Identification of a specific glycoprotein ligand for P-selectin (CD62) on myeloid cells.

• DOI: 10.1083/jcb.118.2.445
• Publication Date: 2004-05-15T00:22:22Z
• Authors: K L Moore; N L Stults; S Diaz; D F Smith; R D Cummings; A Varki; R P McEver
• Keywords: P-selectin; Sialidase

P-selectin (CD62, GMP-140, PADGEM), a Ca(2+)-dependent lectin on activated platelets and endothelium, functions as receptor for myeloid cells by interacting with sialylated, fucosylated lactosaminoglycans. binds to limited number of protease-sensitive sites cells, but the protein(s) that carry glycans recognized are unknown. Blotting neutrophil or HL-60 cell membrane extracts [125I]P-selectin affinity chromatography [3H]glucosamine-labeled were used identify ligands. A major ligand was identified an approximately 250,000 M(r) under nonreducing conditions 120,000 reducing conditions. Binding Ca2+ dependent blocked mAbs P-selectin. Brief sialidase digestion increased its apparent molecular weight; however, prolonged abolished binding Peptide:N-glycosidase F treatment reduced weight 3,000 did not affect binding. Western blot immunodepletion experiments indicated lamp-1, lamp-2, L-selectin, which sialyl Le(x), nor it leukosialin, heavily sialylated glycoprotein similar weight. The preferential interaction suggests may play role in adhesion endothelial cells.