Evidence map›Paper›PMID 41345709›Full record

ArticleTranslational neurodegeneration2025

Stratification of brain-derived extracellular vesicles of Alzheimer's disease patients indicates a unique proteomic content and a higher seeding capacity of small extracellular vesicles.

Marie Oosterlynck, Elodie Leroux, Balasubramaniam Namasivayam, Thomas Bouillet, Raphaelle Caillierez, Anne Loyens, Daniele Mazur, Romain Perbet, Christophe Lefebvre, Soulaimane Aboulouard and 4 more

Abstract read
In one paragraph

Article in Translational neurodegeneration, 2025. 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
–field-weighted citation impact
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.

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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

14 authors.

Marie Oosterlynck *Inserm UMR-S 1172, 'Alzheimer & Tauopathies', CHU-Lille, Lille Neuroscience & Cognition, Faculty of Medecine - pole recherche, University of Lille, Bâtiment Biserte, Rue Polonovski, 59000, Lille, France.
Elodie Leroux *Inserm UMR-S 1172, 'Alzheimer & Tauopathies', CHU-Lille, Lille Neuroscience & Cognition, Faculty of Medecine - pole recherche, University of Lille, Bâtiment Biserte, Rue Polonovski, 59000, Lille, France.
Balasubramaniam NamasivayamInserm UMR-S 1172, 'Alzheimer & Tauopathies', CHU-Lille, Lille Neuroscience & Cognition, Faculty of Medecine - pole recherche, University of Lille, Bâtiment Biserte, Rue Polonovski, 59000, Lille, France.
Thomas BouilletInserm UMR-S 1172, 'Alzheimer & Tauopathies', CHU-Lille, Lille Neuroscience & Cognition, Faculty of Medecine - pole recherche, University of Lille, Bâtiment Biserte, Rue Polonovski, 59000, Lille, France.
Raphaelle CaillierezInserm UMR-S 1172, 'Alzheimer & Tauopathies', CHU-Lille, Lille Neuroscience & Cognition, Faculty of Medecine - pole recherche, University of Lille, Bâtiment Biserte, Rue Polonovski, 59000, Lille, France.
Anne LoyensInserm UMR-S 1172, 'Alzheimer & Tauopathies', CHU-Lille, Lille Neuroscience & Cognition, Faculty of Medecine - pole recherche, University of Lille, Bâtiment Biserte, Rue Polonovski, 59000, Lille, France.
Daniele MazurInserm UMR-S 1172, 'Alzheimer & Tauopathies', CHU-Lille, Lille Neuroscience & Cognition, Faculty of Medecine - pole recherche, University of Lille, Bâtiment Biserte, Rue Polonovski, 59000, Lille, France.
Romain PerbetInserm UMR-S 1172, 'Alzheimer & Tauopathies', CHU-Lille, Lille Neuroscience & Cognition, Faculty of Medecine - pole recherche, University of Lille, Bâtiment Biserte, Rue Polonovski, 59000, Lille, France.
Christophe LefebvreInserm, U1192-Laboratoire Protéomique, Réponse Inflammatoire Et Spectrométrie de Masse (PRISM), University of Lille, Lille, France.
Soulaimane AboulouardInserm, U1192-Laboratoire Protéomique, Réponse Inflammatoire Et Spectrométrie de Masse (PRISM), University of Lille, Lille, France.
Claude-Alain MaurageCHU-Lille, CRB/CIC1403, Centre de Ressources Biologiques du Centre d'Investigation Clinique, University of Lille, Lille, France.
Bertrand AccartCHU-Lille, CRB/CIC1403, Centre de Ressources Biologiques du Centre d'Investigation Clinique, University of Lille, Lille, France.
Luc BuéeInserm UMR-S 1172, 'Alzheimer & Tauopathies', CHU-Lille, Lille Neuroscience & Cognition, Faculty of Medecine - pole recherche, University of Lille, Bâtiment Biserte, Rue Polonovski, 59000, Lille, France. luc.buee@inserm.fr.ORCID http://orcid.org/0000-0002-6261-4230
Morvane ColinInserm UMR-S 1172, 'Alzheimer & Tauopathies', CHU-Lille, Lille Neuroscience & Cognition, Faculty of Medecine - pole recherche, University of Lille, Bâtiment Biserte, Rue Polonovski, 59000, Lille, France. morvane.colin@inserm.fr.ORCID http://orcid.org/0000-0003-0611-4167

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAlzheimer's disease (AD) is the most prominent form of dementia worldwide. It is characterized by tau lesions that spread throughout the brain in a spatio-temporal manner. This has led to the prion-like propagation hypothesis implicating a transfer of pathological tau seeds from cell to cell. Human brain-derived extracellular vesicles (BD-EVs) isolated from the brain-derived fluid of AD patients contain seeds that contribute to this tau pathology spreading. Knowing the rich diversity of EVs, isolation of functional EV sub-populations is required to unravel their implication in the pathophysiology of AD.

methodsHere, enriched-small EVs (eSEVs) and enriched-large EVs (eLEVs) were isolated from frozen tissues after collagenase enzymatic brain dissociation to guarantee the best EVs' integrity. Then proteomic profiling and tau seeding capacity testing were performed in vitro and in vivo.

resultsBD-EVs were stratified according to their size (eSEVs and eLEVs) and characterized to define new markers specific to EVs in AD. Both AD-derived eSEVs and eLEVs show the presence of GWAS-associated proteins and indicate a specific AD pathophysiological signature. Notably, AD eSEVs contain more proteins relative to the integrin-mediated synaptic signaling, while AD eLEVs proteins were more related to respiratory electron transport and brain immunity. Injection of these vesicles in transgenic mouse brain revealed that the AD-derived eSEVs are more prone than eLEVs to participate in the prion-like propagation and hence represent an interesting therapeutic target.

conclusionThis study highlights the significant contribution of AD-derived EVs to tau propagation and provides new insights into different roles of EV sub-populations in AD.

Indexed as

Alzheimer DiseaseBrainExtracellular VesiclesAgedAged, 80 and overAnimalsFemaleHumansMaleMiceMice, TransgenicProteomicstau Proteinstau ProteinsAlzheimer's diseaseClusterinCollagenase brain dissociationExtracellular vesiclesFERMT2GWASProteomic profilingTau seeding

Identifiers

PMID41345709
PMCPMC12679798

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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.