Proteomics of eosinophil activation

Deane F. Mosher, Emily M. Wilkerson, Keren B. Turton, Alexander S. Hebert, Joshua J. Coon

Research output: Contribution to journalReview articlepeer-review

6 Scopus citations


We recently identified and quantified > 7,000 proteins in non-activated human peripheral blood eosinophils using liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS) and described phosphoproteomic changes that accompany acute activation of eosinophils by interleukin-5 (IL5) (1). These data comprise a treasure trove of information about eosinophils. We illustrate the power of label-free LC-MS/MS quantification by considering four examples: complexity of eosinophil STATs, contribution of immunoproteasome subunits to eosinophil proteasomes, complement of integrin subunits, and contribution of platelet proteins originating from platelet-eosinophil complexes to the overall proteome. We describe how isobaric labeling enables robust sample-to-sample comparisons and relate the 220 phosphosites that changed significantly upon treatment with IL5 to previous studies of eosinophil activation. Finally, we review previous attempts to leverage the power of mass spectrometry to discern differences between eosinophils of healthy subjects and those with eosinophil-associated conditions and point out features of label-free quantification and isobaric labeling that are important in planning future mass spectrometric studies.

Original languageEnglish
Article number159
JournalFrontiers in Medicine
Issue numberSEP
StatePublished - 2017


  • Eosinophils
  • Immunoproteasome
  • Integrins
  • Interleukin-5
  • Mass spectrometry-based proteomics
  • Phosphorylation sites
  • STAT3


Dive into the research topics of 'Proteomics of eosinophil activation'. Together they form a unique fingerprint.

Cite this