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dc.contributor.author
Scarcella, Silvana Andrea  
dc.contributor.author
Solana, M. V.  
dc.contributor.author
Fernandez, Vanesa  
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Lamenza, Pamela  
dc.contributor.author
Ceballos, Laura  
dc.contributor.author
Solana, Hugo Daniel  
dc.date.available
2016-03-08T18:49:19Z  
dc.date.issued
2013-11  
dc.identifier.citation
Scarcella, Silvana Andrea; Solana, M. V.; Fernandez, Vanesa; Lamenza, Pamela; Ceballos, Laura; et al.; Increase of gluthatione S-transferase, carboxyl esterase and carbonyl reductase in Fasciola hepatica recovered from triclabendazole treated sheep; Elsevier Science; Molecular and Biochemical Parasitology; 191; 2; 11-2013; 63-65  
dc.identifier.issn
0166-6851  
dc.identifier.uri
http://hdl.handle.net/11336/4686  
dc.description.abstract
Fasciolasis is a zoonotic parasitic disease caused by Fasciola hepatica and its control is mainly based on the use of triclabendazole (TCBZ). Parasite resistance to different anthelmintics is growing worldwide, including the resistance of F. hepatica to TCBZ. In the present work we evaluate “in vivo” the activity of xenobiotic metabolizing enzymes of phase I (carboxyl esterases) and phase II (glutathione S-transferases and carbonyl reductases) recovered of flukes from sheep treated with TCBZ. All three enzymes showed increased activity in TCBZ flukes returning 60 h post-treatment at similar to baseline unexposed flukes. TCBZ action may induce secondary oxidative stress, which may explain the observed increment in activities of the analyzed enzymes as a defensive mechanism. The enzymes analyzed are candidates to participate actively in the development of resistance at TCBZ in F. hepatica.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Elsevier Science  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/  
dc.subject
Fasciola Hepatica  
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Triclabendazole  
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Anthelmintics Resistance  
dc.subject.classification
Ciencias Veterinarias  
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Ciencias Veterinarias  
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CIENCIAS AGRÍCOLAS  
dc.title
Increase of gluthatione S-transferase, carboxyl esterase and carbonyl reductase in Fasciola hepatica recovered from triclabendazole treated sheep  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2016-03-30 10:35:44.97925-03  
dc.journal.volume
191  
dc.journal.number
2  
dc.journal.pagination
63-65  
dc.journal.pais
Países Bajos  
dc.journal.ciudad
Amsterdam  
dc.description.fil
Fil: Scarcella, Silvana Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Tandil. Centro de Investigacion Veterinaria de Tandil; Argentina  
dc.description.fil
Fil: Solana, M. V.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Tandil. Centro de Investigacion Veterinaria de Tandil; Argentina  
dc.description.fil
Fil: Fernandez, Vanesa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Tandil. Centro de Investigacion Veterinaria de Tandil; Argentina  
dc.description.fil
Fil: Lamenza, Pamela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Tandil. Centro de Investigacion Veterinaria de Tandil; Argentina  
dc.description.fil
Fil: Ceballos, Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Tandil. Centro de Investigacion Veterinaria de Tandil; Argentina  
dc.description.fil
Fil: Solana, Hugo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Tandil. Centro de Investigacion Veterinaria de Tandil; Argentina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas; Argentina  
dc.journal.title
Molecular and Biochemical Parasitology  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0166685113001333  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.molbiopara.2013.09.002  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/issn/0166-6851