RT info:eu-repo/semantics/article
T1 The Neuroprotective Lipocalin Apolipoprotein D Stably Interacts with Specific Subtypes of Detergent-Resistant Membrane Domains in a Basigin-Independent Manner
A1 Corraliza Gómez, Miriam
A1 Caño Espinel, Manuela del
A1 Sánchez, Diego
A1 Ganfornina, María D.
K1 Neuroprotection
K1 Lipid rafts
K1 Plasma membrane
K1 Lysosome
K1 Lipid peroxidation
K1 Endocytosis
K1 Química
K1 Chemistry
K1 Biología molecular
K1 Molecular biology
AB Accumulated 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.
PB Springer
SN 0893-7648
YR 2022
FD 2022
LK http://hdl.handle.net/10259/8202
UL http://hdl.handle.net/10259/8202
LA eng
NO Open 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.
DS Repositorio Institucional de la Universidad de Burgos
RD 23-nov-2024