Evidence map›Paper›PMID 33548451›Full record

ArticleFree radical biology & medicine2021

Platelet-derived extracellular vesicles express NADPH oxidase-1 (Nox-1), generate superoxide and modulate platelet function.

Renato Simões Gaspar, Plinio M Ferreira, Joanne L Mitchell, Giordano Pula, Jonathan M Gibbins

Open access · hybridAbstract read
In one paragraph

Article in Free radical biology & medicine, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

22 citing papers in PubMed, 37 citations in OpenAlex.

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  8. Redox Control in Platelet Activity and Therapy.Antioxidants (Basel, Switzerland) · 2025
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  14. The Effect of Extracellular Vesicles on Thrombosis.Journal of cardiovascular translational research · 2023
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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

5 authors at 3 institutions in 2 countries.

Renato Simões GasparInstitute for Cardiovascular and Metabolic Research, School of Biological Sciences, University of Reading, Reading, UK. Electronic address: renatosgaspar@gmail.com.
Plinio M FerreiraNational Heart and Lung Institute, Imperial College London, London, UK.
Joanne L MitchellInstitute for Cardiovascular and Metabolic Research, School of Biological Sciences, University of Reading, Reading, UK.
Giordano PulaUniversity Medical Center Eppendorf Hamburg, Institute for Clinical Chemistry and Laboratory Medicine, Hamburg, Germany.
Jonathan M GibbinsInstitute for Cardiovascular and Metabolic Research, School of Biological Sciences, University of Reading, Reading, UK.
University of Reading · GBImperial College London · GBUniversität Hamburg · DE

Funding

British Heart Foundation FS/17/13/3269British Heart Foundation PG/15/40/31522British Heart Foundation RG/15/2/31224
6 · The paper itself

Abstract

backgroundPlatelets release platelet-derived extracellular vesicles (PDEVs) upon activation - in a process that is regulated by generation of reactive oxygen species (ROS). Platelet NADPH oxidase-1 (Nox-1) contributes to ROS generation and thrombus formation downstream of the collagen receptor GPVI.

objectivesWe aimed to investigate whether PDEVs contain Nox-1 and whether this is relevant for PDEV-induced platelet activation.

methodsPDEVs were isolated through serial centrifugation after platelet activation with thrombin receptor agonist TRAP-6 (activated PDEVs) or in the absence of agonist (resting PDEVs). The physical properties of PDEVs were analyzed through nanoparticle tracking analysis. Nox-1 levels, fibrinogen binding and P-selectin exposure were measured using flow cytometry, and protein levels quantified by immunoblot analysis. ROS were quantified using DCF fluorescence and electron paramagnetic resonance.

resultsNox-1 was found to be increased on the platelet outer membrane upon activation and was present in PDEVs. PDEVs induced platelet activation, while co-addition of GPVI agonist collagen-related peptide (CRP) did not potentiate this response. PDEVs were shown to be able to generate superoxide in a process at least partially mediated by Nox-1, while Nox-1 inhibition with ML171 (also known as 2-APT) did not influence PDEV production. Finally, inhibition of Nox-1 abrogated PDEV-mediated platelet activation.

conclusionsPDEVs are able to generate superoxide, bind to and activate platelets in a process mediated by Nox-1. These data provide novel mechanisms by which Nox-1 potentiates platelet responses, thus proposing Nox-1 inhibition as a feasible strategy to treat and prevent thrombotic diseases.

Indexed as

Blood PlateletsExtracellular VesiclesNADPH Oxidase 1NADPH OxidasesPlatelet ActivationReactive Oxygen SpeciesSuperoxidesNADPH Oxidase 1NADPH OxidasesReactive Oxygen SpeciesSuperoxidesExtracellular vesiclesNADPH OxidasePlatelet activationPlateletsRedox biology

Identifiers

PMID33548451
PMCPMC7985666
OpenAlexW3126685718

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Registered trials

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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.