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Related Experiment Videos

Eotaxin-2 alters eosinophil integrin function via mitogen-activated protein kinases.

Hiroshi Tachimoto1, Matsuo Kikuchi, Sherry A Hudson

  • 1Department of Medicine, Division of Allergy and Clinical Immunology, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21224, USA.

American Journal of Respiratory Cell and Molecular Biology
|May 30, 2002
PubMed
Summary

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Eotaxin-2, a chemokine, alters eosinophil adhesion during allergic inflammation by promoting ICAM-1 use over VCAM-1, mediated by MAP kinases.

Area of Science:

  • Immunology
  • Cell Biology
  • Allergic Inflammation Research

Background:

  • Eosinophils are key players in allergic inflammation.
  • Adhesion molecules and chemokines regulate eosinophil recruitment.

Purpose of the Study:

  • To investigate the effect of eotaxin-2 on eosinophil adhesion to VCAM-1 and ICAM-1.
  • To understand the role of CCR3 and MAP kinases in eotaxin-2-mediated adhesion.

Main Methods:

  • Utilized a parallel plate flow system to assess eosinophil adhesion.
  • Co-immobilized eotaxin-2 with VCAM-1 and/or ICAM-1 on tissue culture plates.
  • Employed blocking monoclonal antibodies and MAP-kinase inhibitors for mechanistic studies.

Main Results:

Related Experiment Videos

  • Eotaxin-2 shifted eosinophil adhesion from VCAM-1 to ICAM-1.
  • ICAM-1's contribution to adhesion increased with eotaxin-2 presence.
  • CCR3 and MAP kinase pathways were essential for eotaxin-2's effects.

    • Conclusions:

    • Eotaxin-2 modulates eosinophil adhesion pathways during allergic inflammation.
    • MAP kinase signaling is involved in eotaxin-2-induced changes in eosinophil adhesion.
    • Eotaxin-2 may facilitate eosinophil recruitment by altering adhesion molecule preference.