A Lipidomic Perspective of the Action of Group IIA Secreted Phospholipase A2 on Human Monocytes: Lipid Droplet Biogenesis and Activation of Cytosolic Phospholipase A2α

Autores
Rodríguez, Juan Pablo; Leiguez, Elbio; Guijas, Carlos; Lomonte, Bruno; Gutiérrez, José M.; Teixeira, Catarina; Balboa, María A.; Balsinde, Jesús
Año de publicación
2020
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Phospholipase A2s constitute a wide group of lipid‐modifying enzymes which display a variety of functions in innate immune responses. In this work, we utilized mass spectrometry‐based lipidomic approaches to investigate the action of Asp‐49 Ca2+‐dependent secreted phospholipase A2 (sPLA2) (MT‐III) and Lys‐49 sPLA2 (MT‐II), two group IIA phospholipase A2s isolated from the venom of the snake Bothrops asper, on human peripheral blood monocytes. MT‐III is catalytically active, whereas MT‐II lacks enzyme activity. A large decrease in the fatty acid content of membrane phospholipids was detected in MT III‐treated monocytes. The significant diminution of the cellular content of phospholipid‐bound arachidonic acid seemed to be mediated, in part, by the activation of the endogenous group IVA cytosolic phospholipase A2α. MT‐III triggered the formation of triacylglycerol and cholesterol enriched in palmitic, stearic, and oleic acids, but not arachidonic acid, along with an increase in lipid droplet synthesis. Additionally, it was shown that the increased availability of arachidonic acid arising from phospholipid hydrolysis promoted abundant eicosanoid synthesis. The inactive form, MT‐II, failed to produce any of the effects described above. These studies provide a complete lipidomic characterization of the monocyte response to snake venom group IIA phospholipase A2, and reveal significant connections among lipid droplet biogenesis, cell signaling and biochemical pathways that contribute to initiating the inflammatory response.
Fil: Rodríguez, Juan Pablo. 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: Leiguez, Elbio. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil. Consejo Superior de Investigaciones Científicas; España
Fil: Guijas, Carlos. Universidad de Valladolid; España. Consejo Superior de Investigaciones Científicas; España
Fil: Lomonte, Bruno. Universidad de Costa Rica; Costa Rica
Fil: Gutiérrez, José M.. Universidad de Costa Rica; Costa Rica
Fil: Teixeira, Catarina. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil
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
INFLAMMATION
LIPID SIGNALING
LIPIDOMICS
MASS SPECTROMETRY
MONOCYTES/MACROPHAGES
PHOSPHOLIPASE A2
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:11336/130757
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/130757
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A Lipidomic Perspective of the Action of Group IIA Secreted Phospholipase A2 on Human Monocytes: Lipid Droplet Biogenesis and Activation of Cytosolic Phospholipase A2αRodríguez, Juan PabloLeiguez, ElbioGuijas, CarlosLomonte, BrunoGutiérrez, José M.Teixeira, CatarinaBalboa, María A.Balsinde, JesúsINFLAMMATIONLIPID SIGNALINGLIPIDOMICSMASS SPECTROMETRYMONOCYTES/MACROPHAGESPHOSPHOLIPASE A2https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Phospholipase A2s constitute a wide group of lipid‐modifying enzymes which display a variety of functions in innate immune responses. In this work, we utilized mass spectrometry‐based lipidomic approaches to investigate the action of Asp‐49 Ca2+‐dependent secreted phospholipase A2 (sPLA2) (MT‐III) and Lys‐49 sPLA2 (MT‐II), two group IIA phospholipase A2s isolated from the venom of the snake Bothrops asper, on human peripheral blood monocytes. MT‐III is catalytically active, whereas MT‐II lacks enzyme activity. A large decrease in the fatty acid content of membrane phospholipids was detected in MT III‐treated monocytes. The significant diminution of the cellular content of phospholipid‐bound arachidonic acid seemed to be mediated, in part, by the activation of the endogenous group IVA cytosolic phospholipase A2α. MT‐III triggered the formation of triacylglycerol and cholesterol enriched in palmitic, stearic, and oleic acids, but not arachidonic acid, along with an increase in lipid droplet synthesis. Additionally, it was shown that the increased availability of arachidonic acid arising from phospholipid hydrolysis promoted abundant eicosanoid synthesis. The inactive form, MT‐II, failed to produce any of the effects described above. These studies provide a complete lipidomic characterization of the monocyte response to snake venom group IIA phospholipase A2, and reveal significant connections among lipid droplet biogenesis, cell signaling and biochemical pathways that contribute to initiating the inflammatory response.Fil: Rodríguez, Juan Pablo. 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: Leiguez, Elbio. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil. Consejo Superior de Investigaciones Científicas; EspañaFil: Guijas, Carlos. Universidad de Valladolid; España. Consejo Superior de Investigaciones Científicas; EspañaFil: Lomonte, Bruno. Universidad de Costa Rica; Costa RicaFil: Gutiérrez, José M.. Universidad de Costa Rica; Costa RicaFil: Teixeira, Catarina. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; BrasilFil: 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 International2020-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/130757Rodríguez, Juan Pablo; Leiguez, Elbio; Guijas, Carlos; Lomonte, Bruno; Gutiérrez, José M.; et al.; A Lipidomic Perspective of the Action of Group IIA Secreted Phospholipase A2 on Human Monocytes: Lipid Droplet Biogenesis and Activation of Cytosolic Phospholipase A2α; Molecular Diversity Preservation International; Biomolecules; 10; 6; 6-2020; 1-202218-273XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2218-273X/10/6/891info:eu-repo/semantics/altIdentifier/doi/10.3390/biom10060891info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:06:35Zoai:ri.conicet.gov.ar:11336/130757instacron: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 10:06:35.562CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A Lipidomic Perspective of the Action of Group IIA Secreted Phospholipase A2 on Human Monocytes: Lipid Droplet Biogenesis and Activation of Cytosolic Phospholipase A2α
title A Lipidomic Perspective of the Action of Group IIA Secreted Phospholipase A2 on Human Monocytes: Lipid Droplet Biogenesis and Activation of Cytosolic Phospholipase A2α
spellingShingle A Lipidomic Perspective of the Action of Group IIA Secreted Phospholipase A2 on Human Monocytes: Lipid Droplet Biogenesis and Activation of Cytosolic Phospholipase A2α
Rodríguez, Juan Pablo
INFLAMMATION
LIPID SIGNALING
LIPIDOMICS
MASS SPECTROMETRY
MONOCYTES/MACROPHAGES
PHOSPHOLIPASE A2
title_short A Lipidomic Perspective of the Action of Group IIA Secreted Phospholipase A2 on Human Monocytes: Lipid Droplet Biogenesis and Activation of Cytosolic Phospholipase A2α
title_full A Lipidomic Perspective of the Action of Group IIA Secreted Phospholipase A2 on Human Monocytes: Lipid Droplet Biogenesis and Activation of Cytosolic Phospholipase A2α
title_fullStr A Lipidomic Perspective of the Action of Group IIA Secreted Phospholipase A2 on Human Monocytes: Lipid Droplet Biogenesis and Activation of Cytosolic Phospholipase A2α
title_full_unstemmed A Lipidomic Perspective of the Action of Group IIA Secreted Phospholipase A2 on Human Monocytes: Lipid Droplet Biogenesis and Activation of Cytosolic Phospholipase A2α
title_sort A Lipidomic Perspective of the Action of Group IIA Secreted Phospholipase A2 on Human Monocytes: Lipid Droplet Biogenesis and Activation of Cytosolic Phospholipase A2α
dc.creator.none.fl_str_mv Rodríguez, Juan Pablo
Leiguez, Elbio
Guijas, Carlos
Lomonte, Bruno
Gutiérrez, José M.
Teixeira, Catarina
Balboa, María A.
Balsinde, Jesús
author Rodríguez, Juan Pablo
author_facet Rodríguez, Juan Pablo
Leiguez, Elbio
Guijas, Carlos
Lomonte, Bruno
Gutiérrez, José M.
Teixeira, Catarina
Balboa, María A.
Balsinde, Jesús
author_role author
author2 Leiguez, Elbio
Guijas, Carlos
Lomonte, Bruno
Gutiérrez, José M.
Teixeira, Catarina
Balboa, María A.
Balsinde, Jesús
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv INFLAMMATION
LIPID SIGNALING
LIPIDOMICS
MASS SPECTROMETRY
MONOCYTES/MACROPHAGES
PHOSPHOLIPASE A2
topic INFLAMMATION
LIPID SIGNALING
LIPIDOMICS
MASS SPECTROMETRY
MONOCYTES/MACROPHAGES
PHOSPHOLIPASE A2
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Phospholipase A2s constitute a wide group of lipid‐modifying enzymes which display a variety of functions in innate immune responses. In this work, we utilized mass spectrometry‐based lipidomic approaches to investigate the action of Asp‐49 Ca2+‐dependent secreted phospholipase A2 (sPLA2) (MT‐III) and Lys‐49 sPLA2 (MT‐II), two group IIA phospholipase A2s isolated from the venom of the snake Bothrops asper, on human peripheral blood monocytes. MT‐III is catalytically active, whereas MT‐II lacks enzyme activity. A large decrease in the fatty acid content of membrane phospholipids was detected in MT III‐treated monocytes. The significant diminution of the cellular content of phospholipid‐bound arachidonic acid seemed to be mediated, in part, by the activation of the endogenous group IVA cytosolic phospholipase A2α. MT‐III triggered the formation of triacylglycerol and cholesterol enriched in palmitic, stearic, and oleic acids, but not arachidonic acid, along with an increase in lipid droplet synthesis. Additionally, it was shown that the increased availability of arachidonic acid arising from phospholipid hydrolysis promoted abundant eicosanoid synthesis. The inactive form, MT‐II, failed to produce any of the effects described above. These studies provide a complete lipidomic characterization of the monocyte response to snake venom group IIA phospholipase A2, and reveal significant connections among lipid droplet biogenesis, cell signaling and biochemical pathways that contribute to initiating the inflammatory response.
Fil: Rodríguez, Juan Pablo. 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: Leiguez, Elbio. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil. Consejo Superior de Investigaciones Científicas; España
Fil: Guijas, Carlos. Universidad de Valladolid; España. Consejo Superior de Investigaciones Científicas; España
Fil: Lomonte, Bruno. Universidad de Costa Rica; Costa Rica
Fil: Gutiérrez, José M.. Universidad de Costa Rica; Costa Rica
Fil: Teixeira, Catarina. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil
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 Phospholipase A2s constitute a wide group of lipid‐modifying enzymes which display a variety of functions in innate immune responses. In this work, we utilized mass spectrometry‐based lipidomic approaches to investigate the action of Asp‐49 Ca2+‐dependent secreted phospholipase A2 (sPLA2) (MT‐III) and Lys‐49 sPLA2 (MT‐II), two group IIA phospholipase A2s isolated from the venom of the snake Bothrops asper, on human peripheral blood monocytes. MT‐III is catalytically active, whereas MT‐II lacks enzyme activity. A large decrease in the fatty acid content of membrane phospholipids was detected in MT III‐treated monocytes. The significant diminution of the cellular content of phospholipid‐bound arachidonic acid seemed to be mediated, in part, by the activation of the endogenous group IVA cytosolic phospholipase A2α. MT‐III triggered the formation of triacylglycerol and cholesterol enriched in palmitic, stearic, and oleic acids, but not arachidonic acid, along with an increase in lipid droplet synthesis. Additionally, it was shown that the increased availability of arachidonic acid arising from phospholipid hydrolysis promoted abundant eicosanoid synthesis. The inactive form, MT‐II, failed to produce any of the effects described above. These studies provide a complete lipidomic characterization of the monocyte response to snake venom group IIA phospholipase A2, and reveal significant connections among lipid droplet biogenesis, cell signaling and biochemical pathways that contribute to initiating the inflammatory response.
publishDate 2020
dc.date.none.fl_str_mv 2020-06
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/11336/130757
Rodríguez, Juan Pablo; Leiguez, Elbio; Guijas, Carlos; Lomonte, Bruno; Gutiérrez, José M.; et al.; A Lipidomic Perspective of the Action of Group IIA Secreted Phospholipase A2 on Human Monocytes: Lipid Droplet Biogenesis and Activation of Cytosolic Phospholipase A2α; Molecular Diversity Preservation International; Biomolecules; 10; 6; 6-2020; 1-20
2218-273X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/130757
identifier_str_mv Rodríguez, Juan Pablo; Leiguez, Elbio; Guijas, Carlos; Lomonte, Bruno; Gutiérrez, José M.; et al.; A Lipidomic Perspective of the Action of Group IIA Secreted Phospholipase A2 on Human Monocytes: Lipid Droplet Biogenesis and Activation of Cytosolic Phospholipase A2α; Molecular Diversity Preservation International; Biomolecules; 10; 6; 6-2020; 1-20
2218-273X
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.mdpi.com/2218-273X/10/6/891
info:eu-repo/semantics/altIdentifier/doi/10.3390/biom10060891
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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score 13.13397

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