Inactivation of Trypanosoma cruzi and Crithidia fasciculata topoisomerase I by Fenton systems

Autores
Podestá, Dolores; Stoppani, Andrés; Fernandez Villamil, Silvia Hebe
Año de publicación
2003
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Fenton systems (H2O2/Fe(II) or H2O2/Cu(II)) inhibited Trypanosoma cruzi and Crithidia fasciculata topoisomerase I activity. About 61-71% inactivation was produced by 25 μM Fe(II) or Cu(II) with 3.0 mM H2O2. Thiol compounds and free radical scavengers prevented Fenton system effects, depending on the topoisomerase assayed. With the T. cruzi enzyme, reduced glutathione (GSH), dithiothreitol (DTT), cysteine and N-acetyl-L-cysteine (NAC) entirely prevented the effect of the H2O2/Fe(II) system; mannitol protected 37%, whereas histidine and ethanol were ineffective. With C. fasciculata topoisomerase, GSH, DTT and NAC protected 100%, cysteine, histidine and mannitol protected 28%, 34% and 48%, respectively, whereas ethanol was ineffective. With the H2O2/Cu(II) system and T. cruzi topoisomerase, DTT and histidine protected 100% and 60%, respectively, but the other assayed protectors were less effective. Similar results were obtained with the C. fasciculata enzyme. Topoisomerase inactivation by the H2O2/Fe(II) or H2O2/Cu(II) systems proved to be irreversible since it was not reversed by the more effective enzyme protectors. It is suggested that topoisomerases could act either as targets of 'reactive oxygen species' (ROS) generated by Fenton systems or bind the corresponding metal ions, whose redox cycling would generate reactive oxygen species in situ.
Fil: Podestá, Dolores. Universidad de Buenos Aires. Facultad de Medicina; Argentina
Fil: Stoppani, Andrés. Universidad de Buenos Aires. Facultad de Medicina; Argentina
Fil: Fernandez Villamil, Silvia Hebe. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Medicina; Argentina
Materia
Trypanosomatids
Ros
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:11336/79915
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Inactivation of Trypanosoma cruzi and Crithidia fasciculata topoisomerase I by Fenton systemsPodestá, DoloresStoppani, AndrésFernandez Villamil, Silvia HebeTrypanosomatidsRoshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Fenton systems (H2O2/Fe(II) or H2O2/Cu(II)) inhibited Trypanosoma cruzi and Crithidia fasciculata topoisomerase I activity. About 61-71% inactivation was produced by 25 μM Fe(II) or Cu(II) with 3.0 mM H2O2. Thiol compounds and free radical scavengers prevented Fenton system effects, depending on the topoisomerase assayed. With the T. cruzi enzyme, reduced glutathione (GSH), dithiothreitol (DTT), cysteine and N-acetyl-L-cysteine (NAC) entirely prevented the effect of the H2O2/Fe(II) system; mannitol protected 37%, whereas histidine and ethanol were ineffective. With C. fasciculata topoisomerase, GSH, DTT and NAC protected 100%, cysteine, histidine and mannitol protected 28%, 34% and 48%, respectively, whereas ethanol was ineffective. With the H2O2/Cu(II) system and T. cruzi topoisomerase, DTT and histidine protected 100% and 60%, respectively, but the other assayed protectors were less effective. Similar results were obtained with the C. fasciculata enzyme. Topoisomerase inactivation by the H2O2/Fe(II) or H2O2/Cu(II) systems proved to be irreversible since it was not reversed by the more effective enzyme protectors. It is suggested that topoisomerases could act either as targets of 'reactive oxygen species' (ROS) generated by Fenton systems or bind the corresponding metal ions, whose redox cycling would generate reactive oxygen species in situ.Fil: Podestá, Dolores. Universidad de Buenos Aires. Facultad de Medicina; ArgentinaFil: Stoppani, Andrés. Universidad de Buenos Aires. Facultad de Medicina; ArgentinaFil: Fernandez Villamil, Silvia Hebe. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Medicina; ArgentinaManey Publishing2003-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/mswordapplication/pdfhttp://hdl.handle.net/11336/79915Podestá, Dolores; Stoppani, Andrés; Fernandez Villamil, Silvia Hebe; Inactivation of Trypanosoma cruzi and Crithidia fasciculata topoisomerase I by Fenton systems; Maney Publishing; Redox Report; 8; 6; 4-2003; 357-3631351-0002CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.tandfonline.com/doi/abs/10.1179/135100003225003366info:eu-repo/semantics/altIdentifier/doi/10.1179/135100003225003366info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:27:47Zoai:ri.conicet.gov.ar:11336/79915instacron: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:34982025-10-22 11:27:47.26CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Inactivation of Trypanosoma cruzi and Crithidia fasciculata topoisomerase I by Fenton systems
title Inactivation of Trypanosoma cruzi and Crithidia fasciculata topoisomerase I by Fenton systems
spellingShingle Inactivation of Trypanosoma cruzi and Crithidia fasciculata topoisomerase I by Fenton systems
Podestá, Dolores
Trypanosomatids
Ros
title_short Inactivation of Trypanosoma cruzi and Crithidia fasciculata topoisomerase I by Fenton systems
title_full Inactivation of Trypanosoma cruzi and Crithidia fasciculata topoisomerase I by Fenton systems
title_fullStr Inactivation of Trypanosoma cruzi and Crithidia fasciculata topoisomerase I by Fenton systems
title_full_unstemmed Inactivation of Trypanosoma cruzi and Crithidia fasciculata topoisomerase I by Fenton systems
title_sort Inactivation of Trypanosoma cruzi and Crithidia fasciculata topoisomerase I by Fenton systems
dc.creator.none.fl_str_mv Podestá, Dolores
Stoppani, Andrés
Fernandez Villamil, Silvia Hebe
author Podestá, Dolores
author_facet Podestá, Dolores
Stoppani, Andrés
Fernandez Villamil, Silvia Hebe
author_role author
author2 Stoppani, Andrés
Fernandez Villamil, Silvia Hebe
author2_role author
author
dc.subject.none.fl_str_mv Trypanosomatids
Ros
topic Trypanosomatids
Ros
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Fenton systems (H2O2/Fe(II) or H2O2/Cu(II)) inhibited Trypanosoma cruzi and Crithidia fasciculata topoisomerase I activity. About 61-71% inactivation was produced by 25 μM Fe(II) or Cu(II) with 3.0 mM H2O2. Thiol compounds and free radical scavengers prevented Fenton system effects, depending on the topoisomerase assayed. With the T. cruzi enzyme, reduced glutathione (GSH), dithiothreitol (DTT), cysteine and N-acetyl-L-cysteine (NAC) entirely prevented the effect of the H2O2/Fe(II) system; mannitol protected 37%, whereas histidine and ethanol were ineffective. With C. fasciculata topoisomerase, GSH, DTT and NAC protected 100%, cysteine, histidine and mannitol protected 28%, 34% and 48%, respectively, whereas ethanol was ineffective. With the H2O2/Cu(II) system and T. cruzi topoisomerase, DTT and histidine protected 100% and 60%, respectively, but the other assayed protectors were less effective. Similar results were obtained with the C. fasciculata enzyme. Topoisomerase inactivation by the H2O2/Fe(II) or H2O2/Cu(II) systems proved to be irreversible since it was not reversed by the more effective enzyme protectors. It is suggested that topoisomerases could act either as targets of 'reactive oxygen species' (ROS) generated by Fenton systems or bind the corresponding metal ions, whose redox cycling would generate reactive oxygen species in situ.
Fil: Podestá, Dolores. Universidad de Buenos Aires. Facultad de Medicina; Argentina
Fil: Stoppani, Andrés. Universidad de Buenos Aires. Facultad de Medicina; Argentina
Fil: Fernandez Villamil, Silvia Hebe. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires. Facultad de Medicina; Argentina
description Fenton systems (H2O2/Fe(II) or H2O2/Cu(II)) inhibited Trypanosoma cruzi and Crithidia fasciculata topoisomerase I activity. About 61-71% inactivation was produced by 25 μM Fe(II) or Cu(II) with 3.0 mM H2O2. Thiol compounds and free radical scavengers prevented Fenton system effects, depending on the topoisomerase assayed. With the T. cruzi enzyme, reduced glutathione (GSH), dithiothreitol (DTT), cysteine and N-acetyl-L-cysteine (NAC) entirely prevented the effect of the H2O2/Fe(II) system; mannitol protected 37%, whereas histidine and ethanol were ineffective. With C. fasciculata topoisomerase, GSH, DTT and NAC protected 100%, cysteine, histidine and mannitol protected 28%, 34% and 48%, respectively, whereas ethanol was ineffective. With the H2O2/Cu(II) system and T. cruzi topoisomerase, DTT and histidine protected 100% and 60%, respectively, but the other assayed protectors were less effective. Similar results were obtained with the C. fasciculata enzyme. Topoisomerase inactivation by the H2O2/Fe(II) or H2O2/Cu(II) systems proved to be irreversible since it was not reversed by the more effective enzyme protectors. It is suggested that topoisomerases could act either as targets of 'reactive oxygen species' (ROS) generated by Fenton systems or bind the corresponding metal ions, whose redox cycling would generate reactive oxygen species in situ.
publishDate 2003
dc.date.none.fl_str_mv 2003-04
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/11336/79915
Podestá, Dolores; Stoppani, Andrés; Fernandez Villamil, Silvia Hebe; Inactivation of Trypanosoma cruzi and Crithidia fasciculata topoisomerase I by Fenton systems; Maney Publishing; Redox Report; 8; 6; 4-2003; 357-363
1351-0002
CONICET Digital
CONICET
url http://hdl.handle.net/11336/79915
identifier_str_mv Podestá, Dolores; Stoppani, Andrés; Fernandez Villamil, Silvia Hebe; Inactivation of Trypanosoma cruzi and Crithidia fasciculata topoisomerase I by Fenton systems; Maney Publishing; Redox Report; 8; 6; 4-2003; 357-363
1351-0002
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.tandfonline.com/doi/abs/10.1179/135100003225003366
info:eu-repo/semantics/altIdentifier/doi/10.1179/135100003225003366
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/msword
application/pdf
dc.publisher.none.fl_str_mv Maney Publishing
publisher.none.fl_str_mv Maney Publishing
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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score 12.982451

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