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Related Concept Videos

Proteomics01:33

Proteomics

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A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
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A Streamlined Approach for Mass Spectrometry-Based Proteomics Using Selected Tissue Regions
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The Peripheral Blood Eosinophil Proteome.

Emily M Wilkerson, Mats W Johansson, Alexander S Hebert1

  • 1Genome Center of Wisconsin, University of Wisconsin , 425 Henry Mall, Madison, Wisconsin 53706, United States.

Journal of Proteome Research
|March 24, 2016
PubMed
Summary
This summary is machine-generated.

Researchers mapped the eosinophil proteome, identifying over 6,800 proteins and thousands of phosphorylation sites. This deep proteomic analysis enhances understanding of eosinophil function in immunity and disease.

Keywords:
eosinophilimmunologyquantitative proteomics

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Area of Science:

  • Proteomics
  • Immunology
  • Cell Biology

Background:

  • A comprehensive understanding of biological systems necessitates detailed knowledge of their protein components.
  • Eosinophils, crucial for defense and immunity, have a largely unannotated proteome with fewer than 500 identified proteins.
  • Existing proteomic maps lack deep coverage of eosinophil-specific proteins.

Purpose of the Study:

  • To create a comprehensive map of the nonstimulated peripheral blood eosinophil proteome.
  • To identify and quantify proteins and phosphorylation events within eosinophils.
  • To analyze proteomic variability and activation states of eosinophils.

Main Methods:

  • Two-dimensional liquid chromatography coupled with high-resolution mass spectrometry was employed.
  • Purified peripheral blood eosinophils were analyzed for their protein content.
  • Platelet contamination was accounted for, and proteomic changes upon interleukin-5 activation were assessed.

Main Results:

  • The analysis identified 7,086 protein groups from 6,813 genes, including 100,892 unique peptides.
  • Over 4,800 site-specific phosphorylation events were detected.
  • Proteomic variability among individuals and changes upon eosinophil activation were characterized.

Conclusions:

  • This study provides a deep and quantitative map of the eosinophil proteome, significantly expanding known eosinophil proteins.
  • The findings address a critical gap in human proteome mapping, particularly for immune cells.
  • This resource will facilitate future proteomic research on eosinophils in health and disease contexts, including allergic responses.