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J Biol Chem, Vol. 274, Issue 9, 5271-5278, February 26, 1999
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From the Synthetic carbohydrate and glycoprotein mimics
displaying sulfated saccharide residues have been assayed for their
L-selectin inhibitory properties under static and flow conditions.
Polymers displaying the L-selectin recognition epitopes 3',6-disulfo
Lewis x(Glc)
(3-O-SO3-Gal Departments of Chemistry and Biochemistry,
University of Wisconsin-Madison, Madison, Wisconsin 53706, the
¶ Department of Internal Medicine, The University of
Texas Medical School, Houston, Texas 77030, and the
§ Department of Immunology, Weizmann Institute of Science,
76100 Rehovot, Israel
1
4(Fuc13)-6-O-SO3-Glc-OR)
and 3',6'-disulfo Lewis x(Glc)
(3,6-di-O-SO3-Gal14(Fuc13)Glc-OR)
both inhibit L-selectin binding to heparin under static, cell-free
binding conditions with similar efficacies. Under conditions of shear flow, however, only the polymer displaying 3',6-disulfo Lewis x(Glc)
inhibits the rolling of L-selectin-transfected cells on the
glycoprotein ligand GlyCAM-1. Although it has been shown to more
effective than sialyl Lewis x at blocking the L-selectin-GlyCAM-1 interaction in static binding studies, the corresponding monomer had no
effect in the dynamic assay. These data indicate that multivalent ligands are far more effective inhibitors of L-selectin-mediated rolling than their monovalent counterparts and that the inhibitory activities are dependent on the specific sulfation pattern of the
recognition epitope. Importantly, our results indicate the L-selectin
specificity for one ligand over another found in static, cell-free
binding assays is not necessarily retained under the conditions of
shear flow. The results suggest that monovalent or polyvalent
carbohydrate or glycoprotein mimetics that inhibit selectin binding in
static assays may not block the more physiologically relevant process
of selectin-mediated rolling.
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