Entamoeba histolytica |
title_full_unstemmed |
Thioredoxin-linked metabolism in Entamoeba histolytica |
title_sort |
Thioredoxin-linked metabolism in Entamoeba histolytica |
dc.creator.none.fl_str_mv |
Arias, Diego Gustavo Gutierrez, Pablo Cesar Iglesias, Alberto Alvaro Guerrero, Sergio Adrian |
author |
Arias, Diego Gustavo |
author_facet |
Arias, Diego Gustavo Gutierrez, Pablo Cesar Iglesias, Alberto Alvaro Guerrero, Sergio Adrian |
author_role |
author |
author2 |
Gutierrez, Pablo Cesar Iglesias, Alberto Alvaro Guerrero, Sergio Adrian |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
ENTAMOEBA HISTOLYTICA FREE RADICALS REDOX METABOLISM STRUCTURAL AND FUNCTIONAL CHARACTERIZATION THIOREDOXIN SYSTEM |
topic |
ENTAMOEBA HISTOLYTICA FREE RADICALS REDOX METABOLISM STRUCTURAL AND FUNCTIONAL CHARACTERIZATION THIOREDOXIN SYSTEM |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Entamoeba histolytica, an intestinal protozoan that is the causative agent of amoebiasis, is exposed to elevated amounts of highly toxic reactive oxygen species during tissue invasion. In this work, we report the molecular cloning, from E. histolytica genomic DNA, of the genes ehtrxr and ehtrx41, respectively coding for thioredoxin reductase (EhTRXR) and thioredoxin (EhTRX41). The genes were expressed in Escherichia coli cells, and the corresponding recombinant proteins were purified and characterized. EhTRXR catalyzed the NADPH (Km = 4.5 μM)-dependent reduction of 5,5′-dithiobis-(2-nitrobenzoic) acid (Km = 1.7 mM), EhTRX41 (Km = 3.6 μM), and E. coli TRX (Km = 4.6 μM). EhTRXR and EhTRX41 could be assayed as a functional redox pair that, together with peroxiredoxin, mediate the NADPH-dependent reduction of hydrogen peroxide and tert-butyl hydroperoxide. It is proposed that this detoxifying system could be operative in vivo. Results add value to the genome project information and advise reconsideration of key metabolic pathways operating in E. histolytica. Fil: Arias, Diego Gustavo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina Fil: Gutierrez, Pablo Cesar. Universidad Nacional del Litoral; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina Fil: Guerrero, Sergio Adrian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina |
description |
Entamoeba histolytica, an intestinal protozoan that is the causative agent of amoebiasis, is exposed to elevated amounts of highly toxic reactive oxygen species during tissue invasion. In this work, we report the molecular cloning, from E. histolytica genomic DNA, of the genes ehtrxr and ehtrx41, respectively coding for thioredoxin reductase (EhTRXR) and thioredoxin (EhTRX41). The genes were expressed in Escherichia coli cells, and the corresponding recombinant proteins were purified and characterized. EhTRXR catalyzed the NADPH (Km = 4.5 μM)-dependent reduction of 5,5′-dithiobis-(2-nitrobenzoic) acid (Km = 1.7 mM), EhTRX41 (Km = 3.6 μM), and E. coli TRX (Km = 4.6 μM). EhTRXR and EhTRX41 could be assayed as a functional redox pair that, together with peroxiredoxin, mediate the NADPH-dependent reduction of hydrogen peroxide and tert-butyl hydroperoxide. It is proposed that this detoxifying system could be operative in vivo. Results add value to the genome project information and advise reconsideration of key metabolic pathways operating in E. histolytica. |
publishDate |
2007 |
dc.date.none.fl_str_mv |
2007-05 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/84788 Arias, Diego Gustavo; Gutierrez, Pablo Cesar; Iglesias, Alberto Alvaro; Guerrero, Sergio Adrian; Thioredoxin-linked metabolism in Entamoeba histolytica; Elsevier Science Inc; Free Radical Biology and Medicine; 42; 10; 5-2007; 1496-1505 0891-5849 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/84788 |
identifier_str_mv |
Arias, Diego Gustavo; Gutierrez, Pablo Cesar; Iglesias, Alberto Alvaro; Guerrero, Sergio Adrian; Thioredoxin-linked metabolism in Entamoeba histolytica; Elsevier Science Inc; Free Radical Biology and Medicine; 42; 10; 5-2007; 1496-1505 0891-5849 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.freeradbiomed.2007.02.012 info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0891584907001177 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier Science Inc |
publisher.none.fl_str_mv |
Elsevier Science Inc |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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1846083493617991680 |
score |
13.22299 |