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L-selectin, the leukocyte selectin, mediates the
carbohydrate-dependent attachment of circulating leukocytes to
endothelium, preceding emigration into tissues. It functions in
inflammatory leukocyte trafficking and in lymphocyte homing to lymph
nodes. From previous work, the binding of L-selectin to
endothelial-associated glycoprotein ligands, GlyCAM-1 and CD34,
requires oligosaccharide sialylation, sulfation, and probably
fucosylation. We have recently identified a major capping group in
GlyCAM-1 as 6` sulfated sialyl Lewis x, a novel structure which
potentially satisfies all of these requirements. In the present study,
we define the complete structure of
The implications of these structures and
more complex O-glycans for binding by L-selectin are
discussed.
Volume 270,
Number 20,
Issue of May 19, pp. 12035-12047, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
-eliminated chains of GlyCAM-1
using metabolic radiolabeling, plant lectin binding, and glycosidase
digestions in conjunction with high pH anion-exchange chromatography.
The majority of the O-glycans in GlyCAM-1 contain the
T-antigen, i.e. Gal13GalNAc, which is incorporated
into the core-2 structure, i.e. Gal
13[GlcNAc
16]GalNAc or larger
core structures with additional GlcNAc residues. The structures of two
O-glycans, based on core-2, were determined to be: ±
Fuc
1 3 ± Fuc
1 3 Sia
2
3Gal
1 4GlcNAc
1 Sia2 3Gal
1
4GlcNAc
1 6 ‖ 6 ‖ SO
‖SO
‖
6
6 Sia
3Gal
1 3GalNAc-OH Sia
2
3Gal
1 3GalNAc-OH
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