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dc.contributor.authorCorraliza Gómez, Miriam
dc.contributor.authorCaño Espinel, Manuela del
dc.contributor.authorSánchez, Diego
dc.contributor.authorGanfornina, María D.
dc.date.accessioned2023-12-13T17:05:53Z
dc.date.available2023-12-13T17:05:53Z
dc.date.issued2022
dc.identifier.issn0893-7648
dc.identifier.urihttp://hdl.handle.net/10259/8202
dc.description.abstractAccumulated evidence points to the lipocalin apolipoprotein D (ApoD), one of the few genes consistently upregulated upon brain ageing and neurodegeneration, as an endogenous controller of the redox state of cellular and extracellular lipid structures. This biochemical function has downstream consequences as apparently varied as control of glycocalyx and myelin compaction, cell viability upon oxidative stress or modulation of signalling pathways. In spite of this knowledge, it is still unclear if ApoD function requires canonical receptor-mediated transductions systems. This work aims to examine ApoD-cell membrane interaction and its dependence on a proposed ApoD receptor, Basigin. Whole and fractionated membrane preparations from the brain, primary astrocytes, glial and neuronal cell lines, reveal ApoD as a very specific component of particular subtypes of detergent-resistant microdomains (DRMs). ApoD interacts in vitro with neuronal membranes and is stably associated with astrocytic membranes. ApoD associates with DRMs with specific buoyancy properties that co-fractionate with plasma or late-endosome-lysosome markers. A mass spectrometry analysis reveals that these Triton X-114 DRMs contain both plasma membrane and endosomal-lysosomal compartment lipid raft proteins. ApoD-DRM association is maintained under metabolic and acute oxidative stress conditions. However, ApoD-membrane interaction, its internalization and its lipid-antioxidant function do not require the presence of Basigin. This work supports a stable association of ApoD with membranes, independent of Basigin, and provides the basis to fully understand ApoD antioxidant neuroprotective mechanism as a mechanism taking place in specific membrane subdomains.en
dc.description.sponsorshipOpen Access funding provided thanks to the CRUE-CSIC agreement with Springer Nature. This work was supported by Ministerio de Ciencia e Innovacion grants BFU2015-68149-R and PID2019-110911RB-I00 to M.D.G. and D.S.en
dc.format.mimetypeapplication/pdf
dc.language.isoenges
dc.publisherSpringeres
dc.relation.ispartofMolecular Neurobiology. 2022, V. 59, n. 7, p. 4015-4029es
dc.rightsAtribución 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectNeuroprotectionen
dc.subjectLipid raftsen
dc.subjectPlasma membraneen
dc.subjectLysosomeen
dc.subjectLipid peroxidationen
dc.subjectEndocytosisen
dc.subject.otherQuímicaes
dc.subject.otherChemistryen
dc.subject.otherBiología moleculares
dc.subject.otherMolecular biologyen
dc.titleThe Neuroprotective Lipocalin Apolipoprotein D Stably Interacts with Specific Subtypes of Detergent-Resistant Membrane Domains in a Basigin-Independent Manneren
dc.typeinfo:eu-repo/semantics/articlees
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses
dc.relation.publisherversionhttps://doi.org/10.1007/S12035-022-02829-Zes
dc.identifier.doi10.1007/S12035-022-02829-Z
dc.identifier.essn1559-1182
dc.journal.titleMolecular Neurobiologyes
dc.volume.number59es
dc.issue.number7es
dc.page.initial4015es
dc.page.final4029es
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersiones


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