Peptides derived from the lectin domain of selectin adhesion molecules inhibit leukocyte rolling in vivo.

Objective: The selectins are a family of adhesion molecules that mediate leukocyte rolling, a prerequisite for their later firm adhesion and migration to sites of inflammation. The N-terminal lectin domain of selectins is important for Ca2+-dependent binding to oligosaccharide ligands. We set out to study the effect of peptides corresponding to residues 11–20, 23–30, 36–50, 54–63, 70–79 and 109–118 (counting from the N-terminus of the mature proteins) of the lectin domain of human L-, P- and E-selectins on leukocyte rolling in vivo.Methods: Peptides were applied by local intravascular microinfusion via a glass micropipette into rat mesenteric venules. Visibly rolling cells were counted off-line and compared with rolling cells counted during control periods.Results: Peptides corresponding to residues 70–79 of P-selectin and 11–20 of L-selectin reduced leukocyte rolling flux in rat mesenteric venules to less than 30% of that measured during control infusion. Peptides corresponding to residues 109–118 of P-s...