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Procoagulant Platelet Characterization by Measuring Phosphatidylserine Exposure and Microvesicle Release from Human Purified Platelets
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Comparative proteomics reveals unexpected quantitative phosphorylation differences linked to platelet activation

G J Schmidt1, C M Reumiller2, H Ercan2

  • 1Department of Clinical Pharmacology, Medical University of Vienna, Vienna, Austria.

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|December 14, 2019
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Summary

This study reveals new protein targets for assessing platelet function in thrombotic disorders. It highlights novel phosphorylation changes in inhibited platelets, offering better diagnostic alternatives than P-selectin.

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Area of Science:

  • Biochemistry
  • Hematology
  • Proteomics

Background:

  • Assessing platelet activation is crucial for managing thrombotic disorders.
  • Current methods like flow cytometry for P-selectin and activated integrin αIIbβ3, and VASP phosphorylation monitoring have limitations.
  • A more comprehensive understanding of platelet reactivity proteome changes is needed.

Purpose of the Study:

  • To compare the human non-secretory platelet proteome during in-vitro activation and inhibition.
  • To identify novel protein markers for platelet reactivity.
  • To evaluate alternatives to P-selectin for characterizing platelet activation and inactivation.

Main Methods:

  • Unbiased fluorescence two-dimensional differential in-gel electrophoresis (2D-DIGE) was used to compare platelet proteomes.
  • Platelet samples were analyzed after in-vitro activation and inhibition, with untreated controls.
  • Phosphorylation levels of specific proteins and P-selectin surface expression were quantified.

Main Results:

  • The platelet proteome was more affected by inhibition than activation.
  • Inhibited platelets showed increased phosphorylation of VASP (1.3-fold) and other protein kinase A targets like LIM and SH3 domain protein 1 (6.7-fold), Src kinase-associated phosphoprotein 2 (4.6-fold), and Ras-related protein Rap1b (4.1-fold).
  • Dephosphorylated integrin-linked protein kinase (ILK) and phosphorylated pleckstrin (PLEK) showed higher discrimination power (Cohen's d effect size 3.79 and 3.77, respectively) than P-selectin (2.35).

Conclusions:

  • This study provides novel insights into quantitative changes in the platelet reactivity proteome.
  • Dephosphorylated ILK and phosphorylated PLEK are proposed as powerful alternatives for assessing platelet activation and inactivation potential.
  • These findings could lead to improved diagnostic tools for thrombotic disorders.