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Division of Gastrointestinal Pathology, Department of Pathology and Laboratory Medicine, Emory University, Atlanta, GA 30322
CD11b/CD18-mediated adhesive interactions play a key role in
regulating polymorphonuclear leukocytes (PMN)) migration across
intestinal epithelium. However, the identity of epithelial ligands for
migrating PMN remains obscure. In this study we investigated the role
of carbohydrates in mediating adhesive interactions between T84
intestinal epithelial cells and CD11b/CD18 purified from PMN. Fucoidin,
heparin/heparin sulfate,
N-acetyl-D-glucosamine, mannose-6-phosphate,
and laminarin were found to inhibit adhesion of T84 cells to
CD11b/CD18. The most potent inhibitory effects were observed with
fucoidin (50% inhibition at 1–5 x 10-8 M). Binding
assays demonstrated that fucoidin directly bound to CD11b/CD18 in a
divalent cation- and sulfation-dependent fashion that was blocked by
anti-CD11b mAbs. Experiments employing CD11b/CD18 as a probe to
blot T84 cell fucosylated proteins purified via fucose-specific lectin
column revealed several candidate CD11b/CD18 binding proteins with
molecular masses of 95, 50, 30, 25, and 20 kDa. Fucosidase treatment of
T84 cells resulted in significantly reduced cell adhesion to
CD11b/CD18, while no inhibition was observed after neuraminidase
treatment. Finally, significant inhibition of T84 cell adhesion to
CD11b/CD18 was observed after blocking cell proteoglycan synthesis with
p-nitrophenyl-
-D-xylopyranoside. These
findings implicate epithelial cell surface proteoglycans decorated with
sulfated fucose moieties as ligands for CD11b/CD18 during PMN migration
across mucosal surfaces.
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