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Updated: Aug 8, 2026

Analysis of Physiologic E-Selectin-Mediated Leukocyte Rolling on Microvascular Endothelium
Published on: February 11, 2009
[Structure and function of L-selectin]
1Department of Immunology, Tokyo Metropolitan Institute of Medical Science.
Insights
Researchers investigated the function of L-selectin, a key molecule in lymphocyte homing. They developed tools to study its interaction with ligands, revealing its biological significance in leukocyte adhesion and trafficking.
Area of Science:
- Immunology
- Cell Biology
- Molecular Biology
Context:
- L-selectin (LECAM) is a critical lymphocyte homing receptor mediating lymphocyte binding to high endothelial venules.
- Despite being well-characterized, its precise mechanism in lymphocyte-HE cell interactions remains unclear.
- L-selectin is expressed on lymphocytes and other leukocytes, complicating its role in recirculation.
Purpose:
- To elucidate the exact operating mechanism of L-selectin in lymphocyte-HE cell interactions.
- To identify ligand structures recognized by L-selectin.
- To produce blocking and non-blocking monoclonal antibodies for L-selectin research.
Summary:
- Rat L-selectin cDNA was cloned, and a soluble fusion protein was generated.
- This fusion protein aided in identifying L-selectin ligand structures.
- Monoclonal antibodies were produced to further investigate L-selectin's biological significance.
Impact:
- Provides novel tools (fusion protein, antibodies) for studying L-selectin.
- Contributes to understanding leukocyte adhesion and homing mechanisms.
- Advances knowledge on the biological significance of L-selectin-ligand interactions in immune cell trafficking.
Abstract:
L-selectin, one of the selectin (LECAM) members, is thought to be the lymphocyte homing receptor that mediates binding of lymphocytes to high endothelial venules of peripheral lymph nodes. Although L-selectin is probably the most well-characterized lymphocyte adhesion molecule, there are still a number of unresolved issues, one of which is exact operating mechanism in the lymphocyte-HE cell interaction. This molecule is expressed not only by lymphocytes but also by all other types of leukocytes which in fact never recirculate in the body. We have cloned cDNA encoding rat L-selectin and produced a soluble fusion protein of rat L-selectin and human IgG, and used it to identify ligand structures recognized by L-selectin, and also to produce blocking as well as non-blocking monoclonal antibodies to rat L-selectin. By using these tools, we investigated the biological significance of interaction between L-selectin and its ligand. Summary of these results are presented herein.
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