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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/79915
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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 Técnicas2025-09-29T09:58:27Zoai: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:34982025-09-29 09:58:28.024CONICET 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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1844613742102315008 |
score |
13.070432 |