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Related Experiment Videos

Thrombin affects eosinophil migration via protease-activated receptor-1.

Clemens Feistritzer1, Birgit A Mosheimer, Nicole C Kaneider

  • 1Division of General Internal Medicine, Department of Internal Medicine, Medical University of Innsbruck, Anichstrasse 35, AT-6020 Innsbruck, Austria.

International Archives of Allergy and Immunology
|August 3, 2004
PubMed
Summary

Thrombin stimulates human eosinophil migration via protease-activated receptor 1 (PAR1) activation. This finding suggests a role for thrombin in eosinophil-mediated tissue and allergic inflammation.

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Area of Science:

  • Immunology
  • Cell Biology
  • G-protein-coupled receptors

Background:

  • Protease-activated receptors (PARs) are G-protein-coupled receptors activated by proteolytic cleavage.
  • PAR1, typically activated by thrombin, is expressed on human eosinophils.
  • The effect of thrombin on eosinophil function remained largely unknown.

Purpose of the Study:

  • To investigate the effect of thrombin on human eosinophil migration in vitro.
  • To determine if thrombin influences eosinophil chemotaxis.

Main Methods:

  • Eosinophils were isolated from healthy donor blood.
  • Micropore filter assays were used to study cell migration.
  • Functional assays included PAR agonists and a PAR1 blocking antibody to assess thrombin's role.

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Main Results:

  • Thrombin significantly stimulated eosinophil chemotaxis in a dose-dependent manner.
  • The PAR1 agonist mimicked thrombin's effect, while the PAR2 agonist did not.
  • A PAR1 blocking antibody reversed thrombin-induced migration, confirming PAR1 involvement.
  • Eosinophil migration was dependent on a thrombin concentration gradient.

Conclusions:

  • Thrombin activation of PAR1 stimulates directed migration of human eosinophils.
  • This mechanism may influence eosinophil behavior in tissue and allergic inflammation.