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Functional and structural characterization of the eosinophil P-selectin ligand
F A Symon1, M B Lawrence, M L Williamson
1Department of Respiratory Medicine, Leicester University Medical School, Glenfield Hospital, United Kingdom.
Journal of Immunology (Baltimore, Md. : 1950)
|August 15, 1996
Summary
Eosinophils exhibit greater adhesion to P-selectin than neutrophils, suggesting P-selectin
Area of Science:
- Immunology
- Cell Biology
- Biochemistry
Background:
- P-selectin mediates leukocyte adhesion.
- Eosinophil adhesion is crucial in inflammatory diseases.
Purpose of the Study:
- Compare eosinophil and neutrophil binding to P-selectin.
- Investigate the structure and expression of P-selectin ligands on eosinophils and neutrophils.
Main Methods:
- Frozen section assay with nasal polyp endothelium.
- Flow conditions assay with purified P-selectin.
- SDS-PAGE to characterize P-selectin ligands.
Main Results:
- Eosinophils showed significantly higher binding to nasal polyp endothelium and purified P-selectin compared to neutrophils.
- Eosinophils express greater amounts of P-selectin glycoprotein ligand-1 (PSGL-1) than neutrophils.
- Eosinophil PSGL-1 is a sialylated, homodimeric glycoprotein with a distinct peptide backbone compared to neutrophil PSGL-1.
Conclusions:
- P-selectin plays a role in directing eosinophil migration.
- Increased eosinophil binding is likely due to higher PSGL-1 expression and/or structural differences.