Evidence map›Paper›PMID 25713122›Full record

ArticleMolecular & cellular proteomics : MCP2015

A Human Platelet Receptor Protein Microarray Identifies the High Affinity Immunoglobulin E Receptor Subunit α (FcεR1α) as an Activating Platelet Endothelium Aggregation Receptor 1 (PEAR1) Ligand.

Yi Sun, Christophe Vandenbriele, Alexandre Kauskot, Peter Verhamme, Marc F Hoylaerts, Gavin J Wright

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.9field-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.

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

43 citing papers in PubMed, 80 citations in OpenAlex.

  1. Review
  2. Platelet Membrane Receptors and Signalling Pathways.Handbook of experimental pharmacology · 2026
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  11. Complement receptor 1 is the human erythrocyte receptor forProceedings of the National Academy of Sciences of the United States of America · 2024
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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 2 institutions in 2 countries.

Yi SunFrom the ‡Cell Surface Signalling Laboratory, Wellcome Trust Sanger Institute, Cambridge, CB10 1SA, United Kingdom and.
Christophe Vandenbriele§Center for Molecular and Vascular Biology, Department of Cardiovascular Sciences, University of Leuven, Leuven 3000, Belgium.
Alexandre Kauskot§Center for Molecular and Vascular Biology, Department of Cardiovascular Sciences, University of Leuven, Leuven 3000, Belgium.
Peter Verhamme§Center for Molecular and Vascular Biology, Department of Cardiovascular Sciences, University of Leuven, Leuven 3000, Belgium.
Marc F Hoylaerts§Center for Molecular and Vascular Biology, Department of Cardiovascular Sciences, University of Leuven, Leuven 3000, Belgium.
Gavin J WrightFrom the ‡Cell Surface Signalling Laboratory, Wellcome Trust Sanger Institute, Cambridge, CB10 1SA, United Kingdom and gw2@sanger.ac.uk.
KU Leuven · BEWellcome Sanger Institute · GB

Funding

Wellcome Trust 098051
6 · The paper itself

Abstract

Genome-wide association studies to identify loci responsible for platelet function and cardiovascular disease susceptibility have repeatedly identified polymorphisms linked to a gene encoding platelet endothelium aggregation receptor 1 (PEAR1), an "orphan" cell surface receptor that is activated to stabilize platelet aggregates. To investigate how PEAR1 signaling is initiated, we sought to identify its extracellular ligand by creating a protein microarray representing the secretome and receptor repertoire of the human platelet. Using an avid soluble recombinant PEAR1 protein and a systematic screening assay designed to detect extracellular interactions, we identified the high affinity immunoglobulin E (IgE) receptor subunit α (FcεR1α) as a PEAR1 ligand. FcεR1α and PEAR1 directly interacted through their membrane-proximal Ig-like and 13th epidermal growth factor domains with a relatively strong affinity (KD ∼ 30 nm). Precomplexing FcεR1α with IgE potently inhibited the FcεR1α-PEAR1 interaction, and this was relieved by the anti-IgE therapeutic omalizumab. Oligomerized FcεR1α potentiated platelet aggregation and led to PEAR1 phosphorylation, an effect that was also inhibited by IgE. These findings demonstrate how a protein microarray resource can be used to gain important insight into the function of platelet receptors and provide a mechanistic basis for the initiation of PEAR1 signaling in platelet aggregation.

Indexed as

Binding SitesBlood PlateletsGene ExpressionHEK293 CellsHumansImmunoglobulin EKineticsLigandsOmalizumabPhosphorylationPlatelet AggregationProtein Array AnalysisProtein BindingProtein Interaction Domains and MotifsProtein MultimerizationProtein Structure, SecondaryFcepsilonRI alpha-chain, humanImmunoglobulin ELigandsOmalizumabPEAR1 protein, humanReceptors, Cell SurfaceReceptors, IgERecombinant Proteins

Identifiers

PMID25713122
PMCPMC4424398
OpenAlexW2166327916

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.