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Related Experiment Videos

Proteomics of Eosinophil Activation.

Deane F Mosher1,2, Emily M Wilkerson3, Keren B Turton1

  • 1Department of Biomolecular Chemistry, University of Wisconsin, Madison, WI, United States.

Frontiers in Medicine
|October 17, 2017
PubMed
Summary
This summary is machine-generated.

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This study quantified over 7,000 proteins in human eosinophils and detailed their phosphoproteomic changes upon activation by interleukin-5 (IL5). These findings offer new insights into eosinophil biology and mass spectrometry applications.

Area of Science:

  • Immunology
  • Proteomics
  • Cell Biology

Background:

  • Human peripheral blood eosinophils play crucial roles in immune responses.
  • Understanding eosinophil protein composition and activation is vital for disease research.
  • Previous mass spectrometry studies have limitations in comprehensive eosinophil analysis.

Purpose of the Study:

  • To identify and quantify a large number of proteins in non-activated human eosinophils.
  • To characterize phosphoproteomic alterations in eosinophils following interleukin-5 (IL5) activation.
  • To demonstrate the utility of label-free and isobaric labeling mass spectrometry techniques for eosinophil research.

Main Methods:

  • Liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS) for protein identification and quantification.
Keywords:
STAT3eosinophilsimmunoproteasomeintegrinsinterleukin-5mass spectrometry-based proteomicsphosphorylation sites

Related Experiment Videos

  • Label-free quantification to assess protein abundance variations.
  • Isobaric labeling techniques for robust sample-to-sample comparisons.
  • Analysis of phosphoproteomic changes upon IL5 stimulation.

    • Main Results:

    • Identification and quantification of over 7,000 proteins in human eosinophils.
    • Detailed characterization of phosphoproteomic changes induced by IL5 activation, identifying 220 significantly altered phosphosites.
    • Illustrative examples of label-free quantification applied to eosinophil STATs, immunoproteasome, integrin subunits, and platelet-derived proteins.
    • Demonstration of robust sample comparisons using isobaric labeling.

    Conclusions:

    • Mass spectrometry, particularly label-free LC-MS/MS and isobaric labeling, provides powerful tools for comprehensive eosinophil proteomic and phosphoproteomic analysis.
    • The study provides a rich dataset for understanding eosinophil biology and activation pathways.
    • Findings inform future mass spectrometry-based studies for discerning eosinophil differences in health and disease states.