Hepatic cytochrome P450 and flavin cointaining monoogygenase metabolic activities in male and female sheep

Autores
Maté, María Laura; Virkel, Guillermo Leon; Lifschitz, Adrian Luis; Ballent, Mariana; Sallovitz, Juan Manuel; Lanusse, Carlos Edmundo
Año de publicación
2009
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
Xenobiotic metabolizing enzymes play a major role in determining the persistence of therapeutically used drugs in target tissues. Phase 1 oxidative reactions are catalyzed by the cytochrome P450 (CYP) superfamily and the flavin-containing monooxygenase (FMO) system, the most important membranebound mixed function oxidases in mammals. The objective of this work was to evaluate CYP- and FMO-dependent activities in liver microsomes obtained from male and female Romney Marsh sheep aged 8-10 months. The involvement of both enzyme systems on the hepatic enantioselective sulphoxidation of the benzimidazole anthelmintic albendazole (ABZ) was also characterized. CYP- and FMO-dependent metabolic activities were measured by using known marker substrates. The total CYP contents in the hepatic microsomes were 0.51±0.18 (males) and 0.53±0.08 (females) nmol/mg of microsomal protein. No gender differences were observed in CYP1A-, CYP2B-, CYP2C-, CYP3A- and FMO-dependent activities. The metabolic ratios FMO/CYP for the total sulphoxidation of ABZ were 3.35 and 3.58 in male and female sheep, respectively. This finding also indicates no gender differences on the contribution of both enzyme systems to the hepatic metabolism of this anthelmintic. Overall, male and female Romney Marsh sheep displayed similar phase 1 metabolic activities in the liver.
Fil: Maté, María Laura. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Departamento de Fisiopatología. Laboratorio de Farmacología; Argentina
Fil: Virkel, Guillermo Leon. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Departamento de Fisiopatología. Laboratorio de Farmacología; Argentina
Fil: Lifschitz, Adrian Luis. 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. Departamento de Fisiopatología. Laboratorio de Farmacología; Argentina
Fil: Ballent, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Departamento de Fisiopatología. Laboratorio de Farmacología; Argentina
Fil: Sallovitz, Juan Manuel. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Departamento de Fisiopatología. Laboratorio de Farmacología; Argentina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas; Argentina
Fil: Lanusse, Carlos Edmundo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Departamento de Fisiopatología. Laboratorio de Farmacología; Argentina
XLI Reunión anual de la Asociación Argentina de Farmacología Experimental
Rosario
Argentina
Asociación Argentina de Farmacología Experimental
Materia
Cytochrome P450
Flavin cointaining monoogygenase
Sheep
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:11336/250208
Acceder
id CONICETDig_1089e1b54773fedef43fbb0bed5304b8
oai_identifier_str oai:ri.conicet.gov.ar:11336/250208
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Hepatic cytochrome P450 and flavin cointaining monoogygenase metabolic activities in male and female sheepMaté, María LauraVirkel, Guillermo LeonLifschitz, Adrian LuisBallent, MarianaSallovitz, Juan ManuelLanusse, Carlos EdmundoCytochrome P450Flavin cointaining monoogygenaseSheephttps://purl.org/becyt/ford/4.3https://purl.org/becyt/ford/4Xenobiotic metabolizing enzymes play a major role in determining the persistence of therapeutically used drugs in target tissues. Phase 1 oxidative reactions are catalyzed by the cytochrome P450 (CYP) superfamily and the flavin-containing monooxygenase (FMO) system, the most important membranebound mixed function oxidases in mammals. The objective of this work was to evaluate CYP- and FMO-dependent activities in liver microsomes obtained from male and female Romney Marsh sheep aged 8-10 months. The involvement of both enzyme systems on the hepatic enantioselective sulphoxidation of the benzimidazole anthelmintic albendazole (ABZ) was also characterized. CYP- and FMO-dependent metabolic activities were measured by using known marker substrates. The total CYP contents in the hepatic microsomes were 0.51±0.18 (males) and 0.53±0.08 (females) nmol/mg of microsomal protein. No gender differences were observed in CYP1A-, CYP2B-, CYP2C-, CYP3A- and FMO-dependent activities. The metabolic ratios FMO/CYP for the total sulphoxidation of ABZ were 3.35 and 3.58 in male and female sheep, respectively. This finding also indicates no gender differences on the contribution of both enzyme systems to the hepatic metabolism of this anthelmintic. Overall, male and female Romney Marsh sheep displayed similar phase 1 metabolic activities in the liver.Fil: Maté, María Laura. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Departamento de Fisiopatología. Laboratorio de Farmacología; ArgentinaFil: Virkel, Guillermo Leon. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Departamento de Fisiopatología. Laboratorio de Farmacología; ArgentinaFil: Lifschitz, Adrian Luis. 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. Departamento de Fisiopatología. Laboratorio de Farmacología; ArgentinaFil: Ballent, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Departamento de Fisiopatología. Laboratorio de Farmacología; ArgentinaFil: Sallovitz, Juan Manuel. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Departamento de Fisiopatología. Laboratorio de Farmacología; Argentina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas; ArgentinaFil: Lanusse, Carlos Edmundo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Departamento de Fisiopatología. Laboratorio de Farmacología; ArgentinaXLI Reunión anual de la Asociación Argentina de Farmacología ExperimentalRosarioArgentinaAsociación Argentina de Farmacología ExperimentalAsociación Argentina de Farmacología Experimental2009info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectReuniónBookhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/mswordapplication/pdfhttp://hdl.handle.net/11336/250208Hepatic cytochrome P450 and flavin cointaining monoogygenase metabolic activities in male and female sheep; XLI Reunión anual de la Asociación Argentina de Farmacología Experimental; Rosario; Argentina; 2009; 51-51CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://aafeargentina.org/congresos-aafe/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:09:35Zoai:ri.conicet.gov.ar:11336/250208instacron: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 13:09:36.027CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Hepatic cytochrome P450 and flavin cointaining monoogygenase metabolic activities in male and female sheep
title Hepatic cytochrome P450 and flavin cointaining monoogygenase metabolic activities in male and female sheep
spellingShingle Hepatic cytochrome P450 and flavin cointaining monoogygenase metabolic activities in male and female sheep
Maté, María Laura
Cytochrome P450
Flavin cointaining monoogygenase
Sheep
title_short Hepatic cytochrome P450 and flavin cointaining monoogygenase metabolic activities in male and female sheep
title_full Hepatic cytochrome P450 and flavin cointaining monoogygenase metabolic activities in male and female sheep
title_fullStr Hepatic cytochrome P450 and flavin cointaining monoogygenase metabolic activities in male and female sheep
title_full_unstemmed Hepatic cytochrome P450 and flavin cointaining monoogygenase metabolic activities in male and female sheep
title_sort Hepatic cytochrome P450 and flavin cointaining monoogygenase metabolic activities in male and female sheep
dc.creator.none.fl_str_mv Maté, María Laura
Virkel, Guillermo Leon
Lifschitz, Adrian Luis
Ballent, Mariana
Sallovitz, Juan Manuel
Lanusse, Carlos Edmundo
author Maté, María Laura
author_facet Maté, María Laura
Virkel, Guillermo Leon
Lifschitz, Adrian Luis
Ballent, Mariana
Sallovitz, Juan Manuel
Lanusse, Carlos Edmundo
author_role author
author2 Virkel, Guillermo Leon
Lifschitz, Adrian Luis
Ballent, Mariana
Sallovitz, Juan Manuel
Lanusse, Carlos Edmundo
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Cytochrome P450
Flavin cointaining monoogygenase
Sheep
topic Cytochrome P450
Flavin cointaining monoogygenase
Sheep
purl_subject.fl_str_mv https://purl.org/becyt/ford/4.3
https://purl.org/becyt/ford/4
dc.description.none.fl_txt_mv Xenobiotic metabolizing enzymes play a major role in determining the persistence of therapeutically used drugs in target tissues. Phase 1 oxidative reactions are catalyzed by the cytochrome P450 (CYP) superfamily and the flavin-containing monooxygenase (FMO) system, the most important membranebound mixed function oxidases in mammals. The objective of this work was to evaluate CYP- and FMO-dependent activities in liver microsomes obtained from male and female Romney Marsh sheep aged 8-10 months. The involvement of both enzyme systems on the hepatic enantioselective sulphoxidation of the benzimidazole anthelmintic albendazole (ABZ) was also characterized. CYP- and FMO-dependent metabolic activities were measured by using known marker substrates. The total CYP contents in the hepatic microsomes were 0.51±0.18 (males) and 0.53±0.08 (females) nmol/mg of microsomal protein. No gender differences were observed in CYP1A-, CYP2B-, CYP2C-, CYP3A- and FMO-dependent activities. The metabolic ratios FMO/CYP for the total sulphoxidation of ABZ were 3.35 and 3.58 in male and female sheep, respectively. This finding also indicates no gender differences on the contribution of both enzyme systems to the hepatic metabolism of this anthelmintic. Overall, male and female Romney Marsh sheep displayed similar phase 1 metabolic activities in the liver.
Fil: Maté, María Laura. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Departamento de Fisiopatología. Laboratorio de Farmacología; Argentina
Fil: Virkel, Guillermo Leon. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Departamento de Fisiopatología. Laboratorio de Farmacología; Argentina
Fil: Lifschitz, Adrian Luis. 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. Departamento de Fisiopatología. Laboratorio de Farmacología; Argentina
Fil: Ballent, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Departamento de Fisiopatología. Laboratorio de Farmacología; Argentina
Fil: Sallovitz, Juan Manuel. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Departamento de Fisiopatología. Laboratorio de Farmacología; Argentina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas; Argentina
Fil: Lanusse, Carlos Edmundo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Departamento de Fisiopatología. Laboratorio de Farmacología; Argentina
XLI Reunión anual de la Asociación Argentina de Farmacología Experimental
Rosario
Argentina
Asociación Argentina de Farmacología Experimental
description Xenobiotic metabolizing enzymes play a major role in determining the persistence of therapeutically used drugs in target tissues. Phase 1 oxidative reactions are catalyzed by the cytochrome P450 (CYP) superfamily and the flavin-containing monooxygenase (FMO) system, the most important membranebound mixed function oxidases in mammals. The objective of this work was to evaluate CYP- and FMO-dependent activities in liver microsomes obtained from male and female Romney Marsh sheep aged 8-10 months. The involvement of both enzyme systems on the hepatic enantioselective sulphoxidation of the benzimidazole anthelmintic albendazole (ABZ) was also characterized. CYP- and FMO-dependent metabolic activities were measured by using known marker substrates. The total CYP contents in the hepatic microsomes were 0.51±0.18 (males) and 0.53±0.08 (females) nmol/mg of microsomal protein. No gender differences were observed in CYP1A-, CYP2B-, CYP2C-, CYP3A- and FMO-dependent activities. The metabolic ratios FMO/CYP for the total sulphoxidation of ABZ were 3.35 and 3.58 in male and female sheep, respectively. This finding also indicates no gender differences on the contribution of both enzyme systems to the hepatic metabolism of this anthelmintic. Overall, male and female Romney Marsh sheep displayed similar phase 1 metabolic activities in the liver.
publishDate 2009
dc.date.none.fl_str_mv 2009
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/conferenceObject
Reunión
Book
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/11336/250208
Hepatic cytochrome P450 and flavin cointaining monoogygenase metabolic activities in male and female sheep; XLI Reunión anual de la Asociación Argentina de Farmacología Experimental; Rosario; Argentina; 2009; 51-51
CONICET Digital
CONICET
url http://hdl.handle.net/11336/250208
identifier_str_mv Hepatic cytochrome P450 and flavin cointaining monoogygenase metabolic activities in male and female sheep; XLI Reunión anual de la Asociación Argentina de Farmacología Experimental; Rosario; Argentina; 2009; 51-51
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://aafeargentina.org/congresos-aafe/
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 Asociación Argentina de Farmacología Experimental
publisher.none.fl_str_mv Asociación Argentina de Farmacología Experimental
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 12.993085

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