Aging Modifies the Enzymatic Activities Involved in 2-Arachidonoylglycerol Metabolism

Autores
Pascual, Ana Clara; Gaveglio, Virginia Lucía; Giusto, Norma Maria; Pasquaré, Susana Juana
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
One of the principal monoacylglycerol (MAG) species in animal tissues is 2-arachidonoylglycerol (2-AG), and the diacylglycerol lipase (DAGL) pathway is the most important 2-AG biosynthetic pathway proposed to date. Lysophosphatidate phosphatase (LPAase) activity is part of another 2-AG-forming pathway in which monoacylglycerol lipase (MAGL) is the major degrading enzyme. The purpose of this study was to analyze the manner in which DAGL, LPAase, and MAGL enzymes are modified in the central nervous system (CNS) during aging. To this end, diacylglycerols (DAGs) and MAGs of different composition were used as substrates of DAGL and MAGL, respectively. All enzymatic activities were evaluated in membrane and soluble fractions as well as in synaptic terminals from the cerebral cortex (CC) of adult and aged rats. Results related to 2-AG metabolism show that aging: (a) decreases DAGL-alfa expression in the membrane fraction whereas in synaptosomes it increases DAGL-beta and decreases MAGL expression; (b) decreases LPAase activity in both membrane and soluble fractions; (c) decreases DAGL and stimulates LPAase activities in CC synaptic terminals; (d) stimulates membrane-associated MAGL-coupled DAGL activity; and (e) stimulates MAGL activity in CC synaptosomes. Our results also reveal that during aging the net balance between the enzymatic activities involved in 2-AG synthesis and breakdown is low availability of 2-AG in CC membrane fractions and synaptic terminals. Taken together, our results lead us to conclude that these enzymes play crucial roles in the regulation of 2-AG tissue levels during aging.
Fil: Pascual, Ana Clara. Universidad Nacional del Sur; Argentina. Consejo Nacional de Investigaciones Cientí­ficas y Técnicas. Centro Científico Tecnológico Bahí­a Blanca. Instituto de Investigaciones Bioquímicas Bahí­a Blanca (i); Argentina
Fil: Gaveglio, Virginia Lucía. Universidad Nacional del Sur; Argentina. Consejo Nacional de Investigaciones Cientí­ficas y Técnicas. Centro Científico Tecnológico Bahí­a Blanca. Instituto de Investigaciones Bioquímicas Bahí­a Blanca (i); Argentina
Fil: Giusto, Norma Maria. Universidad Nacional del Sur; Argentina. Consejo Nacional de Investigaciones Cientí­ficas y Técnicas. Centro Científico Tecnológico Bahí­a Blanca. Instituto de Investigaciones Bioquímicas Bahí­a Blanca (i); Argentina
Fil: Pasquaré, Susana Juana. Universidad Nacional del Sur; Argentina. Consejo Nacional de Investigaciones Cientí­ficas y Técnicas. Centro Científico Tecnológico Bahí­a Blanca. Instituto de Investigaciones Bioquímicas Bahí­a Blanca (i); Argentina
Materia
2-Arachidonoylglycerol
Cerebral Cortex
Lysophosphatidic Acid
Synaptosomes
Monoacylglycerol
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:11336/4666
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/4666
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Aging Modifies the Enzymatic Activities Involved in 2-Arachidonoylglycerol MetabolismPascual, Ana ClaraGaveglio, Virginia LucíaGiusto, Norma MariaPasquaré, Susana Juana2-ArachidonoylglycerolCerebral CortexLysophosphatidic AcidSynaptosomesMonoacylglycerolhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1One of the principal monoacylglycerol (MAG) species in animal tissues is 2-arachidonoylglycerol (2-AG), and the diacylglycerol lipase (DAGL) pathway is the most important 2-AG biosynthetic pathway proposed to date. Lysophosphatidate phosphatase (LPAase) activity is part of another 2-AG-forming pathway in which monoacylglycerol lipase (MAGL) is the major degrading enzyme. The purpose of this study was to analyze the manner in which DAGL, LPAase, and MAGL enzymes are modified in the central nervous system (CNS) during aging. To this end, diacylglycerols (DAGs) and MAGs of different composition were used as substrates of DAGL and MAGL, respectively. All enzymatic activities were evaluated in membrane and soluble fractions as well as in synaptic terminals from the cerebral cortex (CC) of adult and aged rats. Results related to 2-AG metabolism show that aging: (a) decreases DAGL-alfa expression in the membrane fraction whereas in synaptosomes it increases DAGL-beta and decreases MAGL expression; (b) decreases LPAase activity in both membrane and soluble fractions; (c) decreases DAGL and stimulates LPAase activities in CC synaptic terminals; (d) stimulates membrane-associated MAGL-coupled DAGL activity; and (e) stimulates MAGL activity in CC synaptosomes. Our results also reveal that during aging the net balance between the enzymatic activities involved in 2-AG synthesis and breakdown is low availability of 2-AG in CC membrane fractions and synaptic terminals. Taken together, our results lead us to conclude that these enzymes play crucial roles in the regulation of 2-AG tissue levels during aging.Fil: Pascual, Ana Clara. Universidad Nacional del Sur; Argentina. Consejo Nacional de Investigaciones Cientí­ficas y Técnicas. Centro Científico Tecnológico Bahí­a Blanca. Instituto de Investigaciones Bioquímicas Bahí­a Blanca (i); ArgentinaFil: Gaveglio, Virginia Lucía. Universidad Nacional del Sur; Argentina. Consejo Nacional de Investigaciones Cientí­ficas y Técnicas. Centro Científico Tecnológico Bahí­a Blanca. Instituto de Investigaciones Bioquímicas Bahí­a Blanca (i); ArgentinaFil: Giusto, Norma Maria. Universidad Nacional del Sur; Argentina. Consejo Nacional de Investigaciones Cientí­ficas y Técnicas. Centro Científico Tecnológico Bahí­a Blanca. Instituto de Investigaciones Bioquímicas Bahí­a Blanca (i); ArgentinaFil: Pasquaré, Susana Juana. Universidad Nacional del Sur; Argentina. Consejo Nacional de Investigaciones Cientí­ficas y Técnicas. Centro Científico Tecnológico Bahí­a Blanca. Instituto de Investigaciones Bioquímicas Bahí­a Blanca (i); ArgentinaWiley2013-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/4666Pascual, Ana Clara; Gaveglio, Virginia Lucía; Giusto, Norma Maria; Pasquaré, Susana Juana; Aging Modifies the Enzymatic Activities Involved in 2-Arachidonoylglycerol Metabolism; Wiley; Biofactors; 39; 2; 3-2013; 209-2200951-6433enginfo:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/biof.1055/abstractinfo:eu-repo/semantics/altIdentifier/doi/10.1002/biof.1055info:eu-repo/semantics/altIdentifier/issn/0951-6433info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:57:12Zoai:ri.conicet.gov.ar:11336/4666instacron: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:34982025-09-29 09:57:12.68CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Aging Modifies the Enzymatic Activities Involved in 2-Arachidonoylglycerol Metabolism
title Aging Modifies the Enzymatic Activities Involved in 2-Arachidonoylglycerol Metabolism
spellingShingle Aging Modifies the Enzymatic Activities Involved in 2-Arachidonoylglycerol Metabolism
Pascual, Ana Clara
2-Arachidonoylglycerol
Cerebral Cortex
Lysophosphatidic Acid
Synaptosomes
Monoacylglycerol
title_short Aging Modifies the Enzymatic Activities Involved in 2-Arachidonoylglycerol Metabolism
title_full Aging Modifies the Enzymatic Activities Involved in 2-Arachidonoylglycerol Metabolism
title_fullStr Aging Modifies the Enzymatic Activities Involved in 2-Arachidonoylglycerol Metabolism
title_full_unstemmed Aging Modifies the Enzymatic Activities Involved in 2-Arachidonoylglycerol Metabolism
title_sort Aging Modifies the Enzymatic Activities Involved in 2-Arachidonoylglycerol Metabolism
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.subject.none.fl_str_mv 2-Arachidonoylglycerol
Cerebral Cortex
Lysophosphatidic Acid
Synaptosomes
Monoacylglycerol
topic 2-Arachidonoylglycerol
Cerebral Cortex
Lysophosphatidic Acid
Synaptosomes
Monoacylglycerol
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv One of the principal monoacylglycerol (MAG) species in animal tissues is 2-arachidonoylglycerol (2-AG), and the diacylglycerol lipase (DAGL) pathway is the most important 2-AG biosynthetic pathway proposed to date. Lysophosphatidate phosphatase (LPAase) activity is part of another 2-AG-forming pathway in which monoacylglycerol lipase (MAGL) is the major degrading enzyme. The purpose of this study was to analyze the manner in which DAGL, LPAase, and MAGL enzymes are modified in the central nervous system (CNS) during aging. To this end, diacylglycerols (DAGs) and MAGs of different composition were used as substrates of DAGL and MAGL, respectively. All enzymatic activities were evaluated in membrane and soluble fractions as well as in synaptic terminals from the cerebral cortex (CC) of adult and aged rats. Results related to 2-AG metabolism show that aging: (a) decreases DAGL-alfa expression in the membrane fraction whereas in synaptosomes it increases DAGL-beta and decreases MAGL expression; (b) decreases LPAase activity in both membrane and soluble fractions; (c) decreases DAGL and stimulates LPAase activities in CC synaptic terminals; (d) stimulates membrane-associated MAGL-coupled DAGL activity; and (e) stimulates MAGL activity in CC synaptosomes. Our results also reveal that during aging the net balance between the enzymatic activities involved in 2-AG synthesis and breakdown is low availability of 2-AG in CC membrane fractions and synaptic terminals. Taken together, our results lead us to conclude that these enzymes play crucial roles in the regulation of 2-AG tissue levels during aging.
Fil: Pascual, Ana Clara. Universidad Nacional del Sur; Argentina. Consejo Nacional de Investigaciones Cientí­ficas y Técnicas. Centro Científico Tecnológico Bahí­a Blanca. Instituto de Investigaciones Bioquímicas Bahí­a Blanca (i); Argentina
Fil: Gaveglio, Virginia Lucía. Universidad Nacional del Sur; Argentina. Consejo Nacional de Investigaciones Cientí­ficas y Técnicas. Centro Científico Tecnológico Bahí­a Blanca. Instituto de Investigaciones Bioquímicas Bahí­a Blanca (i); Argentina
Fil: Giusto, Norma Maria. Universidad Nacional del Sur; Argentina. Consejo Nacional de Investigaciones Cientí­ficas y Técnicas. Centro Científico Tecnológico Bahí­a Blanca. Instituto de Investigaciones Bioquímicas Bahí­a Blanca (i); Argentina
Fil: Pasquaré, Susana Juana. Universidad Nacional del Sur; Argentina. Consejo Nacional de Investigaciones Cientí­ficas y Técnicas. Centro Científico Tecnológico Bahí­a Blanca. Instituto de Investigaciones Bioquímicas Bahí­a Blanca (i); Argentina
description One of the principal monoacylglycerol (MAG) species in animal tissues is 2-arachidonoylglycerol (2-AG), and the diacylglycerol lipase (DAGL) pathway is the most important 2-AG biosynthetic pathway proposed to date. Lysophosphatidate phosphatase (LPAase) activity is part of another 2-AG-forming pathway in which monoacylglycerol lipase (MAGL) is the major degrading enzyme. The purpose of this study was to analyze the manner in which DAGL, LPAase, and MAGL enzymes are modified in the central nervous system (CNS) during aging. To this end, diacylglycerols (DAGs) and MAGs of different composition were used as substrates of DAGL and MAGL, respectively. All enzymatic activities were evaluated in membrane and soluble fractions as well as in synaptic terminals from the cerebral cortex (CC) of adult and aged rats. Results related to 2-AG metabolism show that aging: (a) decreases DAGL-alfa expression in the membrane fraction whereas in synaptosomes it increases DAGL-beta and decreases MAGL expression; (b) decreases LPAase activity in both membrane and soluble fractions; (c) decreases DAGL and stimulates LPAase activities in CC synaptic terminals; (d) stimulates membrane-associated MAGL-coupled DAGL activity; and (e) stimulates MAGL activity in CC synaptosomes. Our results also reveal that during aging the net balance between the enzymatic activities involved in 2-AG synthesis and breakdown is low availability of 2-AG in CC membrane fractions and synaptic terminals. Taken together, our results lead us to conclude that these enzymes play crucial roles in the regulation of 2-AG tissue levels during aging.
publishDate 2013
dc.date.none.fl_str_mv 2013-03
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/11336/4666
Pascual, Ana Clara; Gaveglio, Virginia Lucía; Giusto, Norma Maria; Pasquaré, Susana Juana; Aging Modifies the Enzymatic Activities Involved in 2-Arachidonoylglycerol Metabolism; Wiley; Biofactors; 39; 2; 3-2013; 209-220
0951-6433
url http://hdl.handle.net/11336/4666
identifier_str_mv Pascual, Ana Clara; Gaveglio, Virginia Lucía; Giusto, Norma Maria; Pasquaré, Susana Juana; Aging Modifies the Enzymatic Activities Involved in 2-Arachidonoylglycerol Metabolism; Wiley; Biofactors; 39; 2; 3-2013; 209-220
0951-6433
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/biof.1055/abstract
info:eu-repo/semantics/altIdentifier/doi/10.1002/biof.1055
info:eu-repo/semantics/altIdentifier/issn/0951-6433
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
publisher.none.fl_str_mv Wiley
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 13.070432

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