Title :

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

Author(s) :

Esnault, Stéphane [Auteur]
University of Wisconsin School of Medicine and Public Health
Hebert, Alexander S [Auteur]
Jarjour, Nizar N [Auteur]
Coon, Joshua J [Auteur]
Mosher, Deane F [Auteur]

Journal title :

Journal of Proteome Research

Abbreviated title :

J Proteome Res

Volume number :

17

Pages :

2102-2111

Publication date :

2018-06-01

ISSN :

1535-3907

English keyword(s) :

Adult
Cells, Cultured
Chromatography, Liquid
Cluster Analysis
Eosinophils
Female
Humans
Interleukin-3
Male
Mass Spectrometry
Middle Aged
Phosphoproteins
Phosphorylation
Proteomics
Signal Transduction
Up-Regulation
Young Adult
IL-3
eosinophil
mass spectrometry-based proteomics
phosphorylation sites

HAL domain(s) :

Sciences du Vivant [q-bio]

English abstract : [en]

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 ...
Show more >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.Show less >

Language :

Anglais

Peer reviewed article :

Oui

Audience :

Internationale

Popular science :

Non

Administrative institution(s) :

Université de Lille
Inserm
CHU Lille

Collections :

• Autres travaux scientifiques

Submission date :

2023-10-23T11:38:29Z
2024-03-16T08:45:12Z