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Related Experiment Video

Updated: Jul 16, 2026

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

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Published on: June 13, 2014

Mechanisms of eosinophil cationic protein release in the serum: role of adhesion molecules.

Y Kato¹, T Fujisawa, A Terada

¹Department of Psychiatry, University of Mie School of Medicine, Mie, Japan.

International Archives of Allergy and Immunology

|October 26, 1999

Summary

Eosinophil cationic protein (ECP) release during blood clotting is calcium-dependent and involves cell adhesion molecules. Blocking specific integrins significantly reduced ECP levels, clarifying its in vitro release mechanism.

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Area of Science:

Immunology
Allergy Research

Background:

Serum eosinophil cationic protein (ECP) is a marker for allergic inflammation.
In vitro ECP levels include proteins released during blood coagulation, but release mechanisms are unclear.
This study investigates the role of adhesion molecules in ECP release.

Purpose of the Study:

To explore the mechanisms of eosinophil cationic protein (ECP) release during blood coagulation.
To determine the involvement of cell adhesion molecules in ECP release from eosinophils.

Main Methods:

Blood from allergic donors was incubated with antibodies targeting adhesion molecules (CD18, CD11a, CD11b, CD29, CD49d, CD54, alpha4beta7).
Calcium was added to induce coagulation, followed by incubation and centrifugation to obtain serum.
ECP levels were measured using radioimmunoassay (RIA); experiments with purified eosinophils were also conducted.

Main Results:

ECP levels were significantly higher in samples with calcium compared to those without.
Purified eosinophils released ECP when incubated with plasma and calcium.
Antibodies against CD18, CD49d, and alpha4beta7 suppressed ECP release.

Conclusions:

ECP release into serum is dependent on calcium and plasma coagulation.
Cell adhesion, particularly through alphaLbeta2, alphaMbeta2, alpha4beta1, and alpha4beta7 integrins, plays a role in ECP release.