Effect of different orgaphosphates on the hepatic oxidative metabolism by mixed function oxidases in cattle
- Autores
- Larsen, Karen Elizabeth; Lifschitz, Adrian Luis; Virkel, Guillermo Leon
- Año de publicación
- 2021
- Idioma
- inglés
- Tipo de recurso
- documento de conferencia
- Estado
- versión publicada
- Descripción
- Organophosphates (OPs) are widely used for crop protection in agriculture and for the control of ectoparasites in animal husbandry. The sustained use of these chemical compounds increases the risk of environmental contamination and/or alteration of different physiological cellular functions in farm animals. A number of OPs are substrates of hepatic mixed function oxidases, such as those belonging to the cytochrome P450 (CYP) and flavin-containing monooxygenase (FMO) families of enzymes. In addition, these xenobiotics may also affect enzyme function by induction or inhibition of their catalytic activities. This work aimed to evaluate in vitro the effect of the following OPs: chlorpyrifos (CPF), ethion (ETN), diazinon (DZN) and dichlorvos (DCV) on CYP- and FMO-dependent enzyme activities in cattle liver. Bovine (n=4) liver microsomes were incubated (10 min at 37°C in aerobiosis) in the absence (control assays) and in presence of each OP compound under study at 1, 10 and 100 µM (final concentrations). Five CYP- or FMO-dependent catalytic activities were assayed by spectrofluorimetric or HPLC methods: 7-ethoxyresorufin O-deethylase (EROD, for CYP1A1), methoxyresorufin O-demethylase (MROD, for CYP1A2), benzyloxyresorufin O-debenzylase (BROD, for CYP2B), testosterone 6-beta hydroxylase (for CYP3A) and benzydamine N-oxidase (for FMO). Only the CYP3A-dependent hepatic metabolism was significantly affected by the presence of ETN and DZN. ETN, at 10 µM and 100 µM, inhibited (p<0.01) testosterone 6-beta hydroxylase activity (76% and 81%, respectively) in cattle liver microsomes. Similar results were obtained in presence of equimolar concentrations of DZN (74% and 93% at 10 uM and 100 µM, respectively; p<0.01). Both ETN and DZN would potentially interfere with the pattern of the hepatic metabolism of relevant CYP3A substrates pharmacologically relevant in bovine medicine, such as tiamulin, macrolide antibiotics and the ionophore monensin.
Fil: Larsen, Karen Elizabeth. 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 Ecotoxicología; Argentina
Fil: Lifschitz, Adrian Luis. 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: Virkel, Guillermo Leon. 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
LXVI Reunión anual de la Sociedad Argentina de Investigación Clínica (SAIC); LXIX Reunión Anual de la Sociedad Argentina de Inmunología (SAI); LIII Reunión Anual de la Asociación Argentina de Farmacología Experimental (AAFE) y XI Reunión Anual de la Asociación Argentina de Nanomedicinas (NANOMED-AR)
Argentina
Sociedad Argentina de Investigación Clínica
Sociedad Argentina de Inmunología
Asociación Argentina de Farmacología Experimental
Asociación Argentina de Nanomedicinas - Materia
-
ORGANOPHOSPHATES
CYTOCHROME P450
FLAVIN-CONTAINING MONOOXYGENASE
LIVER - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/156074
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Effect of different orgaphosphates on the hepatic oxidative metabolism by mixed function oxidases in cattleLarsen, Karen ElizabethLifschitz, Adrian LuisVirkel, Guillermo LeonORGANOPHOSPHATESCYTOCHROME P450FLAVIN-CONTAINING MONOOXYGENASELIVERhttps://purl.org/becyt/ford/4.3https://purl.org/becyt/ford/4Organophosphates (OPs) are widely used for crop protection in agriculture and for the control of ectoparasites in animal husbandry. The sustained use of these chemical compounds increases the risk of environmental contamination and/or alteration of different physiological cellular functions in farm animals. A number of OPs are substrates of hepatic mixed function oxidases, such as those belonging to the cytochrome P450 (CYP) and flavin-containing monooxygenase (FMO) families of enzymes. In addition, these xenobiotics may also affect enzyme function by induction or inhibition of their catalytic activities. This work aimed to evaluate in vitro the effect of the following OPs: chlorpyrifos (CPF), ethion (ETN), diazinon (DZN) and dichlorvos (DCV) on CYP- and FMO-dependent enzyme activities in cattle liver. Bovine (n=4) liver microsomes were incubated (10 min at 37°C in aerobiosis) in the absence (control assays) and in presence of each OP compound under study at 1, 10 and 100 µM (final concentrations). Five CYP- or FMO-dependent catalytic activities were assayed by spectrofluorimetric or HPLC methods: 7-ethoxyresorufin O-deethylase (EROD, for CYP1A1), methoxyresorufin O-demethylase (MROD, for CYP1A2), benzyloxyresorufin O-debenzylase (BROD, for CYP2B), testosterone 6-beta hydroxylase (for CYP3A) and benzydamine N-oxidase (for FMO). Only the CYP3A-dependent hepatic metabolism was significantly affected by the presence of ETN and DZN. ETN, at 10 µM and 100 µM, inhibited (p<0.01) testosterone 6-beta hydroxylase activity (76% and 81%, respectively) in cattle liver microsomes. Similar results were obtained in presence of equimolar concentrations of DZN (74% and 93% at 10 uM and 100 µM, respectively; p<0.01). Both ETN and DZN would potentially interfere with the pattern of the hepatic metabolism of relevant CYP3A substrates pharmacologically relevant in bovine medicine, such as tiamulin, macrolide antibiotics and the ionophore monensin.Fil: Larsen, Karen Elizabeth. 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 Ecotoxicología; ArgentinaFil: Lifschitz, Adrian Luis. 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: Virkel, Guillermo Leon. 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; ArgentinaLXVI Reunión anual de la Sociedad Argentina de Investigación Clínica (SAIC); LXIX Reunión Anual de la Sociedad Argentina de Inmunología (SAI); LIII Reunión Anual de la Asociación Argentina de Farmacología Experimental (AAFE) y XI Reunión Anual de la Asociación Argentina de Nanomedicinas (NANOMED-AR)ArgentinaSociedad Argentina de Investigación ClínicaSociedad Argentina de InmunologíaAsociación Argentina de Farmacología ExperimentalAsociación Argentina de NanomedicinasFundación Revista Medicina2021info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectReuniónJournalhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/156074Effect of different orgaphosphates on the hepatic oxidative metabolism by mixed function oxidases in cattle; LXVI Reunión anual de la Sociedad Argentina de Investigación Clínica (SAIC); LXIX Reunión Anual de la Sociedad Argentina de Inmunología (SAI); LIII Reunión Anual de la Asociación Argentina de Farmacología Experimental (AAFE) y XI Reunión Anual de la Asociación Argentina de Nanomedicinas (NANOMED-AR); Argentina; 2021; 94-951669-9106CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://medicinabuenosaires.com/revistas/vol81-21/s3/Mv81s3.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 Técnicas2025-09-10T13:10:14Zoai:ri.conicet.gov.ar:11336/156074instacron: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 13:10:15.048CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Effect of different orgaphosphates on the hepatic oxidative metabolism by mixed function oxidases in cattle |
title |
Effect of different orgaphosphates on the hepatic oxidative metabolism by mixed function oxidases in cattle |
spellingShingle |
Effect of different orgaphosphates on the hepatic oxidative metabolism by mixed function oxidases in cattle Larsen, Karen Elizabeth ORGANOPHOSPHATES CYTOCHROME P450 FLAVIN-CONTAINING MONOOXYGENASE LIVER |
title_short |
Effect of different orgaphosphates on the hepatic oxidative metabolism by mixed function oxidases in cattle |
title_full |
Effect of different orgaphosphates on the hepatic oxidative metabolism by mixed function oxidases in cattle |
title_fullStr |
Effect of different orgaphosphates on the hepatic oxidative metabolism by mixed function oxidases in cattle |
title_full_unstemmed |
Effect of different orgaphosphates on the hepatic oxidative metabolism by mixed function oxidases in cattle |
title_sort |
Effect of different orgaphosphates on the hepatic oxidative metabolism by mixed function oxidases in cattle |
dc.creator.none.fl_str_mv |
Larsen, Karen Elizabeth Lifschitz, Adrian Luis Virkel, Guillermo Leon |
author |
Larsen, Karen Elizabeth |
author_facet |
Larsen, Karen Elizabeth Lifschitz, Adrian Luis Virkel, Guillermo Leon |
author_role |
author |
author2 |
Lifschitz, Adrian Luis Virkel, Guillermo Leon |
author2_role |
author author |
dc.subject.none.fl_str_mv |
ORGANOPHOSPHATES CYTOCHROME P450 FLAVIN-CONTAINING MONOOXYGENASE LIVER |
topic |
ORGANOPHOSPHATES CYTOCHROME P450 FLAVIN-CONTAINING MONOOXYGENASE LIVER |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/4.3 https://purl.org/becyt/ford/4 |
dc.description.none.fl_txt_mv |
Organophosphates (OPs) are widely used for crop protection in agriculture and for the control of ectoparasites in animal husbandry. The sustained use of these chemical compounds increases the risk of environmental contamination and/or alteration of different physiological cellular functions in farm animals. A number of OPs are substrates of hepatic mixed function oxidases, such as those belonging to the cytochrome P450 (CYP) and flavin-containing monooxygenase (FMO) families of enzymes. In addition, these xenobiotics may also affect enzyme function by induction or inhibition of their catalytic activities. This work aimed to evaluate in vitro the effect of the following OPs: chlorpyrifos (CPF), ethion (ETN), diazinon (DZN) and dichlorvos (DCV) on CYP- and FMO-dependent enzyme activities in cattle liver. Bovine (n=4) liver microsomes were incubated (10 min at 37°C in aerobiosis) in the absence (control assays) and in presence of each OP compound under study at 1, 10 and 100 µM (final concentrations). Five CYP- or FMO-dependent catalytic activities were assayed by spectrofluorimetric or HPLC methods: 7-ethoxyresorufin O-deethylase (EROD, for CYP1A1), methoxyresorufin O-demethylase (MROD, for CYP1A2), benzyloxyresorufin O-debenzylase (BROD, for CYP2B), testosterone 6-beta hydroxylase (for CYP3A) and benzydamine N-oxidase (for FMO). Only the CYP3A-dependent hepatic metabolism was significantly affected by the presence of ETN and DZN. ETN, at 10 µM and 100 µM, inhibited (p<0.01) testosterone 6-beta hydroxylase activity (76% and 81%, respectively) in cattle liver microsomes. Similar results were obtained in presence of equimolar concentrations of DZN (74% and 93% at 10 uM and 100 µM, respectively; p<0.01). Both ETN and DZN would potentially interfere with the pattern of the hepatic metabolism of relevant CYP3A substrates pharmacologically relevant in bovine medicine, such as tiamulin, macrolide antibiotics and the ionophore monensin. Fil: Larsen, Karen Elizabeth. 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 Ecotoxicología; Argentina Fil: Lifschitz, Adrian Luis. 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: Virkel, Guillermo Leon. 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 LXVI Reunión anual de la Sociedad Argentina de Investigación Clínica (SAIC); LXIX Reunión Anual de la Sociedad Argentina de Inmunología (SAI); LIII Reunión Anual de la Asociación Argentina de Farmacología Experimental (AAFE) y XI Reunión Anual de la Asociación Argentina de Nanomedicinas (NANOMED-AR) Argentina Sociedad Argentina de Investigación Clínica Sociedad Argentina de Inmunología Asociación Argentina de Farmacología Experimental Asociación Argentina de Nanomedicinas |
description |
Organophosphates (OPs) are widely used for crop protection in agriculture and for the control of ectoparasites in animal husbandry. The sustained use of these chemical compounds increases the risk of environmental contamination and/or alteration of different physiological cellular functions in farm animals. A number of OPs are substrates of hepatic mixed function oxidases, such as those belonging to the cytochrome P450 (CYP) and flavin-containing monooxygenase (FMO) families of enzymes. In addition, these xenobiotics may also affect enzyme function by induction or inhibition of their catalytic activities. This work aimed to evaluate in vitro the effect of the following OPs: chlorpyrifos (CPF), ethion (ETN), diazinon (DZN) and dichlorvos (DCV) on CYP- and FMO-dependent enzyme activities in cattle liver. Bovine (n=4) liver microsomes were incubated (10 min at 37°C in aerobiosis) in the absence (control assays) and in presence of each OP compound under study at 1, 10 and 100 µM (final concentrations). Five CYP- or FMO-dependent catalytic activities were assayed by spectrofluorimetric or HPLC methods: 7-ethoxyresorufin O-deethylase (EROD, for CYP1A1), methoxyresorufin O-demethylase (MROD, for CYP1A2), benzyloxyresorufin O-debenzylase (BROD, for CYP2B), testosterone 6-beta hydroxylase (for CYP3A) and benzydamine N-oxidase (for FMO). Only the CYP3A-dependent hepatic metabolism was significantly affected by the presence of ETN and DZN. ETN, at 10 µM and 100 µM, inhibited (p<0.01) testosterone 6-beta hydroxylase activity (76% and 81%, respectively) in cattle liver microsomes. Similar results were obtained in presence of equimolar concentrations of DZN (74% and 93% at 10 uM and 100 µM, respectively; p<0.01). Both ETN and DZN would potentially interfere with the pattern of the hepatic metabolism of relevant CYP3A substrates pharmacologically relevant in bovine medicine, such as tiamulin, macrolide antibiotics and the ionophore monensin. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/publishedVersion info:eu-repo/semantics/conferenceObject Reunión 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/11336/156074 Effect of different orgaphosphates on the hepatic oxidative metabolism by mixed function oxidases in cattle; LXVI Reunión anual de la Sociedad Argentina de Investigación Clínica (SAIC); LXIX Reunión Anual de la Sociedad Argentina de Inmunología (SAI); LIII Reunión Anual de la Asociación Argentina de Farmacología Experimental (AAFE) y XI Reunión Anual de la Asociación Argentina de Nanomedicinas (NANOMED-AR); Argentina; 2021; 94-95 1669-9106 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/156074 |
identifier_str_mv |
Effect of different orgaphosphates on the hepatic oxidative metabolism by mixed function oxidases in cattle; LXVI Reunión anual de la Sociedad Argentina de Investigación Clínica (SAIC); LXIX Reunión Anual de la Sociedad Argentina de Inmunología (SAI); LIII Reunión Anual de la Asociación Argentina de Farmacología Experimental (AAFE) y XI Reunión Anual de la Asociación Argentina de Nanomedicinas (NANOMED-AR); Argentina; 2021; 94-95 1669-9106 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://medicinabuenosaires.com/revistas/vol81-21/s3/Mv81s3.pdf |
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/ |
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application/pdf application/pdf application/pdf |
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Internacional |
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Fundación Revista Medicina |
publisher.none.fl_str_mv |
Fundación Revista Medicina |
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reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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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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