Identification of a Carbohydrate-Based Endothelial Ligand for a Lymphocyte Homing Receptor

Lymphocyte attachment to high endothelial venules within lymph nodes is mediated by the peripheral lymph node homing receptor (pnHR), originally defined on mouse lymphocytes by the MEL-14 mAb. The pnHR is a calcium-dependent lectin-like receptor, a member of the LEC-CAM family of adhesion proteins....

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Published inThe Journal of cell biology Vol. 113; no. 5; pp. 1213 - 1221
Main Authors Imai, Yasuyuki, Singer, Mark S., Fennie, Christopher, Lasky, Laurence A., Rosen, Steven D.
Format Journal Article
LanguageEnglish
Published New York, NY Rockefeller University Press 01.06.1991
The Rockefeller University Press
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Summary:Lymphocyte attachment to high endothelial venules within lymph nodes is mediated by the peripheral lymph node homing receptor (pnHR), originally defined on mouse lymphocytes by the MEL-14 mAb. The pnHR is a calcium-dependent lectin-like receptor, a member of the LEC-CAM family of adhesion proteins. Here, using a soluble recombinant form of the homing receptor, we have identified an endothelial ligand for the pnHR as an ∼50-kD sulfated, fucosylated, and sialylated glycoprotein, which we designate Sgp50(sulfated glycoprotein of 50 kD). Recombinant receptor binding to this lymph node-specific glycoprotein requires calcium and is inhibitable by specific carbohydrates and by MEL-14 mAb. Sialylation of the component is required for binding. Additionally, the glycoprotein is precipitated by MECA-79, an adhesion-blocking mAb reactive with lymph node HEV. A related glycoprotein of ∼90 kD (designated as Sgp90) is also identified.
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ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.113.5.1213