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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/225907
Ver los metadatos del registro completo
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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 |
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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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