Abstract

The adhesive interactions between leukocyte L-selectin and the endothelium are involved in the migration of lymphocytes through peripheral lymph nodes and of neutrophils to sites of inflammation. A recombinant L-selectin stains high endothelial venules (HEVs) in lymph nodes and recognizes sulfated carbohydrates found on two endothelial glycoproteins, Sgp50 and Sgp90. Amino acid sequencing of purified Sgp90 revealed a protein core identical to that of CD34, a sialomucin expressed on hematopoietic stem cells and endothelium. A polyclonal antiserum to recombinant murine CD34 stains peripheral lymph node endothelium and recognizes Sgp90 that is functionally bound by L-selectin. Thus, an HEV glycoform of CD34 can function as a ligand for L-selectin.

Keywords

High endothelial venulesCD34EndotheliumPolyclonal antibodiesRecombinant DNAChemistryMolecular biologyGlycoproteinL-selectinLymphocyte homing receptorBiologyCell biologyLymph nodeStem cellImmunologyAntigenBiochemistryCell adhesion moleculeCell adhesionCellGene

Affiliated Institutions

Related Publications

Publication Info

Year
1993
Type
article
Volume
262
Issue
5132
Pages
436-438
Citations
628
Access
Closed

External Links

View on DOI.org

Social Impact

Altmetric
PlumX Metrics

Social media, news, blog, policy document mentions

Citation Metrics

628
OpenAlex

Cite This

Susanne Baumheter, Mark S. Singer, William J. Henzel et al. (1993). Binding of L-Selectin to the Vascular Sialomucin CD34. Science , 262 (5132) , 436-438. https://doi.org/10.1126/science.7692600

Identifiers

DOI
10.1126/science.7692600