Evidence map›Paper›PMID 27590054›Full record

ArticleJournal of neuroinflammation2016

The anti-inflammatory Annexin A1 induces the clearance and degradation of the amyloid-β peptide.

Miriam Ries, Rodrigo Loiola, Urvi N Shah, Steve M Gentleman, Egle Solito, Magdalena Sastre

Open access · goldAbstract read
In one paragraph

Article in Journal of neuroinflammation, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed, 2 pooled it
5.0field-weighted citation impact, top 4% 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

62 citing papers in PubMed, 2 syntheses or guidelines pooled it, 113 citations in OpenAlex.

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  13. Connecting genomic and proteomic signatures of amyloid burden in the brain.medRxiv : the preprint server for health sciences · 2024
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2 more citing papers are in PubMed but not listed here.

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.

Miriam RiesDivision of Brain Sciences, Hammersmith Hospital, Imperial College London, London, W12 0NN, UK.
Rodrigo LoiolaWilliam Harvey Research Institute, Barts and The London School of Medicine and Dentistry, Queen Mary University of London, Charterhouse Square, London, EC1M 6BQ, UK.
Urvi N ShahDivision of Brain Sciences, Hammersmith Hospital, Imperial College London, London, W12 0NN, UK.
Steve M GentlemanDivision of Brain Sciences, Hammersmith Hospital, Imperial College London, London, W12 0NN, UK.
Egle SolitoWilliam Harvey Research Institute, Barts and The London School of Medicine and Dentistry, Queen Mary University of London, Charterhouse Square, London, EC1M 6BQ, UK. e.solito@qmul.ac.uk.
Magdalena SastreDivision of Brain Sciences, Hammersmith Hospital, Imperial College London, London, W12 0NN, UK. m.sastre@imperial.ac.uk.
Hammersmith Hospital · GBImperial College London · GBQueen Mary University of London · GBWilliam Harvey Research Institute · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe toxicity of amyloid-β (Aβ) peptide present in the brain of Alzheimer's disease (AD) patients is thought to be mediated via the increased secretion of pro-inflammatory mediators, which can lead to neuronal dysfunction and cell death. In addition, we have previously shown that inflammation can affect Aβ generation. More recently, we have reported that in vitro administration of the anti-inflammatory mediator Annexin A1 (ANXA1) following an inflammatory challenge suppressed microglial activation and this effect was mediated through formyl peptide receptor-like 1 (FPRL1/FPR2) signalling. The aim of this study was to determine the potential role of ANXA1 in the generation and clearance of Aβ.

methodsWe first compared ANXA1 protein expression in the brains of AD patients and healthy controls as well as in the 5XFAD model of AD. To determine the role of ANXA1 in the processing of amyloid precursor protein (APP) and the degradation of Aβ, N2a neuroblastoma cells were treated with human recombinant ANXA1 or transfected with ANXA1 siRNA. We also investigated the effect of ANXA1 on Aβ phagocytosis and microglial activation in BV2 cells treated with synthetic Aβ.

resultsOur data show that ANXA1 is increased in the brains of AD patients and animal models of AD at early stages. ANXA1 was able to reduce the levels of Aβ by increasing its enzymatic degradation by neprilysin in N2a cells and to stimulate Aβ phagocytosis by microglia. These effects were mediated through FPRL1 receptors. In addition, ANXA1 inhibited the Aβ-stimulated secretion of inflammatory mediators by microglia.

conclusionsThese data suggest that ANXA1 plays a pivotal role in Aβ clearance and supports the use of ANXA1 as potential pharmacological tool for AD therapeutics.

Indexed as

AdultAgedAged, 80 and overAlzheimer DiseaseAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAnimalsAnnexin A1Anti-Inflammatory AgentsCell LineCerebral CortexDisease Models, AnimalEnzyme InhibitorsFemaleGene Expression RegulationHumansAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAnnexin A1Anti-Inflammatory AgentsEnzyme InhibitorsOligopeptidestryptophyl-arginyl-tryptophyl-tryptophyl-tryptophyl-tryptophanamideAlzheimer’s diseaseAmyloid-βAnnexin A1Anti-inflammatoryFormyl-peptide receptorInflammationMicrogliaNeprilysin

Identifiers

PMID27590054
PMCPMC5010757
OpenAlexW2515285024

What OpenQuestion holds

Textmetadata
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.