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Blood, Vol. 93 No. 4 (February 15), 1999:
pp. 1245-1252
Sialylation of the Sialic Acid Binding Lectin Sialoadhesin Regulates
Its Ability to Mediate Cell Adhesion
Yvonne C. Barnes,
Tim P. Skelton,
Ivan Stamenkovic, and
Dennis C. Sgroi
From the Department of Pathology, Harvard Medical School and the
Molecular Pathology Unit, Massachusetts General Hospital, Boston, MA.
The macrophage-specific cell surface receptor sialoadhesin, which is
a member of the newly recognized family of sialic acid binding lectins
called siglecs, binds glycoprotein and glycolipid ligands containing
a2-3-linked sialic acid on the surface of several leukocyte subsets.
Recently, the sialic acid binding activity of the siglec CD22 has been
demonstrated to be regulated by sialylation of the CD22 receptor
molecule. In the present work, we show that desialylation of in vivo
macrophage sialylconjugates enhances sialoadhesin-mediated lectin
activity. Herein, we show that receptor sialylation of soluble
sialoadhesin inhibits its binding to Jurkat cell ligands, and that
charge-dependent repulsion alone cannot explain this inhibition.
Furthermore, we show that the inhibitory effect of sialic acid is
partially dependent on the presence of an intact exocyclic side chain.
These results, in conjunction with previous findings, suggest that
sialylation of siglecs by specific glycosyltransferases may be a common
mechanism by which siglec-mediated adhesion is regulated.
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