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Updated: Jul 4, 2026

Analysis of Physiologic E-Selectin-Mediated Leukocyte Rolling on Microvascular Endothelium
Published on: February 11, 2009
E-selectin receptors on human leukocytes
Leonardo Nimrichter1, Monica M Burdick, Kazuhiro Aoki
1Department of Pharmacology and Molecular Sciences, The Johns Hopkins School of Medicine, Baltimore, MD 21205, USA.
Sialylated glycosphingolipids with N-acetyllactosamine repeats and fucose residues are identified as key E-selectin receptors on human neutrophils, mediating inflammation. These findings clarify neutrophil adhesion mechanisms in inflammatory responses.
Area of Science:
- Immunology
- Glycobiology
- Cell Biology
Background:
- Selectins on activated endothelium mediate inflammation by binding to neutrophil carbohydrates.
- The specific human neutrophil receptor for E-selectin remained unidentified.
Purpose of the Study:
- To identify the functional E-selectin receptor on human neutrophils.
- To characterize the role of sialylated glycosphingolipids in E-selectin-mediated adhesion.
Main Methods:
- Glycolipids were extracted from human neutrophils and purified using chromatography.
- Model membrane monolayers were used to quantify selectin-mediated cell tethering and rolling under fluid shear.
- Glycosphingolipid biosynthesis was blocked in cultured neutrophils to assess adhesion changes.
Main Results:
- Sialylated glycosphingolipids with N-acetyllactosamine (LacNAc) repeats and fucose residues were identified as major functional E-selectin receptors.
- These potent receptors constituted over 60% of E-selectin-binding activity and were expressed at high densities on neutrophils.
- Blocking glycosphingolipid biosynthesis reduced E-selectin adhesion, but not P-selectin adhesion.
Conclusions:
- Specific sialylated glycosphingolipids act as functional E-selectin receptors on human neutrophils.
- These findings elucidate the molecular basis of E-selectin-mediated neutrophil adhesion in inflammation.
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