Aged-related changes in 2-AG metabolism enzymes expression and activity in rat cerebral cortex

Autores
Pascual, Ana Clara; Giusto, Norma Maria; Pasquaré, Susana Juana
Año de publicación
2012
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
Endocannabinoid 2-arachidonoylglycerol (2-AG) is synthesized by the enzymes diacylglycerol lipase (DAGL) and lysophosphatidate phosphohydrolase (LPAase). Its hydrolysis is carried out by monoacylglycerol lipase (MAGL) although other enzymes, such as fatty acid amide hydrolase (FAAH) and serine hydrolase ABHD may also be involved. The aim of this study was to analyze 2-AG synthesis and hydrolysis during physiological aging. Cerebral cortex membrane and soluble fractions; and synaptosomes from adult (3 mo) and aged (28 mo) rats were isolated by differential centrifugation and the synaptosomes were purified in ficoll gradients. LPAase, DAGL, and MAGLactivities were assayed using radiolabeled substrates, and their products were quantified from aqueous or lipid phase, previously separated by TLC. The expression of DAGL, MAGL and FAAH was analyzed by Western Blot. Both DAGL and ß were expressed in membranes while the second was only expressed in synaptosomes. The expression and activitiy of DAGL changed during aging. 2-AG hydrolysis showed no changes in the membrane fraction during aging in coincidence with the absence of changes in MAGL expression. 2-AG hydrolysis was observed to be higher in synaptosomes whereas MAGL expression decreased during aging. Our results show that the expression and activity of the enzymes involved in 2-AG metabolism are differently modulated 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: 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. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina. 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
XLVIII Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular
Mendoza
Argentina
Sociedad Argentina de Investigaciones en Bioquímica y Biología Molecular
Materia
2- ARACHIDONOYL GLYCEROL
SYNAPTOSOMES
AGING
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:11336/225907

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network_name_str CONICET Digital (CONICET)
spelling Aged-related changes in 2-AG metabolism enzymes expression and activity in rat cerebral cortexPascual, Ana ClaraGiusto, Norma MariaPasquaré, Susana Juana2- ARACHIDONOYL GLYCEROLSYNAPTOSOMESAGINGhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Endocannabinoid 2-arachidonoylglycerol (2-AG) is synthesized by the enzymes diacylglycerol lipase (DAGL) and lysophosphatidate phosphohydrolase (LPAase). Its hydrolysis is carried out by monoacylglycerol lipase (MAGL) although other enzymes, such as fatty acid amide hydrolase (FAAH) and serine hydrolase ABHD may also be involved. The aim of this study was to analyze 2-AG synthesis and hydrolysis during physiological aging. Cerebral cortex membrane and soluble fractions; and synaptosomes from adult (3 mo) and aged (28 mo) rats were isolated by differential centrifugation and the synaptosomes were purified in ficoll gradients. LPAase, DAGL, and MAGLactivities were assayed using radiolabeled substrates, and their products were quantified from aqueous or lipid phase, previously separated by TLC. The expression of DAGL, MAGL and FAAH was analyzed by Western Blot. Both DAGL and ß were expressed in membranes while the second was only expressed in synaptosomes. The expression and activitiy of DAGL changed during aging. 2-AG hydrolysis showed no changes in the membrane fraction during aging in coincidence with the absence of changes in MAGL expression. 2-AG hydrolysis was observed to be higher in synaptosomes whereas MAGL expression decreased during aging. Our results show that the expression and activity of the enzymes involved in 2-AG metabolism are differently modulated 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; 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. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina. 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; ArgentinaXLVIII Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología MolecularMendozaArgentinaSociedad Argentina de Investigaciones en Bioquímica y Biología MolecularUniversidad Nacional de Cuyo2012info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectReuniónJournalhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/vnd.openxmlformats-officedocument.wordprocessingml.documentapplication/vnd.openxmlformats-officedocument.wordprocessingml.documentapplication/pdfhttp://hdl.handle.net/11336/225907Aged-related changes in 2-AG metabolism enzymes expression and activity in rat cerebral cortex; XLVIII Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; Mendoza; Argentina; 2012; 109-1090327-95451667-5746CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://saib.org.ar/archivos/biocell-36.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 Técnicas2025-09-10T13:09:25Zoai:ri.conicet.gov.ar:11336/225907instacron: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 13:09:26.041CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Aged-related changes in 2-AG metabolism enzymes expression and activity in rat cerebral cortex
title Aged-related changes in 2-AG metabolism enzymes expression and activity in rat cerebral cortex
spellingShingle Aged-related changes in 2-AG metabolism enzymes expression and activity in rat cerebral cortex
Pascual, Ana Clara
2- ARACHIDONOYL GLYCEROL
SYNAPTOSOMES
AGING
title_short Aged-related changes in 2-AG metabolism enzymes expression and activity in rat cerebral cortex
title_full Aged-related changes in 2-AG metabolism enzymes expression and activity in rat cerebral cortex
title_fullStr Aged-related changes in 2-AG metabolism enzymes expression and activity in rat cerebral cortex
title_full_unstemmed Aged-related changes in 2-AG metabolism enzymes expression and activity in rat cerebral cortex
title_sort Aged-related changes in 2-AG metabolism enzymes expression and activity in rat cerebral cortex
dc.creator.none.fl_str_mv Pascual, Ana Clara
Giusto, Norma Maria
Pasquaré, Susana Juana
author Pascual, Ana Clara
author_facet Pascual, Ana Clara
Giusto, Norma Maria
Pasquaré, Susana Juana
author_role author
author2 Giusto, Norma Maria
Pasquaré, Susana Juana
author2_role author
author
dc.subject.none.fl_str_mv 2- ARACHIDONOYL GLYCEROL
SYNAPTOSOMES
AGING
topic 2- ARACHIDONOYL GLYCEROL
SYNAPTOSOMES
AGING
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Endocannabinoid 2-arachidonoylglycerol (2-AG) is synthesized by the enzymes diacylglycerol lipase (DAGL) and lysophosphatidate phosphohydrolase (LPAase). Its hydrolysis is carried out by monoacylglycerol lipase (MAGL) although other enzymes, such as fatty acid amide hydrolase (FAAH) and serine hydrolase ABHD may also be involved. The aim of this study was to analyze 2-AG synthesis and hydrolysis during physiological aging. Cerebral cortex membrane and soluble fractions; and synaptosomes from adult (3 mo) and aged (28 mo) rats were isolated by differential centrifugation and the synaptosomes were purified in ficoll gradients. LPAase, DAGL, and MAGLactivities were assayed using radiolabeled substrates, and their products were quantified from aqueous or lipid phase, previously separated by TLC. The expression of DAGL, MAGL and FAAH was analyzed by Western Blot. Both DAGL and ß were expressed in membranes while the second was only expressed in synaptosomes. The expression and activitiy of DAGL changed during aging. 2-AG hydrolysis showed no changes in the membrane fraction during aging in coincidence with the absence of changes in MAGL expression. 2-AG hydrolysis was observed to be higher in synaptosomes whereas MAGL expression decreased during aging. Our results show that the expression and activity of the enzymes involved in 2-AG metabolism are differently modulated 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: 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. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina. 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
XLVIII Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular
Mendoza
Argentina
Sociedad Argentina de Investigaciones en Bioquímica y Biología Molecular
description Endocannabinoid 2-arachidonoylglycerol (2-AG) is synthesized by the enzymes diacylglycerol lipase (DAGL) and lysophosphatidate phosphohydrolase (LPAase). Its hydrolysis is carried out by monoacylglycerol lipase (MAGL) although other enzymes, such as fatty acid amide hydrolase (FAAH) and serine hydrolase ABHD may also be involved. The aim of this study was to analyze 2-AG synthesis and hydrolysis during physiological aging. Cerebral cortex membrane and soluble fractions; and synaptosomes from adult (3 mo) and aged (28 mo) rats were isolated by differential centrifugation and the synaptosomes were purified in ficoll gradients. LPAase, DAGL, and MAGLactivities were assayed using radiolabeled substrates, and their products were quantified from aqueous or lipid phase, previously separated by TLC. The expression of DAGL, MAGL and FAAH was analyzed by Western Blot. Both DAGL and ß were expressed in membranes while the second was only expressed in synaptosomes. The expression and activitiy of DAGL changed during aging. 2-AG hydrolysis showed no changes in the membrane fraction during aging in coincidence with the absence of changes in MAGL expression. 2-AG hydrolysis was observed to be higher in synaptosomes whereas MAGL expression decreased during aging. Our results show that the expression and activity of the enzymes involved in 2-AG metabolism are differently modulated by aging.
publishDate 2012
dc.date.none.fl_str_mv 2012
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/11336/225907
Aged-related changes in 2-AG metabolism enzymes expression and activity in rat cerebral cortex; XLVIII Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; Mendoza; Argentina; 2012; 109-109
0327-9545
1667-5746
CONICET Digital
CONICET
url http://hdl.handle.net/11336/225907
identifier_str_mv Aged-related changes in 2-AG metabolism enzymes expression and activity in rat cerebral cortex; XLVIII Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; Mendoza; Argentina; 2012; 109-109
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://saib.org.ar/archivos/biocell-36.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/vnd.openxmlformats-officedocument.wordprocessingml.document
application/vnd.openxmlformats-officedocument.wordprocessingml.document
application/pdf
dc.coverage.none.fl_str_mv Nacional
dc.publisher.none.fl_str_mv Universidad Nacional de Cuyo
publisher.none.fl_str_mv Universidad Nacional de Cuyo
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
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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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