Selectivity of phospholipid hydrolysis by phospholipase A2 enzymes in activated cells leading to polyunsaturated fatty acid mobilization

Phospholipase A2s are enzymes that hydrolyze the fatty acid at the sn-2 position of the glycerol backbone of membrane glycerophospholipids. Given the asymmetric distribution of fatty acids within phospholipids, where saturated fatty acids tend to be present at the sn-1 position, and polyunsaturated...

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Autores: Astudillo, Alma M., Balboa, María A., Balsinde, Jesús
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2019
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/196503
Acceso en línea:http://hdl.handle.net/10261/196503
Access Level:acceso abierto
Palabra clave:Phospholipase A2
Lipid mediator
Glycerophospholipid
Arachidonic acid
Docosahexaenoic acid
Transacylase
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spelling Selectivity of phospholipid hydrolysis by phospholipase A2 enzymes in activated cells leading to polyunsaturated fatty acid mobilizationAstudillo, Alma M.Balboa, María A.Balsinde, JesúsPhospholipase A2Lipid mediatorGlycerophospholipidArachidonic acidDocosahexaenoic acidTransacylasePhospholipase A2s are enzymes that hydrolyze the fatty acid at the sn-2 position of the glycerol backbone of membrane glycerophospholipids. Given the asymmetric distribution of fatty acids within phospholipids, where saturated fatty acids tend to be present at the sn-1 position, and polyunsaturated fatty acids such as those of the omega-3 and omega-6 series overwhelmingly localize in the sn-2 position, the phospholipase A2 reaction is of utmost importance as a regulatory checkpoint for the mobilization of these fatty acids and the subsequent synthesis of proinflammatory omega-6-derived eicosanoids on one hand, and omega-3-derived specialized pro-resolving mediators on the other. The great variety of phospholipase A2s, their differential substrate selectivity under a variety of pathophysiological conditions, as well as the different compartmentalization of each enzyme and accessibility to substrate, render this class of enzymes also key to membrane phospholipid remodeling reactions, and the generation of specific lipid mediators not related with canonical metabolites of omega-6 or omega-3 fatty acids. This review highlights novel findings regarding the selective hydrolysis of phospholipids by phospholipase A2s and the influence this may have on the ability of these enzymes to generate distinct lipid mediators with essential functions in biological processes. This brings a new understanding of the cellular roles of these enzymes depending upon activation conditions.Work in the authors' laboratory was supported by Grants SAF2016-80883-R and SAF2015-73000-EXP from the Spanish Ministry of Economy, Industry and Competitiveness, and Grant CSI073U16 from the Education Department of the Regional Government of Castile and Leon. CIBERDEM is an initiative of Instituto de Salud Carlos III.Peer reviewedElsevierMinisterio de Economía, Industria y Competitividad (España)Ministerio de Economía y Competitividad (España)Junta de Castilla y LeónInstituto de Salud Carlos IIIConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]201920192019info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/196503reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/SAF2016-80883-Rinfo:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/SAF2015-73000-EXPhttps://doi.org/10.1016/j.bbalip.2018.07.002Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1965032026-05-22T06:33:51Z
dc.title.none.fl_str_mv Selectivity of phospholipid hydrolysis by phospholipase A2 enzymes in activated cells leading to polyunsaturated fatty acid mobilization
title Selectivity of phospholipid hydrolysis by phospholipase A2 enzymes in activated cells leading to polyunsaturated fatty acid mobilization
spellingShingle Selectivity of phospholipid hydrolysis by phospholipase A2 enzymes in activated cells leading to polyunsaturated fatty acid mobilization
Astudillo, Alma M.
Phospholipase A2
Lipid mediator
Glycerophospholipid
Arachidonic acid
Docosahexaenoic acid
Transacylase
title_short Selectivity of phospholipid hydrolysis by phospholipase A2 enzymes in activated cells leading to polyunsaturated fatty acid mobilization
title_full Selectivity of phospholipid hydrolysis by phospholipase A2 enzymes in activated cells leading to polyunsaturated fatty acid mobilization
title_fullStr Selectivity of phospholipid hydrolysis by phospholipase A2 enzymes in activated cells leading to polyunsaturated fatty acid mobilization
title_full_unstemmed Selectivity of phospholipid hydrolysis by phospholipase A2 enzymes in activated cells leading to polyunsaturated fatty acid mobilization
title_sort Selectivity of phospholipid hydrolysis by phospholipase A2 enzymes in activated cells leading to polyunsaturated fatty acid mobilization
dc.creator.none.fl_str_mv Astudillo, Alma M.
Balboa, María A.
Balsinde, Jesús
author Astudillo, Alma M.
author_facet Astudillo, Alma M.
Balboa, María A.
Balsinde, Jesús
author_role author
author2 Balboa, María A.
Balsinde, Jesús
author2_role author
author
dc.contributor.none.fl_str_mv Ministerio de Economía, Industria y Competitividad (España)
Ministerio de Economía y Competitividad (España)
Junta de Castilla y León
Instituto de Salud Carlos III
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Phospholipase A2
Lipid mediator
Glycerophospholipid
Arachidonic acid
Docosahexaenoic acid
Transacylase
topic Phospholipase A2
Lipid mediator
Glycerophospholipid
Arachidonic acid
Docosahexaenoic acid
Transacylase
description Phospholipase A2s are enzymes that hydrolyze the fatty acid at the sn-2 position of the glycerol backbone of membrane glycerophospholipids. Given the asymmetric distribution of fatty acids within phospholipids, where saturated fatty acids tend to be present at the sn-1 position, and polyunsaturated fatty acids such as those of the omega-3 and omega-6 series overwhelmingly localize in the sn-2 position, the phospholipase A2 reaction is of utmost importance as a regulatory checkpoint for the mobilization of these fatty acids and the subsequent synthesis of proinflammatory omega-6-derived eicosanoids on one hand, and omega-3-derived specialized pro-resolving mediators on the other. The great variety of phospholipase A2s, their differential substrate selectivity under a variety of pathophysiological conditions, as well as the different compartmentalization of each enzyme and accessibility to substrate, render this class of enzymes also key to membrane phospholipid remodeling reactions, and the generation of specific lipid mediators not related with canonical metabolites of omega-6 or omega-3 fatty acids. This review highlights novel findings regarding the selective hydrolysis of phospholipids by phospholipase A2s and the influence this may have on the ability of these enzymes to generate distinct lipid mediators with essential functions in biological processes. This brings a new understanding of the cellular roles of these enzymes depending upon activation conditions.
publishDate 2019
dc.date.none.fl_str_mv 2019
2019
2019
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Postprint
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/196503
url http://hdl.handle.net/10261/196503
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/SAF2016-80883-R
info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/SAF2015-73000-EXP
https://doi.org/10.1016/j.bbalip.2018.07.002
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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