Anandamide hydrolysis is modulated by cannabinoid receptors in aged rat cerebral cortex

Autores
Pascual, Ana Clara; Gaveglio, Virginia Lucía; Giusto, Norma Maria; Pasquaré, Susana Juana
Año de publicación
2014
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
Fatty acid amide hydrolase (FAAH) has been reported as the main enzyme involved in anandamide (AEA) hydrolysis. Among the multiple functions of AEA we can highlight the regulation of synaptic plasticity and its antiinflammatory role. The aim of this study was to analyze AEA hydrolysis in cerebral cortex (CC) subcellular fractions during physiological aging and its regulation by cannabinoid receptors (CBR). CC membrane and synaptosomal fractions from adult (3 mo) and aged (28 mo) rats were isolated by differential centrifugation and the synaptosomal fraction was purified in ficoll gradients. AEA hydrolysis was assayed using [3H]AEA and its product was quantified from the aqueous phase. Aging differently modulated FAAH by increasing and decreasing its activity in membranes and synaptosomes, respectively. In the presence of FAAH specific inhibitor URB-597 AEA hydrolysis activity assay corroborates that AEA is the main enzyme involved in CC AEA degradation. CBR agonists decreased FAAH activity, mainly by CB2R, thus increasing CC AEA availability. Our results show that while aged CC membrane AEA availability decreases, possibly compromising its antiinflammatory functions, the endocannaboid level in synaptosomes increases, protecting against the synaptic dysfunction inflicted by aging. AEA availability could be increased by targeting CB2R, thus improving brain damage caused by aging
Fil: Pascual, Ana Clara. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Gaveglio, Virginia Lucía. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Giusto, Norma Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Pasquaré, Susana Juana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
L Reunión Anual de la Sociedad de Investigación en Bioquímica y Biología Molecular (SAIB)
Rosario
Argentina
Sociedad de Investigación en Bioquímica y Biología Molecular
Materia
ANANDAMIDA
FAAH
SINAPTOSOMA
ENVEJECIMIENTO
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:11336/225979
Acceder
id CONICETDig_7c875dce2bfbd57a5173535a2675e591
oai_identifier_str oai:ri.conicet.gov.ar:11336/225979
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Anandamide hydrolysis is modulated by cannabinoid receptors in aged rat cerebral cortexPascual, Ana ClaraGaveglio, Virginia LucíaGiusto, Norma MariaPasquaré, Susana JuanaANANDAMIDAFAAHSINAPTOSOMAENVEJECIMIENTOhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Fatty acid amide hydrolase (FAAH) has been reported as the main enzyme involved in anandamide (AEA) hydrolysis. Among the multiple functions of AEA we can highlight the regulation of synaptic plasticity and its antiinflammatory role. The aim of this study was to analyze AEA hydrolysis in cerebral cortex (CC) subcellular fractions during physiological aging and its regulation by cannabinoid receptors (CBR). CC membrane and synaptosomal fractions from adult (3 mo) and aged (28 mo) rats were isolated by differential centrifugation and the synaptosomal fraction was purified in ficoll gradients. AEA hydrolysis was assayed using [3H]AEA and its product was quantified from the aqueous phase. Aging differently modulated FAAH by increasing and decreasing its activity in membranes and synaptosomes, respectively. In the presence of FAAH specific inhibitor URB-597 AEA hydrolysis activity assay corroborates that AEA is the main enzyme involved in CC AEA degradation. CBR agonists decreased FAAH activity, mainly by CB2R, thus increasing CC AEA availability. Our results show that while aged CC membrane AEA availability decreases, possibly compromising its antiinflammatory functions, the endocannaboid level in synaptosomes increases, protecting against the synaptic dysfunction inflicted by aging. AEA availability could be increased by targeting CB2R, thus improving brain damage caused by agingFil: Pascual, Ana Clara. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; ArgentinaFil: Gaveglio, Virginia Lucía. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; ArgentinaFil: Giusto, Norma Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; ArgentinaFil: Pasquaré, Susana Juana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; ArgentinaL Reunión Anual de la Sociedad de Investigación en Bioquímica y Biología Molecular (SAIB)RosarioArgentinaSociedad de Investigación en Bioquímica y Biología MolecularBiocellBurgos, Mario H.Piezzi, Ramon Salvador2014info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectCongresoJournalhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/225979Anandamide hydrolysis is modulated by cannabinoid receptors in aged rat cerebral cortex; L Reunión Anual de la Sociedad de Investigación en Bioquímica y Biología Molecular (SAIB); Rosario; Argentina; 2014; 157-1570327-95451667-5746CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.techscience.com/biocell/v38nSuppl.S/34067/pdfNacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:01:32Zoai:ri.conicet.gov.ar:11336/225979instacron: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:34982025-10-22 12:01:32.516CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Anandamide hydrolysis is modulated by cannabinoid receptors in aged rat cerebral cortex
title Anandamide hydrolysis is modulated by cannabinoid receptors in aged rat cerebral cortex
spellingShingle Anandamide hydrolysis is modulated by cannabinoid receptors in aged rat cerebral cortex
Pascual, Ana Clara
ANANDAMIDA
FAAH
SINAPTOSOMA
ENVEJECIMIENTO
title_short Anandamide hydrolysis is modulated by cannabinoid receptors in aged rat cerebral cortex
title_full Anandamide hydrolysis is modulated by cannabinoid receptors in aged rat cerebral cortex
title_fullStr Anandamide hydrolysis is modulated by cannabinoid receptors in aged rat cerebral cortex
title_full_unstemmed Anandamide hydrolysis is modulated by cannabinoid receptors in aged rat cerebral cortex
title_sort Anandamide hydrolysis is modulated by cannabinoid receptors in aged rat cerebral cortex
dc.creator.none.fl_str_mv Pascual, Ana Clara
Gaveglio, Virginia Lucía
Giusto, Norma Maria
Pasquaré, Susana Juana
author Pascual, Ana Clara
author_facet Pascual, Ana Clara
Gaveglio, Virginia Lucía
Giusto, Norma Maria
Pasquaré, Susana Juana
author_role author
author2 Gaveglio, Virginia Lucía
Giusto, Norma Maria
Pasquaré, Susana Juana
author2_role author
author
author
dc.contributor.none.fl_str_mv Burgos, Mario H.
Piezzi, Ramon Salvador
dc.subject.none.fl_str_mv ANANDAMIDA
FAAH
SINAPTOSOMA
ENVEJECIMIENTO
topic ANANDAMIDA
FAAH
SINAPTOSOMA
ENVEJECIMIENTO
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Fatty acid amide hydrolase (FAAH) has been reported as the main enzyme involved in anandamide (AEA) hydrolysis. Among the multiple functions of AEA we can highlight the regulation of synaptic plasticity and its antiinflammatory role. The aim of this study was to analyze AEA hydrolysis in cerebral cortex (CC) subcellular fractions during physiological aging and its regulation by cannabinoid receptors (CBR). CC membrane and synaptosomal fractions from adult (3 mo) and aged (28 mo) rats were isolated by differential centrifugation and the synaptosomal fraction was purified in ficoll gradients. AEA hydrolysis was assayed using [3H]AEA and its product was quantified from the aqueous phase. Aging differently modulated FAAH by increasing and decreasing its activity in membranes and synaptosomes, respectively. In the presence of FAAH specific inhibitor URB-597 AEA hydrolysis activity assay corroborates that AEA is the main enzyme involved in CC AEA degradation. CBR agonists decreased FAAH activity, mainly by CB2R, thus increasing CC AEA availability. Our results show that while aged CC membrane AEA availability decreases, possibly compromising its antiinflammatory functions, the endocannaboid level in synaptosomes increases, protecting against the synaptic dysfunction inflicted by aging. AEA availability could be increased by targeting CB2R, thus improving brain damage caused by aging
Fil: Pascual, Ana Clara. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Gaveglio, Virginia Lucía. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Giusto, Norma Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
Fil: Pasquaré, Susana Juana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca. Instituto de Investigaciones Bioquímicas de Bahía Blanca. Universidad Nacional del Sur. Instituto de Investigaciones Bioquímicas de Bahía Blanca; Argentina
L Reunión Anual de la Sociedad de Investigación en Bioquímica y Biología Molecular (SAIB)
Rosario
Argentina
Sociedad de Investigación en Bioquímica y Biología Molecular
description Fatty acid amide hydrolase (FAAH) has been reported as the main enzyme involved in anandamide (AEA) hydrolysis. Among the multiple functions of AEA we can highlight the regulation of synaptic plasticity and its antiinflammatory role. The aim of this study was to analyze AEA hydrolysis in cerebral cortex (CC) subcellular fractions during physiological aging and its regulation by cannabinoid receptors (CBR). CC membrane and synaptosomal fractions from adult (3 mo) and aged (28 mo) rats were isolated by differential centrifugation and the synaptosomal fraction was purified in ficoll gradients. AEA hydrolysis was assayed using [3H]AEA and its product was quantified from the aqueous phase. Aging differently modulated FAAH by increasing and decreasing its activity in membranes and synaptosomes, respectively. In the presence of FAAH specific inhibitor URB-597 AEA hydrolysis activity assay corroborates that AEA is the main enzyme involved in CC AEA degradation. CBR agonists decreased FAAH activity, mainly by CB2R, thus increasing CC AEA availability. Our results show that while aged CC membrane AEA availability decreases, possibly compromising its antiinflammatory functions, the endocannaboid level in synaptosomes increases, protecting against the synaptic dysfunction inflicted by aging. AEA availability could be increased by targeting CB2R, thus improving brain damage caused by aging
publishDate 2014
dc.date.none.fl_str_mv 2014
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/conferenceObject
Congreso
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/11336/225979
Anandamide hydrolysis is modulated by cannabinoid receptors in aged rat cerebral cortex; L Reunión Anual de la Sociedad de Investigación en Bioquímica y Biología Molecular (SAIB); Rosario; Argentina; 2014; 157-157
0327-9545
1667-5746
CONICET Digital
CONICET
url http://hdl.handle.net/11336/225979
identifier_str_mv Anandamide hydrolysis is modulated by cannabinoid receptors in aged rat cerebral cortex; L Reunión Anual de la Sociedad de Investigación en Bioquímica y Biología Molecular (SAIB); Rosario; Argentina; 2014; 157-157
0327-9545
1667-5746
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://www.techscience.com/biocell/v38nSuppl.S/34067/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/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.coverage.none.fl_str_mv Nacional
dc.publisher.none.fl_str_mv Biocell
publisher.none.fl_str_mv Biocell
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 12.982451

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