Evidence map›Paper›PMID 29706072›Full record

ArticleJournal of proteome research2018

Proteomic and Phosphoproteomic Changes Induced by Prolonged Activation of Human Eosinophils with IL-3.

Stephane Esnault, Alexander S Hebert, Nizar N Jarjour, Joshua J Coon, Deane F Mosher

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

14 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Eosinophil-Epithelial Cell Interactions in Asthma.International archives of allergy and immunology · 2024
    Review
  5. Article
  6. Article
  7. Increased IL-6 and Potential IL-6 trans-signalling in the airways after an allergen challenge.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Eosinophil cytolysis on Immunoglobulin G is associated with microtubule formation and suppression of rho-associated protein kinase signalling.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2020
    Article
  12. Article
  13. Article
  14. Article
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 1 institution in 1 country.

Stephane EsnaultDepartment of Medicine , University of Wisconsin , Madison , Wisconsin 53792 , United States.
Alexander S HebertDepartment of Chemistry , University of Wisconsin , Madison , Wisconsin 53706 , United States.
Nizar N JarjourDepartment of Medicine , University of Wisconsin , Madison , Wisconsin 53792 , United States.
Joshua J CoonDepartment of Chemistry , University of Wisconsin , Madison , Wisconsin 53706 , United States.ORCID 0000-0002-0004-8253
Deane F MosherDepartment of Medicine , University of Wisconsin , Madison , Wisconsin 53792 , United States.ORCID 0000-0002-1233-1005
University of Wisconsin–Madison · US

Funding

Thr Role of Pin1 in AirwayP01HL088594 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI JARJOUR, NIZAR N · 2008 to 2017
$21.0M
Proteomics of eosinophil activationR01AI125390 · NIAID · UNIVERSITY OF WISCONSIN-MADISON · PI COON, JOSHUA J, MOSHER, DEANE FREMONT · 2016 to 2019
$1.5M
NHLBI NIH HHS P01 HL088594NIAID NIH HHS R01 AI125390
6 · The paper itself

Abstract

Purified human eosinophils treated for 18-24 h with IL-3 adopt a unique activated phenotype marked by increased reactivity to aggregated immunoglobulin-G (IgG). To characterize this phenotype, we quantified protein abundance and phosphorylation by multiplexed isobaric labeling combined with high-resolution mass spectrometry. Purified blood eosinophils of five individuals were treated with IL-3 or no cytokine for 20 h, and comparative data were obtained on abundance of 5385 proteins and phosphorylation at 7330 sites. The 1150 proteins that were significantly up-regulated ( q < 0.05, pairwise t test with Benjamini-Hochberg correction) by IL-3 included the IL3RA and CSF2RB subunits of the IL-3 receptor, the low-affinity receptor for IgG (FCGR2B), 96 proteins involved in protein translation, and 55 proteins involved in cytoskeleton organization. Among the 703 proteins that decreased were 78 mitochondrial proteins. Dynamic regulation of protein phosphorylation was detected at 4218 sites. These included multiple serines in CSF2RB; Y694 of STAT5, a key site of activating phosphorylation downstream of IL3RA/CSF2RB; and multiple sites in RPS6KA1, RPS6, and EIF4B, which are responsible for translational initiation. We conclude that IL-3 up-regulates overall protein synthesis and targets specific proteins for up-regulation, including its own receptor.

Indexed as

AdultCells, CulturedChromatography, LiquidCluster AnalysisEosinophilsFemaleHumansInterleukin-3MaleMass SpectrometryMiddle AgedPhosphoproteinsPhosphorylationProteomicsSignal TransductionUp-RegulationInterleukin-3PhosphoproteinseosinophilIL-3mass spectrometry-based proteomicsphosphorylation sites

Identifiers

PMID29706072
PMCPMC5984179
OpenAlexW2801497868

What OpenQuestion holds

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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.