Phospholipid arachidonic acid remodeling during phagocytosis in mouse peritoneal macrophages

Autores
Gil de Gómez, Luis; Monge, Patricia; Rodríguez, Juan Pablo; Astudillo, Alma M.; Balboa, María A.; Balsinde, Jesús
Año de publicación
2020
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Macrophages contain large amounts of arachidonic acid (AA), which distributes differentially across membrane phospholipids. This is largely due to the action of coenzyme A-independent transacylase (CoA-IT), which transfers theAAprimarily fromdiacyl choline-containing phospholipids to ethanolamine-containing phospholipids. In this work we have comparatively analyzed glycerophospholipid changes leading to AA mobilization in mouse peritoneal macrophages responding to either zymosan or serum-opsonized zymosan (OpZ). These two phagocytic stimuli promote the cytosolic phospholipase A2-dependent mobilization of AA by activating distinct surface receptors. Application of mass spectrometry-based lipid profiling to identify changes in AA-containing phospholipids during macrophage exposure to both stimuli revealed significant decreases in the levels of all major choline phospholipid molecular species and a major phosphatidylinositol species. Importantly, while no changes in ethanolamine phospholipid species were detected on stimulation with zymosan, significant decreases in these species were observed when OpZ was used. Analyses of CoA-IT-mediated AA remodeling revealed that the process occurred faster in the zymosan-stimulated cells compared with OpZ-stimulated cells. Pharmacological inhibition of CoA-IT strongly blunted AA release in response to zymosan but had only a moderate effect on the OpZ-mediated response. These results suggest a hitherto undescribed receptor-dependent role for CoA-independent AA remodeling reactions in modulating the eicosanoid biosynthetic response of macrophages. Our data help define novel targets within the AA remodeling pathway with potential use to control lipid mediator formation.
Fil: Gil de Gómez, Luis. Universidad de Valladolid; España. Consejo Superior de Investigaciones Científicas; España
Fil: Monge, Patricia. Universidad de Valladolid; España. Consejo Superior de Investigaciones Científicas; España
Fil: Rodríguez, Juan Pablo. Universidad de Valladolid; España. Consejo Superior de Investigaciones Científicas; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; Argentina
Fil: Astudillo, Alma M.. Universidad de Valladolid; España. Consejo Superior de Investigaciones Científicas; España
Fil: Balboa, María A.. Consejo Superior de Investigaciones Científicas; España. Universidad de Valladolid; España
Fil: Balsinde, Jesús. Universidad de Valladolid; España. Consejo Superior de Investigaciones Científicas; España
Materia
ARACHIDONIC ACID
EICOSANOIDS
INFLAMMATION
MONOCYTES/MACROPHAGES
PHOSPHOLIPASEA2
PHOSPHOLIPID REMODELING
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:11336/132728

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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Phospholipid arachidonic acid remodeling during phagocytosis in mouse peritoneal macrophagesGil de Gómez, LuisMonge, PatriciaRodríguez, Juan PabloAstudillo, Alma M.Balboa, María A.Balsinde, JesúsARACHIDONIC ACIDEICOSANOIDSINFLAMMATIONMONOCYTES/MACROPHAGESPHOSPHOLIPASEA2PHOSPHOLIPID REMODELINGhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Macrophages contain large amounts of arachidonic acid (AA), which distributes differentially across membrane phospholipids. This is largely due to the action of coenzyme A-independent transacylase (CoA-IT), which transfers theAAprimarily fromdiacyl choline-containing phospholipids to ethanolamine-containing phospholipids. In this work we have comparatively analyzed glycerophospholipid changes leading to AA mobilization in mouse peritoneal macrophages responding to either zymosan or serum-opsonized zymosan (OpZ). These two phagocytic stimuli promote the cytosolic phospholipase A2-dependent mobilization of AA by activating distinct surface receptors. Application of mass spectrometry-based lipid profiling to identify changes in AA-containing phospholipids during macrophage exposure to both stimuli revealed significant decreases in the levels of all major choline phospholipid molecular species and a major phosphatidylinositol species. Importantly, while no changes in ethanolamine phospholipid species were detected on stimulation with zymosan, significant decreases in these species were observed when OpZ was used. Analyses of CoA-IT-mediated AA remodeling revealed that the process occurred faster in the zymosan-stimulated cells compared with OpZ-stimulated cells. Pharmacological inhibition of CoA-IT strongly blunted AA release in response to zymosan but had only a moderate effect on the OpZ-mediated response. These results suggest a hitherto undescribed receptor-dependent role for CoA-independent AA remodeling reactions in modulating the eicosanoid biosynthetic response of macrophages. Our data help define novel targets within the AA remodeling pathway with potential use to control lipid mediator formation.Fil: Gil de Gómez, Luis. Universidad de Valladolid; España. Consejo Superior de Investigaciones Científicas; EspañaFil: Monge, Patricia. Universidad de Valladolid; España. Consejo Superior de Investigaciones Científicas; EspañaFil: Rodríguez, Juan Pablo. Universidad de Valladolid; España. Consejo Superior de Investigaciones Científicas; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; ArgentinaFil: Astudillo, Alma M.. Universidad de Valladolid; España. Consejo Superior de Investigaciones Científicas; EspañaFil: Balboa, María A.. Consejo Superior de Investigaciones Científicas; España. Universidad de Valladolid; EspañaFil: Balsinde, Jesús. Universidad de Valladolid; España. Consejo Superior de Investigaciones Científicas; EspañaMolecular Diversity Preservation International2020-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/132728Gil de Gómez, Luis; Monge, Patricia; Rodríguez, Juan Pablo; Astudillo, Alma M.; Balboa, María A.; et al.; Phospholipid arachidonic acid remodeling during phagocytosis in mouse peritoneal macrophages; Molecular Diversity Preservation International; Biomedicines; 8; 8; 8-2020; 1-172227-9059CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.3390/BIOMEDICINES8080274info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2227-9059/8/8/274info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:43:23Zoai:ri.conicet.gov.ar:11336/132728instacron: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:34982025-09-03 09:43:23.28CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Phospholipid arachidonic acid remodeling during phagocytosis in mouse peritoneal macrophages
title Phospholipid arachidonic acid remodeling during phagocytosis in mouse peritoneal macrophages
spellingShingle Phospholipid arachidonic acid remodeling during phagocytosis in mouse peritoneal macrophages
Gil de Gómez, Luis
ARACHIDONIC ACID
EICOSANOIDS
INFLAMMATION
MONOCYTES/MACROPHAGES
PHOSPHOLIPASEA2
PHOSPHOLIPID REMODELING
title_short Phospholipid arachidonic acid remodeling during phagocytosis in mouse peritoneal macrophages
title_full Phospholipid arachidonic acid remodeling during phagocytosis in mouse peritoneal macrophages
title_fullStr Phospholipid arachidonic acid remodeling during phagocytosis in mouse peritoneal macrophages
title_full_unstemmed Phospholipid arachidonic acid remodeling during phagocytosis in mouse peritoneal macrophages
title_sort Phospholipid arachidonic acid remodeling during phagocytosis in mouse peritoneal macrophages
dc.creator.none.fl_str_mv Gil de Gómez, Luis
Monge, Patricia
Rodríguez, Juan Pablo
Astudillo, Alma M.
Balboa, María A.
Balsinde, Jesús
author Gil de Gómez, Luis
author_facet Gil de Gómez, Luis
Monge, Patricia
Rodríguez, Juan Pablo
Astudillo, Alma M.
Balboa, María A.
Balsinde, Jesús
author_role author
author2 Monge, Patricia
Rodríguez, Juan Pablo
Astudillo, Alma M.
Balboa, María A.
Balsinde, Jesús
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv ARACHIDONIC ACID
EICOSANOIDS
INFLAMMATION
MONOCYTES/MACROPHAGES
PHOSPHOLIPASEA2
PHOSPHOLIPID REMODELING
topic ARACHIDONIC ACID
EICOSANOIDS
INFLAMMATION
MONOCYTES/MACROPHAGES
PHOSPHOLIPASEA2
PHOSPHOLIPID REMODELING
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Macrophages contain large amounts of arachidonic acid (AA), which distributes differentially across membrane phospholipids. This is largely due to the action of coenzyme A-independent transacylase (CoA-IT), which transfers theAAprimarily fromdiacyl choline-containing phospholipids to ethanolamine-containing phospholipids. In this work we have comparatively analyzed glycerophospholipid changes leading to AA mobilization in mouse peritoneal macrophages responding to either zymosan or serum-opsonized zymosan (OpZ). These two phagocytic stimuli promote the cytosolic phospholipase A2-dependent mobilization of AA by activating distinct surface receptors. Application of mass spectrometry-based lipid profiling to identify changes in AA-containing phospholipids during macrophage exposure to both stimuli revealed significant decreases in the levels of all major choline phospholipid molecular species and a major phosphatidylinositol species. Importantly, while no changes in ethanolamine phospholipid species were detected on stimulation with zymosan, significant decreases in these species were observed when OpZ was used. Analyses of CoA-IT-mediated AA remodeling revealed that the process occurred faster in the zymosan-stimulated cells compared with OpZ-stimulated cells. Pharmacological inhibition of CoA-IT strongly blunted AA release in response to zymosan but had only a moderate effect on the OpZ-mediated response. These results suggest a hitherto undescribed receptor-dependent role for CoA-independent AA remodeling reactions in modulating the eicosanoid biosynthetic response of macrophages. Our data help define novel targets within the AA remodeling pathway with potential use to control lipid mediator formation.
Fil: Gil de Gómez, Luis. Universidad de Valladolid; España. Consejo Superior de Investigaciones Científicas; España
Fil: Monge, Patricia. Universidad de Valladolid; España. Consejo Superior de Investigaciones Científicas; España
Fil: Rodríguez, Juan Pablo. Universidad de Valladolid; España. Consejo Superior de Investigaciones Científicas; España. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; Argentina
Fil: Astudillo, Alma M.. Universidad de Valladolid; España. Consejo Superior de Investigaciones Científicas; España
Fil: Balboa, María A.. Consejo Superior de Investigaciones Científicas; España. Universidad de Valladolid; España
Fil: Balsinde, Jesús. Universidad de Valladolid; España. Consejo Superior de Investigaciones Científicas; España
description Macrophages contain large amounts of arachidonic acid (AA), which distributes differentially across membrane phospholipids. This is largely due to the action of coenzyme A-independent transacylase (CoA-IT), which transfers theAAprimarily fromdiacyl choline-containing phospholipids to ethanolamine-containing phospholipids. In this work we have comparatively analyzed glycerophospholipid changes leading to AA mobilization in mouse peritoneal macrophages responding to either zymosan or serum-opsonized zymosan (OpZ). These two phagocytic stimuli promote the cytosolic phospholipase A2-dependent mobilization of AA by activating distinct surface receptors. Application of mass spectrometry-based lipid profiling to identify changes in AA-containing phospholipids during macrophage exposure to both stimuli revealed significant decreases in the levels of all major choline phospholipid molecular species and a major phosphatidylinositol species. Importantly, while no changes in ethanolamine phospholipid species were detected on stimulation with zymosan, significant decreases in these species were observed when OpZ was used. Analyses of CoA-IT-mediated AA remodeling revealed that the process occurred faster in the zymosan-stimulated cells compared with OpZ-stimulated cells. Pharmacological inhibition of CoA-IT strongly blunted AA release in response to zymosan but had only a moderate effect on the OpZ-mediated response. These results suggest a hitherto undescribed receptor-dependent role for CoA-independent AA remodeling reactions in modulating the eicosanoid biosynthetic response of macrophages. Our data help define novel targets within the AA remodeling pathway with potential use to control lipid mediator formation.
publishDate 2020
dc.date.none.fl_str_mv 2020-08
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/11336/132728
Gil de Gómez, Luis; Monge, Patricia; Rodríguez, Juan Pablo; Astudillo, Alma M.; Balboa, María A.; et al.; Phospholipid arachidonic acid remodeling during phagocytosis in mouse peritoneal macrophages; Molecular Diversity Preservation International; Biomedicines; 8; 8; 8-2020; 1-17
2227-9059
CONICET Digital
CONICET
url http://hdl.handle.net/11336/132728
identifier_str_mv Gil de Gómez, Luis; Monge, Patricia; Rodríguez, Juan Pablo; Astudillo, Alma M.; Balboa, María A.; et al.; Phospholipid arachidonic acid remodeling during phagocytosis in mouse peritoneal macrophages; Molecular Diversity Preservation International; Biomedicines; 8; 8; 8-2020; 1-17
2227-9059
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.3390/BIOMEDICINES8080274
info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2227-9059/8/8/274
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 Molecular Diversity Preservation International
publisher.none.fl_str_mv Molecular Diversity Preservation International
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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