Evidence map›Paper›PMID 35460054›Full record

ArticleMolecular neurobiology2022

The Neuroprotective Lipocalin Apolipoprotein D Stably Interacts with Specific Subtypes of Detergent-Resistant Membrane Domains in a Basigin-Independent Manner.

Miriam Corraliza-Gomez, Manuela Del Caño-Espinel, Diego Sanchez, Maria D Ganfornina

Open access · hybridAbstract read
In one paragraph

Article in Molecular neurobiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 30% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Apolipoprotein D in Oxidative Stress and Inflammation.Antioxidants (Basel, Switzerland) · 2023
    Review
  5. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Miriam Corraliza-GomezInstituto de Biología y Genética Molecular, Unidad de Excelencia, Universidad de Valladolid-CSIC, 47003, Valladolid, Spain.ORCID http://orcid.org/0000-0002-1417-2757
Manuela Del Caño-EspinelInstituto de Biología y Genética Molecular, Unidad de Excelencia, Universidad de Valladolid-CSIC, 47003, Valladolid, Spain.ORCID http://orcid.org/0000-0001-5736-3556
Diego SanchezInstituto de Biología y Genética Molecular, Unidad de Excelencia, Universidad de Valladolid-CSIC, 47003, Valladolid, Spain.ORCID http://orcid.org/0000-0001-6296-6773
Maria D GanforninaInstituto de Biología y Genética Molecular, Unidad de Excelencia, Universidad de Valladolid-CSIC, 47003, Valladolid, Spain. opabinia@ibgm.uva.es.ORCID http://orcid.org/0000-0002-8567-4826
Universidad de Valladolid · ES

Funding

Ministerio de Ciencia, Innovación y Universidades BFU2015-68149-RMinisterio de Ciencia, Innovación y Universidades PID2019-110911RB-I00
6 · The paper itself

Abstract

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.

Indexed as

BasiginDetergentsAntioxidantsApolipoproteins DLipocalinsMembrane MicrodomainsAntioxidantsApolipoproteins DBasiginDetergentsLipocalinsEndocytosisLipid peroxidationLipid raftsLysosomeNeuroprotectionPlasma membrane

Identifiers

PMID35460054
PMCPMC9167181
OpenAlexW4224267486

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.