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Selectins

Selectins

Cell adhesion is an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain, which...

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Updated: Jul 4, 2026

Analysis of Physiologic E-Selectin-Mediated Leukocyte Rolling on Microvascular Endothelium

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.

|June 27, 2008

Summary

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.

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Last Updated: Jul 4, 2026

Analysis of Physiologic E-Selectin-Mediated Leukocyte Rolling on Microvascular Endothelium

Analysis of Physiologic E-Selectin-Mediated Leukocyte Rolling on Microvascular Endothelium

Published on: February 11, 2009

Systematic Analysis of In Vitro Cell Rolling Using a Multi-well Plate Microfluidic System

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Published on: October 16, 2013

Simultaneously Capturing Real-time Images in Two Emission Channels Using a Dual Camera Emission Splitting System: Applications to Cell Adhesion

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Published on: September 4, 2013

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.