A multienzyme response is involved in the phenomenon of resistance to triclabendazole on Fasciola

Autores
Fernandez, Vanesa; Acevedo, Maria E.; Solana, Hugo Daniel
Año de publicación
2015
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
The trematode Fasciola hepatica is the producer of a parasitic zoonosis known as fasciolosis. Triclabendazole (TCBZ) is the most widely used fasciolicide anthelmintic. Today, its indiscriminate use has led to the expression of anthelmintic resistance. Our previous studies over the Sligo strain (TCBZ-R) confirmed in the Phase I of detoxification, an overexpression of Flavin-Monooxygenases. This phenomenon should not be the only response that the trematode has and should not rule out the involvement of other processes of detoxification of Phase I or II. In the processes of detoxification in Phase I, the Carboxylesterase (CE) is a serine esterase-dependent with broad substrate specificity. This family of enzymes are involved in many metabolic functions including detoxification of xenobiotics. In Phase II exists a system using the Glutathione (GSH). It is a sequence of certain enzymes that culminate adding reduced GSH to xenobiotic increasing its water solubility and facilitatingtheir excretion. Glutathione addition plays an important role in antioxidant defense in different tissues catalyze the reduction of oxidized to reduced GSH which will be utilized by GST to reduce the peroxide and lipoperoxide, which they are reactive oxygen species. This process involves Glutathione Peroxidase (GPx), Glutathione Reductase (GSR) and Glutathione S-Transferase (GST). In the present work, we evaluate, in vitro, the cytosolic activity of different xenobiotic metabolizing enzymes of Phase I: CE and Phase II: GST, GPx and GSR in adults of F. hepatica TCBZ susceptible (TCBZ-S) and TCBZ resistant (TCBZ-R),respectively Cullompton strain and Sligo and Oberon strains. In the TCBZ-R Sligo and Oberon strains, the GST activity was 1277±32 and 1216±16 nmol/min/mg protein, respectively, higher than that in the TCBZ-S Cullompton strain 800±60 nmol/ min/mg protein. Regarding the GPx activity in the Sligo and Oberon strains, TCBZ-R was 83±3.41 and 81±2.45 nmol/min/ mg protein, respectively, higher than that in the TCBZ-S Cullompton strain 49±2.58 nmol/min/mg protein. The GSR activity in Sligo and Oberon strains was 38±2.07 and 41±1.25 nmol/min/mg protein, respectively, higher than that in the TCBZ-S Cullompton strain 29±1.22 nmol/min/mg protein, whereas CE activity did not differ between the different strains tested. In this work, a multienzyme response involving at all the family of enzymes GSH dependent is detected. Carboxylesterase expressed no significant differences not being involved in the resistance phenomenon. These results contribute to the understanding of the mechanisms referred to the phenomenon 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: Acevedo, Maria E.. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Laboratorio de Biología Celular y Molecular; 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. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Laboratorio de Biología Celular y Molecular; Argentina
International Conference on Parasitology
Philadelphia
Estados Unidos
OMICS Publishing Group
Materia
MULTIENZYMATIC RESPONSE
FASCIOLA
TCBZ
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:11336/196881
Acceder
id CONICETDig_6fc9eec41caef82df252e8d31511629c
oai_identifier_str oai:ri.conicet.gov.ar:11336/196881
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A multienzyme response is involved in the phenomenon of resistance to triclabendazole on FasciolaFernandez, VanesaAcevedo, Maria E.Solana, Hugo DanielMULTIENZYMATIC RESPONSEFASCIOLATCBZhttps://purl.org/becyt/ford/4.3https://purl.org/becyt/ford/4The trematode Fasciola hepatica is the producer of a parasitic zoonosis known as fasciolosis. Triclabendazole (TCBZ) is the most widely used fasciolicide anthelmintic. Today, its indiscriminate use has led to the expression of anthelmintic resistance. Our previous studies over the Sligo strain (TCBZ-R) confirmed in the Phase I of detoxification, an overexpression of Flavin-Monooxygenases. This phenomenon should not be the only response that the trematode has and should not rule out the involvement of other processes of detoxification of Phase I or II. In the processes of detoxification in Phase I, the Carboxylesterase (CE) is a serine esterase-dependent with broad substrate specificity. This family of enzymes are involved in many metabolic functions including detoxification of xenobiotics. In Phase II exists a system using the Glutathione (GSH). It is a sequence of certain enzymes that culminate adding reduced GSH to xenobiotic increasing its water solubility and facilitatingtheir excretion. Glutathione addition plays an important role in antioxidant defense in different tissues catalyze the reduction of oxidized to reduced GSH which will be utilized by GST to reduce the peroxide and lipoperoxide, which they are reactive oxygen species. This process involves Glutathione Peroxidase (GPx), Glutathione Reductase (GSR) and Glutathione S-Transferase (GST). In the present work, we evaluate, in vitro, the cytosolic activity of different xenobiotic metabolizing enzymes of Phase I: CE and Phase II: GST, GPx and GSR in adults of F. hepatica TCBZ susceptible (TCBZ-S) and TCBZ resistant (TCBZ-R),respectively Cullompton strain and Sligo and Oberon strains. In the TCBZ-R Sligo and Oberon strains, the GST activity was 1277±32 and 1216±16 nmol/min/mg protein, respectively, higher than that in the TCBZ-S Cullompton strain 800±60 nmol/ min/mg protein. Regarding the GPx activity in the Sligo and Oberon strains, TCBZ-R was 83±3.41 and 81±2.45 nmol/min/ mg protein, respectively, higher than that in the TCBZ-S Cullompton strain 49±2.58 nmol/min/mg protein. The GSR activity in Sligo and Oberon strains was 38±2.07 and 41±1.25 nmol/min/mg protein, respectively, higher than that in the TCBZ-S Cullompton strain 29±1.22 nmol/min/mg protein, whereas CE activity did not differ between the different strains tested. In this work, a multienzyme response involving at all the family of enzymes GSH dependent is detected. Carboxylesterase expressed no significant differences not being involved in the resistance phenomenon. These results contribute to the understanding of the mechanisms referred to the phenomenon 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: Acevedo, Maria E.. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Laboratorio de Biología Celular y Molecular; 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; Argentina. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Laboratorio de Biología Celular y Molecular; ArgentinaInternational Conference on ParasitologyPhiladelphiaEstados UnidosOMICS Publishing GroupWalsh Medical Media2015info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectConferenciaJournalhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/196881A multienzyme response is involved in the phenomenon of resistance to triclabendazole on Fasciola; International Conference on Parasitology; Philadelphia; Estados Unidos; 2015; 121-1212155-9597CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.walshmedicalmedia.com/conference-abstracts/parasitology-2015-proceedings-60.htmlinfo:eu-repo/semantics/altIdentifier/url/https://www.walshmedicalmedia.com/conference-abstracts-files/2155-9597.S1.014_021.pdfInternacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:04:09Zoai:ri.conicet.gov.ar:11336/196881instacron: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:34982025-09-10 13:04:10.057CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A multienzyme response is involved in the phenomenon of resistance to triclabendazole on Fasciola
title A multienzyme response is involved in the phenomenon of resistance to triclabendazole on Fasciola
spellingShingle A multienzyme response is involved in the phenomenon of resistance to triclabendazole on Fasciola
Fernandez, Vanesa
MULTIENZYMATIC RESPONSE
FASCIOLA
TCBZ
title_short A multienzyme response is involved in the phenomenon of resistance to triclabendazole on Fasciola
title_full A multienzyme response is involved in the phenomenon of resistance to triclabendazole on Fasciola
title_fullStr A multienzyme response is involved in the phenomenon of resistance to triclabendazole on Fasciola
title_full_unstemmed A multienzyme response is involved in the phenomenon of resistance to triclabendazole on Fasciola
title_sort A multienzyme response is involved in the phenomenon of resistance to triclabendazole on Fasciola
dc.creator.none.fl_str_mv Fernandez, Vanesa
Acevedo, Maria E.
Solana, Hugo Daniel
author Fernandez, Vanesa
author_facet Fernandez, Vanesa
Acevedo, Maria E.
Solana, Hugo Daniel
author_role author
author2 Acevedo, Maria E.
Solana, Hugo Daniel
author2_role author
author
dc.subject.none.fl_str_mv MULTIENZYMATIC RESPONSE
FASCIOLA
TCBZ
topic MULTIENZYMATIC RESPONSE
FASCIOLA
TCBZ
purl_subject.fl_str_mv https://purl.org/becyt/ford/4.3
https://purl.org/becyt/ford/4
dc.description.none.fl_txt_mv The trematode Fasciola hepatica is the producer of a parasitic zoonosis known as fasciolosis. Triclabendazole (TCBZ) is the most widely used fasciolicide anthelmintic. Today, its indiscriminate use has led to the expression of anthelmintic resistance. Our previous studies over the Sligo strain (TCBZ-R) confirmed in the Phase I of detoxification, an overexpression of Flavin-Monooxygenases. This phenomenon should not be the only response that the trematode has and should not rule out the involvement of other processes of detoxification of Phase I or II. In the processes of detoxification in Phase I, the Carboxylesterase (CE) is a serine esterase-dependent with broad substrate specificity. This family of enzymes are involved in many metabolic functions including detoxification of xenobiotics. In Phase II exists a system using the Glutathione (GSH). It is a sequence of certain enzymes that culminate adding reduced GSH to xenobiotic increasing its water solubility and facilitatingtheir excretion. Glutathione addition plays an important role in antioxidant defense in different tissues catalyze the reduction of oxidized to reduced GSH which will be utilized by GST to reduce the peroxide and lipoperoxide, which they are reactive oxygen species. This process involves Glutathione Peroxidase (GPx), Glutathione Reductase (GSR) and Glutathione S-Transferase (GST). In the present work, we evaluate, in vitro, the cytosolic activity of different xenobiotic metabolizing enzymes of Phase I: CE and Phase II: GST, GPx and GSR in adults of F. hepatica TCBZ susceptible (TCBZ-S) and TCBZ resistant (TCBZ-R),respectively Cullompton strain and Sligo and Oberon strains. In the TCBZ-R Sligo and Oberon strains, the GST activity was 1277±32 and 1216±16 nmol/min/mg protein, respectively, higher than that in the TCBZ-S Cullompton strain 800±60 nmol/ min/mg protein. Regarding the GPx activity in the Sligo and Oberon strains, TCBZ-R was 83±3.41 and 81±2.45 nmol/min/ mg protein, respectively, higher than that in the TCBZ-S Cullompton strain 49±2.58 nmol/min/mg protein. The GSR activity in Sligo and Oberon strains was 38±2.07 and 41±1.25 nmol/min/mg protein, respectively, higher than that in the TCBZ-S Cullompton strain 29±1.22 nmol/min/mg protein, whereas CE activity did not differ between the different strains tested. In this work, a multienzyme response involving at all the family of enzymes GSH dependent is detected. Carboxylesterase expressed no significant differences not being involved in the resistance phenomenon. These results contribute to the understanding of the mechanisms referred to the phenomenon 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: Acevedo, Maria E.. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Laboratorio de Biología Celular y Molecular; 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. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Laboratorio de Biología Celular y Molecular; Argentina
International Conference on Parasitology
Philadelphia
Estados Unidos
OMICS Publishing Group
description The trematode Fasciola hepatica is the producer of a parasitic zoonosis known as fasciolosis. Triclabendazole (TCBZ) is the most widely used fasciolicide anthelmintic. Today, its indiscriminate use has led to the expression of anthelmintic resistance. Our previous studies over the Sligo strain (TCBZ-R) confirmed in the Phase I of detoxification, an overexpression of Flavin-Monooxygenases. This phenomenon should not be the only response that the trematode has and should not rule out the involvement of other processes of detoxification of Phase I or II. In the processes of detoxification in Phase I, the Carboxylesterase (CE) is a serine esterase-dependent with broad substrate specificity. This family of enzymes are involved in many metabolic functions including detoxification of xenobiotics. In Phase II exists a system using the Glutathione (GSH). It is a sequence of certain enzymes that culminate adding reduced GSH to xenobiotic increasing its water solubility and facilitatingtheir excretion. Glutathione addition plays an important role in antioxidant defense in different tissues catalyze the reduction of oxidized to reduced GSH which will be utilized by GST to reduce the peroxide and lipoperoxide, which they are reactive oxygen species. This process involves Glutathione Peroxidase (GPx), Glutathione Reductase (GSR) and Glutathione S-Transferase (GST). In the present work, we evaluate, in vitro, the cytosolic activity of different xenobiotic metabolizing enzymes of Phase I: CE and Phase II: GST, GPx and GSR in adults of F. hepatica TCBZ susceptible (TCBZ-S) and TCBZ resistant (TCBZ-R),respectively Cullompton strain and Sligo and Oberon strains. In the TCBZ-R Sligo and Oberon strains, the GST activity was 1277±32 and 1216±16 nmol/min/mg protein, respectively, higher than that in the TCBZ-S Cullompton strain 800±60 nmol/ min/mg protein. Regarding the GPx activity in the Sligo and Oberon strains, TCBZ-R was 83±3.41 and 81±2.45 nmol/min/ mg protein, respectively, higher than that in the TCBZ-S Cullompton strain 49±2.58 nmol/min/mg protein. The GSR activity in Sligo and Oberon strains was 38±2.07 and 41±1.25 nmol/min/mg protein, respectively, higher than that in the TCBZ-S Cullompton strain 29±1.22 nmol/min/mg protein, whereas CE activity did not differ between the different strains tested. In this work, a multienzyme response involving at all the family of enzymes GSH dependent is detected. Carboxylesterase expressed no significant differences not being involved in the resistance phenomenon. These results contribute to the understanding of the mechanisms referred to the phenomenon of resistance to TCBZ.
publishDate 2015
dc.date.none.fl_str_mv 2015
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/conferenceObject
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Journal
http://purl.org/coar/resource_type/c_5794
info:ar-repo/semantics/documentoDeConferencia
status_str publishedVersion
format conferenceObject
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/196881
A multienzyme response is involved in the phenomenon of resistance to triclabendazole on Fasciola; International Conference on Parasitology; Philadelphia; Estados Unidos; 2015; 121-121
2155-9597
CONICET Digital
CONICET
url http://hdl.handle.net/11336/196881
identifier_str_mv A multienzyme response is involved in the phenomenon of resistance to triclabendazole on Fasciola; International Conference on Parasitology; Philadelphia; Estados Unidos; 2015; 121-121
2155-9597
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
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dc.coverage.none.fl_str_mv Internacional
dc.publisher.none.fl_str_mv Walsh Medical Media
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