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A hematopoietic cell L-selectin ligand exhibits sulfate-independent binding
activity
R Sackstein, L Fu and KL Allen
H. Lee Moffitt Cancer Center & Research Institute, University of South
Florida College of Medicine, Tampa 33612, USA.
L-selectin is a leukocyte cell-surface glycoprotein that mediates adhesive
interactions between circulating cells and vascular endothelium. All
endothelial ligands of L-selectin characterized to date are glycoproteins
that require sulfation for activity and share reactivity with MECA 79, a
monoclonal antibody that recognizes a sulfate-dependent epitope involved in
L-selectin attachment. We have recently identified by functional assay a
glycoprotein L-selectin ligand expressed on the human hematopoietic cell
line KG1a. We report here that this ligand is not recognized by MECA 79 and
that it retains binding activity after metabolic inhibition of sulfation by
chlorate. A native membrane L-selectin ligand exhibiting
sulfate-independent function has not been described previously.
Identification of this novel ligand on a nonendothelial cell type suggests
that structural determinants conferring L-selectin binding may vary in a
cell- and tissue-specific manner.
Volume 89,
Issue 8,
pp. 2773-2781,
04/15/1997
Copyright © 1997 by The American Society of Hematology
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