Immunolocalization and enzymatic functional characterization of the thioredoxin system in Entamoeba histolytica

Autores
Arias, Diego Gustavo; Carranza, Pedro Gabriel; Lujan, Hugo Daniel; Iglesias, Alberto Alvaro; Guerrero, Sergio Adrian
Año de publicación
2008
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The components of the redox metabolism in Entamoeba histolytica have been recently revisited by Arias et al. (Free Radic. Biol. Med. 42:1496-1505; 2007), after the identification and characterization of a thioredoxin-linked system. The present work deals with studies performed for a better understanding of the localization and identification of different components of the redox machinery present in the parasite. The gene encoding for amoebic thioredoxin 8 was cloned and the recombinant protein typified as having properties similar to those of thioredoxin 41. The ability of these thioredoxins and the specific reductase to assemble a system utilizing NADPH to metabolize hydroperoxides in association with a peroxiredoxin has been kinetically characterized. The peroxiredoxin behaved as a typical 2 cysteine enzyme, exhibiting a ping-pong mechanism with hyperbolic saturation kinetics for thioredoxin 8 (Km = 3.8 μM), thioredoxin 41 (Km = 3.1 μM), and tert-butyl hydroperoxide (Km about 35 μM). Moreover, the tandem system involving thioredoxin reductase and either thioredoxin proved to be operative for reducing low molecular weight disulfides, including putative physiological substrates as cystine and oxidized trypanothione. Thioredoxin reductase and thioredoxin 41 (by association also the functional redox system) have been immunolocalized underlying the plasma membrane in Entamoeba histolytica cells. These findings suggest an important role for the metabolic pathway involving thioredoxin as a redox interchanger, which could be critical for the maintenance and virulence of the parasite when exposed to highly toxic reactive oxygen species.
Fil: Arias, Diego Gustavo. Universidad Nacional del Litoral; Argentina
Fil: Carranza, Pedro Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina
Fil: Lujan, Hugo Daniel. Universidad Católica de Córdoba. Facultad de Medicina; 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
PEROXIREDOXIN
REDOX BALANCE
THIOLS
THIOREDOXIN
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/84801
Acceder
id CONICETDig_65fdc10127cfa114bf322955051fc223
oai_identifier_str oai:ri.conicet.gov.ar:11336/84801
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Immunolocalization and enzymatic functional characterization of the thioredoxin system in Entamoeba histolyticaArias, Diego GustavoCarranza, Pedro GabrielLujan, Hugo DanielIglesias, Alberto AlvaroGuerrero, Sergio AdrianENTAMOEBA HISTOLYTICAPEROXIREDOXINREDOX BALANCETHIOLSTHIOREDOXINhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The components of the redox metabolism in Entamoeba histolytica have been recently revisited by Arias et al. (Free Radic. Biol. Med. 42:1496-1505; 2007), after the identification and characterization of a thioredoxin-linked system. The present work deals with studies performed for a better understanding of the localization and identification of different components of the redox machinery present in the parasite. The gene encoding for amoebic thioredoxin 8 was cloned and the recombinant protein typified as having properties similar to those of thioredoxin 41. The ability of these thioredoxins and the specific reductase to assemble a system utilizing NADPH to metabolize hydroperoxides in association with a peroxiredoxin has been kinetically characterized. The peroxiredoxin behaved as a typical 2 cysteine enzyme, exhibiting a ping-pong mechanism with hyperbolic saturation kinetics for thioredoxin 8 (Km = 3.8 μM), thioredoxin 41 (Km = 3.1 μM), and tert-butyl hydroperoxide (Km about 35 μM). Moreover, the tandem system involving thioredoxin reductase and either thioredoxin proved to be operative for reducing low molecular weight disulfides, including putative physiological substrates as cystine and oxidized trypanothione. Thioredoxin reductase and thioredoxin 41 (by association also the functional redox system) have been immunolocalized underlying the plasma membrane in Entamoeba histolytica cells. These findings suggest an important role for the metabolic pathway involving thioredoxin as a redox interchanger, which could be critical for the maintenance and virulence of the parasite when exposed to highly toxic reactive oxygen species.Fil: Arias, Diego Gustavo. Universidad Nacional del Litoral; ArgentinaFil: Carranza, Pedro Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; ArgentinaFil: Lujan, Hugo Daniel. Universidad Católica de Córdoba. Facultad de Medicina; 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 Inc2008-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/84801Arias, Diego Gustavo; Carranza, Pedro Gabriel; Lujan, Hugo Daniel; Iglesias, Alberto Alvaro; Guerrero, Sergio Adrian; Immunolocalization and enzymatic functional characterization of the thioredoxin system in Entamoeba histolytica; Elsevier Science Inc; Free Radical Biology and Medicine; 45; 1; 7-2008; 32-390891-5849CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.elsevier.com/wps/find/journaldescription.cws_home/525469/description#descriptioninfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.freeradbiomed.2008.03.008info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:57:17Zoai:ri.conicet.gov.ar:11336/84801instacron: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:34982025-09-03 09:57:17.408CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Immunolocalization and enzymatic functional characterization of the thioredoxin system in Entamoeba histolytica
title Immunolocalization and enzymatic functional characterization of the thioredoxin system in Entamoeba histolytica
spellingShingle Immunolocalization and enzymatic functional characterization of the thioredoxin system in Entamoeba histolytica
Arias, Diego Gustavo
ENTAMOEBA HISTOLYTICA
PEROXIREDOXIN
REDOX BALANCE
THIOLS
THIOREDOXIN
title_short Immunolocalization and enzymatic functional characterization of the thioredoxin system in Entamoeba histolytica
title_full Immunolocalization and enzymatic functional characterization of the thioredoxin system in Entamoeba histolytica
title_fullStr Immunolocalization and enzymatic functional characterization of the thioredoxin system in Entamoeba histolytica
title_full_unstemmed Immunolocalization and enzymatic functional characterization of the thioredoxin system in Entamoeba histolytica
title_sort Immunolocalization and enzymatic functional characterization of the thioredoxin system in Entamoeba histolytica
dc.creator.none.fl_str_mv Arias, Diego Gustavo
Carranza, Pedro Gabriel
Lujan, Hugo Daniel
Iglesias, Alberto Alvaro
Guerrero, Sergio Adrian
author Arias, Diego Gustavo
author_facet Arias, Diego Gustavo
Carranza, Pedro Gabriel
Lujan, Hugo Daniel
Iglesias, Alberto Alvaro
Guerrero, Sergio Adrian
author_role author
author2 Carranza, Pedro Gabriel
Lujan, Hugo Daniel
Iglesias, Alberto Alvaro
Guerrero, Sergio Adrian
author2_role author
author
author
author
dc.subject.none.fl_str_mv ENTAMOEBA HISTOLYTICA
PEROXIREDOXIN
REDOX BALANCE
THIOLS
THIOREDOXIN
topic ENTAMOEBA HISTOLYTICA
PEROXIREDOXIN
REDOX BALANCE
THIOLS
THIOREDOXIN
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The components of the redox metabolism in Entamoeba histolytica have been recently revisited by Arias et al. (Free Radic. Biol. Med. 42:1496-1505; 2007), after the identification and characterization of a thioredoxin-linked system. The present work deals with studies performed for a better understanding of the localization and identification of different components of the redox machinery present in the parasite. The gene encoding for amoebic thioredoxin 8 was cloned and the recombinant protein typified as having properties similar to those of thioredoxin 41. The ability of these thioredoxins and the specific reductase to assemble a system utilizing NADPH to metabolize hydroperoxides in association with a peroxiredoxin has been kinetically characterized. The peroxiredoxin behaved as a typical 2 cysteine enzyme, exhibiting a ping-pong mechanism with hyperbolic saturation kinetics for thioredoxin 8 (Km = 3.8 μM), thioredoxin 41 (Km = 3.1 μM), and tert-butyl hydroperoxide (Km about 35 μM). Moreover, the tandem system involving thioredoxin reductase and either thioredoxin proved to be operative for reducing low molecular weight disulfides, including putative physiological substrates as cystine and oxidized trypanothione. Thioredoxin reductase and thioredoxin 41 (by association also the functional redox system) have been immunolocalized underlying the plasma membrane in Entamoeba histolytica cells. These findings suggest an important role for the metabolic pathway involving thioredoxin as a redox interchanger, which could be critical for the maintenance and virulence of the parasite when exposed to highly toxic reactive oxygen species.
Fil: Arias, Diego Gustavo. Universidad Nacional del Litoral; Argentina
Fil: Carranza, Pedro Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina
Fil: Lujan, Hugo Daniel. Universidad Católica de Córdoba. Facultad de Medicina; 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 The components of the redox metabolism in Entamoeba histolytica have been recently revisited by Arias et al. (Free Radic. Biol. Med. 42:1496-1505; 2007), after the identification and characterization of a thioredoxin-linked system. The present work deals with studies performed for a better understanding of the localization and identification of different components of the redox machinery present in the parasite. The gene encoding for amoebic thioredoxin 8 was cloned and the recombinant protein typified as having properties similar to those of thioredoxin 41. The ability of these thioredoxins and the specific reductase to assemble a system utilizing NADPH to metabolize hydroperoxides in association with a peroxiredoxin has been kinetically characterized. The peroxiredoxin behaved as a typical 2 cysteine enzyme, exhibiting a ping-pong mechanism with hyperbolic saturation kinetics for thioredoxin 8 (Km = 3.8 μM), thioredoxin 41 (Km = 3.1 μM), and tert-butyl hydroperoxide (Km about 35 μM). Moreover, the tandem system involving thioredoxin reductase and either thioredoxin proved to be operative for reducing low molecular weight disulfides, including putative physiological substrates as cystine and oxidized trypanothione. Thioredoxin reductase and thioredoxin 41 (by association also the functional redox system) have been immunolocalized underlying the plasma membrane in Entamoeba histolytica cells. These findings suggest an important role for the metabolic pathway involving thioredoxin as a redox interchanger, which could be critical for the maintenance and virulence of the parasite when exposed to highly toxic reactive oxygen species.
publishDate 2008
dc.date.none.fl_str_mv 2008-07
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/11336/84801
Arias, Diego Gustavo; Carranza, Pedro Gabriel; Lujan, Hugo Daniel; Iglesias, Alberto Alvaro; Guerrero, Sergio Adrian; Immunolocalization and enzymatic functional characterization of the thioredoxin system in Entamoeba histolytica; Elsevier Science Inc; Free Radical Biology and Medicine; 45; 1; 7-2008; 32-39
0891-5849
CONICET Digital
CONICET
url http://hdl.handle.net/11336/84801
identifier_str_mv Arias, Diego Gustavo; Carranza, Pedro Gabriel; Lujan, Hugo Daniel; Iglesias, Alberto Alvaro; Guerrero, Sergio Adrian; Immunolocalization and enzymatic functional characterization of the thioredoxin system in Entamoeba histolytica; Elsevier Science Inc; Free Radical Biology and Medicine; 45; 1; 7-2008; 32-39
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/url/http://www.elsevier.com/wps/find/journaldescription.cws_home/525469/description#description
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.freeradbiomed.2008.03.008
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
application/pdf
application/pdf
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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