Characterization of xenobiotic metabolizing enzymes in bovine small intestinal mucosa

Autores
Virkel, Guillermo Leon; Carletti, M.; Cantiello, M.; Della Donna, L.; Gardini, G.; Girolami, F.; Nebbia, C.
Año de publicación
2010
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The intestinal mucosa plays a capital role in dictating the bioavailability of a large array of orally ingested drugs and toxicants. The activity and the expression of several xenobiotic metabolizing enzymes were measured in subcellular fractions from the duodenal mucosa of male veal calves and beef cattle displaying a functional rumen but differing in both age (about 8 months vs. 18 to 24 months) and dietary regimens (i.e., milk replacer plus hay and straw vs. corn and concentrated meal). Intestinal microsomes showed cytochrome P450 (CYP) 2B, 2C- and 3A-mediated activities and the presence of the corresponding immunorelated proteins, but no proof of CYP1A expression and/or functions could be provided. Intestinal microsomes were also active in performing reactions typically mediated by carboxylesterases (indophenylacetate hydrolysis), flavin-containing monooxygenases (methimazole S-oxidation), and uridindiphosphoglucuronyltransferases (1-naphthol glucuronidation), respectively. Cytosolic fractions displayed the glutathione S-transferase (GST)-dependent conjugation of 1-chloro-2,4-dinitrobenzene; besides, the GST-mediated conjugation of ethacrinic acid (GSTφ) or cumene hydroperoxide (GSTα) was matched by the presence of the corresponding immunorelated proteins. Conversely, despite the lack of measurable activity with 3,4-dichloronitrobenzene, a protein cross reacting with anti-rat GSTμ antibodies could be clearly detected. Although, as detected by densitometry, CYPs and GST isoenzymes tended to be more expressed in beef cattle than in veal calf preparations, there was a general poor correlation with the rate of the in vitro metabolism of the selected diagnostic probes.
Fil: Virkel, Guillermo Leon. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Departamento de Fisiopatología. Laboratorio de Farmacología; Argentina. 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: Carletti, M.. Universita degli Studi di Torino; Italia
Fil: Cantiello, M.. Universita degli Studi di Torino; Italia
Fil: Della Donna, L.. Universita degli Studi di Torino; Italia
Fil: Gardini, G.. Universita degli Studi di Torino; Italia
Fil: Girolami, F.. Universita degli Studi di Torino; Italia
Fil: Nebbia, C.. Universita degli Studi di Torino; Italia
Materia
Xenobiotic Metabolizing Enzymes
Intestinal Mucosa
Microsomes
Cattle
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:11336/83897
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/83897
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Characterization of xenobiotic metabolizing enzymes in bovine small intestinal mucosaVirkel, Guillermo LeonCarletti, M.Cantiello, M.Della Donna, L.Gardini, G.Girolami, F.Nebbia, C.Xenobiotic Metabolizing EnzymesIntestinal MucosaMicrosomesCattlehttps://purl.org/becyt/ford/4.3https://purl.org/becyt/ford/4The intestinal mucosa plays a capital role in dictating the bioavailability of a large array of orally ingested drugs and toxicants. The activity and the expression of several xenobiotic metabolizing enzymes were measured in subcellular fractions from the duodenal mucosa of male veal calves and beef cattle displaying a functional rumen but differing in both age (about 8 months vs. 18 to 24 months) and dietary regimens (i.e., milk replacer plus hay and straw vs. corn and concentrated meal). Intestinal microsomes showed cytochrome P450 (CYP) 2B, 2C- and 3A-mediated activities and the presence of the corresponding immunorelated proteins, but no proof of CYP1A expression and/or functions could be provided. Intestinal microsomes were also active in performing reactions typically mediated by carboxylesterases (indophenylacetate hydrolysis), flavin-containing monooxygenases (methimazole S-oxidation), and uridindiphosphoglucuronyltransferases (1-naphthol glucuronidation), respectively. Cytosolic fractions displayed the glutathione S-transferase (GST)-dependent conjugation of 1-chloro-2,4-dinitrobenzene; besides, the GST-mediated conjugation of ethacrinic acid (GSTφ) or cumene hydroperoxide (GSTα) was matched by the presence of the corresponding immunorelated proteins. Conversely, despite the lack of measurable activity with 3,4-dichloronitrobenzene, a protein cross reacting with anti-rat GSTμ antibodies could be clearly detected. Although, as detected by densitometry, CYPs and GST isoenzymes tended to be more expressed in beef cattle than in veal calf preparations, there was a general poor correlation with the rate of the in vitro metabolism of the selected diagnostic probes.Fil: Virkel, Guillermo Leon. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Departamento de Fisiopatología. Laboratorio de Farmacología; Argentina. 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: Carletti, M.. Universita degli Studi di Torino; ItaliaFil: Cantiello, M.. Universita degli Studi di Torino; ItaliaFil: Della Donna, L.. Universita degli Studi di Torino; ItaliaFil: Gardini, G.. Universita degli Studi di Torino; ItaliaFil: Girolami, F.. Universita degli Studi di Torino; ItaliaFil: Nebbia, C.. Universita degli Studi di Torino; ItaliaWiley Blackwell Publishing, Inc2010-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/83897Virkel, Guillermo Leon; Carletti, M.; Cantiello, M.; Della Donna, L.; Gardini, G.; et al.; Characterization of xenobiotic metabolizing enzymes in bovine small intestinal mucosa; Wiley Blackwell Publishing, Inc; Journal of Veterinary Pharmacology and Therapeutics; 33; 3; 2-2010; 295-3030140-7783CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1111/j.1365-2885.2009.01137.xinfo:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1111/j.1365-2885.2009.01137.xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:11:03Zoai:ri.conicet.gov.ar:11336/83897instacron: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:34982025-09-03 10:11:03.714CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Characterization of xenobiotic metabolizing enzymes in bovine small intestinal mucosa
title Characterization of xenobiotic metabolizing enzymes in bovine small intestinal mucosa
spellingShingle Characterization of xenobiotic metabolizing enzymes in bovine small intestinal mucosa
Virkel, Guillermo Leon
Xenobiotic Metabolizing Enzymes
Intestinal Mucosa
Microsomes
Cattle
title_short Characterization of xenobiotic metabolizing enzymes in bovine small intestinal mucosa
title_full Characterization of xenobiotic metabolizing enzymes in bovine small intestinal mucosa
title_fullStr Characterization of xenobiotic metabolizing enzymes in bovine small intestinal mucosa
title_full_unstemmed Characterization of xenobiotic metabolizing enzymes in bovine small intestinal mucosa
title_sort Characterization of xenobiotic metabolizing enzymes in bovine small intestinal mucosa
dc.creator.none.fl_str_mv Virkel, Guillermo Leon
Carletti, M.
Cantiello, M.
Della Donna, L.
Gardini, G.
Girolami, F.
Nebbia, C.
author Virkel, Guillermo Leon
author_facet Virkel, Guillermo Leon
Carletti, M.
Cantiello, M.
Della Donna, L.
Gardini, G.
Girolami, F.
Nebbia, C.
author_role author
author2 Carletti, M.
Cantiello, M.
Della Donna, L.
Gardini, G.
Girolami, F.
Nebbia, C.
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Xenobiotic Metabolizing Enzymes
Intestinal Mucosa
Microsomes
Cattle
topic Xenobiotic Metabolizing Enzymes
Intestinal Mucosa
Microsomes
Cattle
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 intestinal mucosa plays a capital role in dictating the bioavailability of a large array of orally ingested drugs and toxicants. The activity and the expression of several xenobiotic metabolizing enzymes were measured in subcellular fractions from the duodenal mucosa of male veal calves and beef cattle displaying a functional rumen but differing in both age (about 8 months vs. 18 to 24 months) and dietary regimens (i.e., milk replacer plus hay and straw vs. corn and concentrated meal). Intestinal microsomes showed cytochrome P450 (CYP) 2B, 2C- and 3A-mediated activities and the presence of the corresponding immunorelated proteins, but no proof of CYP1A expression and/or functions could be provided. Intestinal microsomes were also active in performing reactions typically mediated by carboxylesterases (indophenylacetate hydrolysis), flavin-containing monooxygenases (methimazole S-oxidation), and uridindiphosphoglucuronyltransferases (1-naphthol glucuronidation), respectively. Cytosolic fractions displayed the glutathione S-transferase (GST)-dependent conjugation of 1-chloro-2,4-dinitrobenzene; besides, the GST-mediated conjugation of ethacrinic acid (GSTφ) or cumene hydroperoxide (GSTα) was matched by the presence of the corresponding immunorelated proteins. Conversely, despite the lack of measurable activity with 3,4-dichloronitrobenzene, a protein cross reacting with anti-rat GSTμ antibodies could be clearly detected. Although, as detected by densitometry, CYPs and GST isoenzymes tended to be more expressed in beef cattle than in veal calf preparations, there was a general poor correlation with the rate of the in vitro metabolism of the selected diagnostic probes.
Fil: Virkel, Guillermo Leon. Universidad Nacional del Centro de la Provincia de Buenos Aires. Facultad de Ciencias Veterinarias. Departamento de Fisiopatología. Laboratorio de Farmacología; Argentina. 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: Carletti, M.. Universita degli Studi di Torino; Italia
Fil: Cantiello, M.. Universita degli Studi di Torino; Italia
Fil: Della Donna, L.. Universita degli Studi di Torino; Italia
Fil: Gardini, G.. Universita degli Studi di Torino; Italia
Fil: Girolami, F.. Universita degli Studi di Torino; Italia
Fil: Nebbia, C.. Universita degli Studi di Torino; Italia
description The intestinal mucosa plays a capital role in dictating the bioavailability of a large array of orally ingested drugs and toxicants. The activity and the expression of several xenobiotic metabolizing enzymes were measured in subcellular fractions from the duodenal mucosa of male veal calves and beef cattle displaying a functional rumen but differing in both age (about 8 months vs. 18 to 24 months) and dietary regimens (i.e., milk replacer plus hay and straw vs. corn and concentrated meal). Intestinal microsomes showed cytochrome P450 (CYP) 2B, 2C- and 3A-mediated activities and the presence of the corresponding immunorelated proteins, but no proof of CYP1A expression and/or functions could be provided. Intestinal microsomes were also active in performing reactions typically mediated by carboxylesterases (indophenylacetate hydrolysis), flavin-containing monooxygenases (methimazole S-oxidation), and uridindiphosphoglucuronyltransferases (1-naphthol glucuronidation), respectively. Cytosolic fractions displayed the glutathione S-transferase (GST)-dependent conjugation of 1-chloro-2,4-dinitrobenzene; besides, the GST-mediated conjugation of ethacrinic acid (GSTφ) or cumene hydroperoxide (GSTα) was matched by the presence of the corresponding immunorelated proteins. Conversely, despite the lack of measurable activity with 3,4-dichloronitrobenzene, a protein cross reacting with anti-rat GSTμ antibodies could be clearly detected. Although, as detected by densitometry, CYPs and GST isoenzymes tended to be more expressed in beef cattle than in veal calf preparations, there was a general poor correlation with the rate of the in vitro metabolism of the selected diagnostic probes.
publishDate 2010
dc.date.none.fl_str_mv 2010-02
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/11336/83897
Virkel, Guillermo Leon; Carletti, M.; Cantiello, M.; Della Donna, L.; Gardini, G.; et al.; Characterization of xenobiotic metabolizing enzymes in bovine small intestinal mucosa; Wiley Blackwell Publishing, Inc; Journal of Veterinary Pharmacology and Therapeutics; 33; 3; 2-2010; 295-303
0140-7783
CONICET Digital
CONICET
url http://hdl.handle.net/11336/83897
identifier_str_mv Virkel, Guillermo Leon; Carletti, M.; Cantiello, M.; Della Donna, L.; Gardini, G.; et al.; Characterization of xenobiotic metabolizing enzymes in bovine small intestinal mucosa; Wiley Blackwell Publishing, Inc; Journal of Veterinary Pharmacology and Therapeutics; 33; 3; 2-2010; 295-303
0140-7783
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1111/j.1365-2885.2009.01137.x
info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/abs/10.1111/j.1365-2885.2009.01137.x
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
dc.publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
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 13.13397

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