Differential activities of glutathione s-transferase isoenzymes in strains of fasciola hepatica susceptible and resistant to triclabendazole

Autores
Fernandez, Vanesa; Ortiz Oblitas P.; Solana, María Victoria; Solana, Hugo Daniel
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Fasciolosis, a parasitic zoonosis of intrahepatic location, is caused by the trematode Fasciola hepatica. Its control is mainly based on the use of the anthelminthic Triclabendazole (TCBZ). The indiscriminate use of this drug has favored the development of anthelmintic resistance. The Glutation S-Transferases (GSTs) are multifunctional enzymes involved in the detoxification of xenobiotics and endogenous compounds using conjugation with endogenous glutathione. Recently, it has been shown an active participation of this family of enzymes in the detoxification of TCBZ related to the phenomenon of resistance. In F. hepatica, eight isoenzymes of the GST are present. Since it is well known that different isoenzymes do not necessarily have the same metabolic activity, this study evaluated the cytosolic activity of mu and pi GST isoenzymes in TCBZ resistant (Sligo and Oberon strains) and TCBZ susceptible (Cullompton strains) of F. hepatica. The results obtained in this study confirm that, although both isoenzymes are involved in different processes of detoxification in F. hepatica, only the GSTmu isoenzyme is involved in the manifestation of resistance to TCBZ.
Fil: Fernandez, Vanesa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tandil. Centro de Investigación Veterinaria de Tandil. Universidad Nacional del Centro de la Provincia de Buenos Aires. Centro de Investigación Veterinaria de Tandil. Provincia de Buenos Aires. Gobernación. Comision de Investigaciones Científicas. Centro de Investigación Veterinaria de Tandil; Argentina
Fil: Ortiz Oblitas P.. Universidad Nacional de Cajamarca; Perú
Fil: Solana, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tandil. Centro de Investigación Veterinaria de Tandil. Universidad Nacional del Centro de la Provincia de Buenos Aires. Centro de Investigación Veterinaria de Tandil. Provincia de Buenos Aires. Gobernación. Comision de Investigaciones Científicas. Centro de Investigación Veterinaria de Tandil; Argentina. Ministerio de Ciencia. Tecnología e Innovación Productiva. Agencia Nacional de Promoción Cientifíca y Tecnológica; Argentina
Fil: Solana, Hugo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tandil. Centro de Investigación Veterinaria de Tandil. Universidad Nacional del Centro de la Provincia de Buenos Aires. Centro de Investigación Veterinaria de Tandil. Provincia de Buenos Aires. Gobernación. Comision de Investigaciones Científicas. Centro de Investigación Veterinaria de Tandil; Argentina
Materia
GLUTATHIONE S-TRANSFERASE
ISOENZYMES
FASCIOLA
RESISTANCE
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:11336/37121
Acceder
id CONICETDig_e46a4e8961c6388c0b8b9f30cfa9f708
oai_identifier_str oai:ri.conicet.gov.ar:11336/37121
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Differential activities of glutathione s-transferase isoenzymes in strains of fasciola hepatica susceptible and resistant to triclabendazoleFernandez, VanesaOrtiz Oblitas P.Solana, María VictoriaSolana, Hugo DanielGLUTATHIONE S-TRANSFERASEISOENZYMESFASCIOLARESISTANCEhttps://purl.org/becyt/ford/4.3https://purl.org/becyt/ford/4Fasciolosis, a parasitic zoonosis of intrahepatic location, is caused by the trematode Fasciola hepatica. Its control is mainly based on the use of the anthelminthic Triclabendazole (TCBZ). The indiscriminate use of this drug has favored the development of anthelmintic resistance. The Glutation S-Transferases (GSTs) are multifunctional enzymes involved in the detoxification of xenobiotics and endogenous compounds using conjugation with endogenous glutathione. Recently, it has been shown an active participation of this family of enzymes in the detoxification of TCBZ related to the phenomenon of resistance. In F. hepatica, eight isoenzymes of the GST are present. Since it is well known that different isoenzymes do not necessarily have the same metabolic activity, this study evaluated the cytosolic activity of mu and pi GST isoenzymes in TCBZ resistant (Sligo and Oberon strains) and TCBZ susceptible (Cullompton strains) of F. hepatica. The results obtained in this study confirm that, although both isoenzymes are involved in different processes of detoxification in F. hepatica, only the GSTmu isoenzyme is involved in the manifestation of resistance to TCBZ.Fil: Fernandez, Vanesa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tandil. Centro de Investigación Veterinaria de Tandil. Universidad Nacional del Centro de la Provincia de Buenos Aires. Centro de Investigación Veterinaria de Tandil. Provincia de Buenos Aires. Gobernación. Comision de Investigaciones Científicas. Centro de Investigación Veterinaria de Tandil; ArgentinaFil: Ortiz Oblitas P.. Universidad Nacional de Cajamarca; PerúFil: Solana, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tandil. Centro de Investigación Veterinaria de Tandil. Universidad Nacional del Centro de la Provincia de Buenos Aires. Centro de Investigación Veterinaria de Tandil. Provincia de Buenos Aires. Gobernación. Comision de Investigaciones Científicas. Centro de Investigación Veterinaria de Tandil; Argentina. Ministerio de Ciencia. Tecnología e Innovación Productiva. Agencia Nacional de Promoción Cientifíca y Tecnológica; ArgentinaFil: Solana, Hugo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tandil. Centro de Investigación Veterinaria de Tandil. Universidad Nacional del Centro de la Provincia de Buenos Aires. Centro de Investigación Veterinaria de Tandil. Provincia de Buenos Aires. Gobernación. Comision de Investigaciones Científicas. Centro de Investigación Veterinaria de Tandil; ArgentinaScience Publications2014-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/37121Fernandez, Vanesa; Ortiz Oblitas P.; Solana, María Victoria; Solana, Hugo Daniel; Differential activities of glutathione s-transferase isoenzymes in strains of fasciola hepatica susceptible and resistant to triclabendazole; Science Publications; American Journal of Animal and Veterinary Sciences; 9; 4; 4-2014; 177-1811557-4555CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.3844/ajavsp.2014.177.181info:eu-repo/semantics/altIdentifier/url/http://thescipub.com/abstract/10.3844/ajavsp.2014.177.181info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:41:05Zoai:ri.conicet.gov.ar:11336/37121instacron: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 09:41:05.967CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Differential activities of glutathione s-transferase isoenzymes in strains of fasciola hepatica susceptible and resistant to triclabendazole
title Differential activities of glutathione s-transferase isoenzymes in strains of fasciola hepatica susceptible and resistant to triclabendazole
spellingShingle Differential activities of glutathione s-transferase isoenzymes in strains of fasciola hepatica susceptible and resistant to triclabendazole
Fernandez, Vanesa
GLUTATHIONE S-TRANSFERASE
ISOENZYMES
FASCIOLA
RESISTANCE
title_short Differential activities of glutathione s-transferase isoenzymes in strains of fasciola hepatica susceptible and resistant to triclabendazole
title_full Differential activities of glutathione s-transferase isoenzymes in strains of fasciola hepatica susceptible and resistant to triclabendazole
title_fullStr Differential activities of glutathione s-transferase isoenzymes in strains of fasciola hepatica susceptible and resistant to triclabendazole
title_full_unstemmed Differential activities of glutathione s-transferase isoenzymes in strains of fasciola hepatica susceptible and resistant to triclabendazole
title_sort Differential activities of glutathione s-transferase isoenzymes in strains of fasciola hepatica susceptible and resistant to triclabendazole
dc.creator.none.fl_str_mv Fernandez, Vanesa
Ortiz Oblitas P.
Solana, María Victoria
Solana, Hugo Daniel
author Fernandez, Vanesa
author_facet Fernandez, Vanesa
Ortiz Oblitas P.
Solana, María Victoria
Solana, Hugo Daniel
author_role author
author2 Ortiz Oblitas P.
Solana, María Victoria
Solana, Hugo Daniel
author2_role author
author
author
dc.subject.none.fl_str_mv GLUTATHIONE S-TRANSFERASE
ISOENZYMES
FASCIOLA
RESISTANCE
topic GLUTATHIONE S-TRANSFERASE
ISOENZYMES
FASCIOLA
RESISTANCE
purl_subject.fl_str_mv https://purl.org/becyt/ford/4.3
https://purl.org/becyt/ford/4
dc.description.none.fl_txt_mv Fasciolosis, a parasitic zoonosis of intrahepatic location, is caused by the trematode Fasciola hepatica. Its control is mainly based on the use of the anthelminthic Triclabendazole (TCBZ). The indiscriminate use of this drug has favored the development of anthelmintic resistance. The Glutation S-Transferases (GSTs) are multifunctional enzymes involved in the detoxification of xenobiotics and endogenous compounds using conjugation with endogenous glutathione. Recently, it has been shown an active participation of this family of enzymes in the detoxification of TCBZ related to the phenomenon of resistance. In F. hepatica, eight isoenzymes of the GST are present. Since it is well known that different isoenzymes do not necessarily have the same metabolic activity, this study evaluated the cytosolic activity of mu and pi GST isoenzymes in TCBZ resistant (Sligo and Oberon strains) and TCBZ susceptible (Cullompton strains) of F. hepatica. The results obtained in this study confirm that, although both isoenzymes are involved in different processes of detoxification in F. hepatica, only the GSTmu isoenzyme is involved in the manifestation of resistance to TCBZ.
Fil: Fernandez, Vanesa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tandil. Centro de Investigación Veterinaria de Tandil. Universidad Nacional del Centro de la Provincia de Buenos Aires. Centro de Investigación Veterinaria de Tandil. Provincia de Buenos Aires. Gobernación. Comision de Investigaciones Científicas. Centro de Investigación Veterinaria de Tandil; Argentina
Fil: Ortiz Oblitas P.. Universidad Nacional de Cajamarca; Perú
Fil: Solana, María Victoria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tandil. Centro de Investigación Veterinaria de Tandil. Universidad Nacional del Centro de la Provincia de Buenos Aires. Centro de Investigación Veterinaria de Tandil. Provincia de Buenos Aires. Gobernación. Comision de Investigaciones Científicas. Centro de Investigación Veterinaria de Tandil; Argentina. Ministerio de Ciencia. Tecnología e Innovación Productiva. Agencia Nacional de Promoción Cientifíca y Tecnológica; Argentina
Fil: Solana, Hugo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tandil. Centro de Investigación Veterinaria de Tandil. Universidad Nacional del Centro de la Provincia de Buenos Aires. Centro de Investigación Veterinaria de Tandil. Provincia de Buenos Aires. Gobernación. Comision de Investigaciones Científicas. Centro de Investigación Veterinaria de Tandil; Argentina
description Fasciolosis, a parasitic zoonosis of intrahepatic location, is caused by the trematode Fasciola hepatica. Its control is mainly based on the use of the anthelminthic Triclabendazole (TCBZ). The indiscriminate use of this drug has favored the development of anthelmintic resistance. The Glutation S-Transferases (GSTs) are multifunctional enzymes involved in the detoxification of xenobiotics and endogenous compounds using conjugation with endogenous glutathione. Recently, it has been shown an active participation of this family of enzymes in the detoxification of TCBZ related to the phenomenon of resistance. In F. hepatica, eight isoenzymes of the GST are present. Since it is well known that different isoenzymes do not necessarily have the same metabolic activity, this study evaluated the cytosolic activity of mu and pi GST isoenzymes in TCBZ resistant (Sligo and Oberon strains) and TCBZ susceptible (Cullompton strains) of F. hepatica. The results obtained in this study confirm that, although both isoenzymes are involved in different processes of detoxification in F. hepatica, only the GSTmu isoenzyme is involved in the manifestation of resistance to TCBZ.
publishDate 2014
dc.date.none.fl_str_mv 2014-04
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/11336/37121
Fernandez, Vanesa; Ortiz Oblitas P.; Solana, María Victoria; Solana, Hugo Daniel; Differential activities of glutathione s-transferase isoenzymes in strains of fasciola hepatica susceptible and resistant to triclabendazole; Science Publications; American Journal of Animal and Veterinary Sciences; 9; 4; 4-2014; 177-181
1557-4555
CONICET Digital
CONICET
url http://hdl.handle.net/11336/37121
identifier_str_mv Fernandez, Vanesa; Ortiz Oblitas P.; Solana, María Victoria; Solana, Hugo Daniel; Differential activities of glutathione s-transferase isoenzymes in strains of fasciola hepatica susceptible and resistant to triclabendazole; Science Publications; American Journal of Animal and Veterinary Sciences; 9; 4; 4-2014; 177-181
1557-4555
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.3844/ajavsp.2014.177.181
info:eu-repo/semantics/altIdentifier/url/http://thescipub.com/abstract/10.3844/ajavsp.2014.177.181
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
dc.publisher.none.fl_str_mv Science Publications
publisher.none.fl_str_mv Science Publications
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
_version_ 1844613299417645056
score 13.069144

Publicaciones similares