Evidence map›Paper›PMID 32772431›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2020

Extracellular vesicles: where the amyloid precursor protein carboxyl-terminal fragments accumulate and amyloid-β oligomerizes.

Rocío Pérez-González, Yohan Kim, Chelsea Miller, Javier Pacheco-Quinto, Elizabeth A Eckman, Efrat Levy

Registry-linked trialOpen access · hybridAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT07314268 (ATTR Amyloid Cardiomyopathy), which is not on this map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.7field-weighted citation impact, top 9% 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.

NCT07314268 recruitingnot on this mapstarted 2024, after this paper: background citation

ATTR Amyloid Cardiomyopathy: Characterization of Extracellular Vesicles as Potential Disease Stratifiers and Prognostic Biomarkers

Typeobservational_patient_registrySponsorUniversity of Sao Paulo General HospitalRan2024 to 2026Enrolled70ConditionsWild-type ATTR Amyloidosis, Amyloidosis Cardiac, Amyloidosis, Hereditary, Amyloidosis Transthyretin
3 · Its place in the literature

Who cites it

39 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
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  5. Review
  6. Article
  7. Article
  8. Organelle abnormalities in Alzheimer's disease.Organelle (Tucson, Ariz.) · 2025
    Article
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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

6 authors at 4 institutions in 1 country.

Rocío Pérez-GonzálezCenter for Dementia Research, Nathan S. Kline Institute, Orangeburg, NY, USA.
Yohan KimCenter for Dementia Research, Nathan S. Kline Institute, Orangeburg, NY, USA.
Chelsea MillerCenter for Dementia Research, Nathan S. Kline Institute, Orangeburg, NY, USA.
Javier Pacheco-QuintoBiomedical Research Institute of New Jersey, Cedar Knolls, and Atlantic Health Systems, Morristown, NJ, USA.
Elizabeth A EckmanBiomedical Research Institute of New Jersey, Cedar Knolls, and Atlantic Health Systems, Morristown, NJ, USA.
Efrat LevyCenter for Dementia Research, Nathan S. Kline Institute, Orangeburg, NY, USA.
Biomedical Research Institute · USNathan Kline Institute for Psychiatric Research · USNeurosciences Institute · USNew York University · US

Funding

Uncovering Alzheimer's disease risk mechanisms through neuron-specific analysis of autophagy and endosomal-lysosomal functionP01AG017617 · NIA · NATHAN S. KLINE INSTITUTE FOR PSYCH RES · PI NIXON, RALPH A. · 2000 to 2021
$40.0M
Preventing early events in Aβ-driven pathology in vivoR01AG056732 · NIA · NATHAN S. KLINE INSTITUTE FOR PSYCH RES · PI LEVY, EFRAT · 2017 to 2021
$2.0M
NIA NIH HHS P01 AG017617NIA NIH HHS R01 AG056732
6 · The paper itself

Abstract

Pleiotropic roles are proposed for brain extracellular vesicles (EVs) in the development of Alzheimer's disease (AD). Our previous studies have suggested a beneficial role for EVs in AD, where the endosomal system in vulnerable neurons is compromised, contributing to the removal of accumulated material from neurons. However, the involvement of EVs in propagating AD amyloidosis throughout the brain has been considered because the amyloid-β precursor protein (APP), APP metabolites, and key APP cleaving enzymes were identified in association with EVs. Here, we undertook to determine whether the secretase machinery is actively processing APP in EVs isolated from the brains of wild-type and APP overexpressing Tg2576 mice. We found that full-length APP is cleaved in EVs incubated in the absence of cells. The resulting metabolites, both α- and β-APP carboxyl-terminal fragments and APP intracellular domain accumulate in EVs over time and amyloid-β dimerizes. Thus, EVs contribute to the removal from neurons and transport of APP-derived neurotoxic peptides. While this is potentially a venue for propagation of the pathology throughout the brain, it may contribute to efficient removal of neurotoxic peptides from the brain.

Indexed as

BrainAlzheimer DiseaseAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAnimalsExtracellular VesiclesFemaleMaleMiceMice, TransgenicPeptide FragmentsProtein Aggregation, PathologicalAmyloid beta-PeptidesAmyloid beta-Protein PrecursorPeptide FragmentsAlzheimer's diseaseAPP-CTFsAPP metabolismAβ oligomersexosomes

Identifiers

PMID32772431
PMCPMC7496786
OpenAlexW3048120681

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

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.