Abstract
In the present study we examine the functional distribution of the human endothelial L-selectin ligand, which determines the sites of extravasation of L-selectin-positive cells. A murine cell line transfected with human L-selectin adhered preferentially to the high endothelial venules (HEV) of human peripheral lymph nodes compared to the HEV of mucosal lymphoid tissues (mean of 0.83 compared to a mean of 0.07 cells per HEV respectively). In addition, an antibody against L-selectin differentially inhibited the adhesion of human lymphocytes to peripheral lymphoid tissue versus mucosal lymphoid tissue HEV (mean 41 and 5% inhibition respectively). Although both sulfoglucuronyl-containing glycolipids and sialyl-Lewis X have been proposed as endothelial ligands for L-selectin, an antibody against the former did not bind to peripheral lymph node endothelium, and an antibody against the latter did not block adhesion of L-selectin-expressing cells. The enzyme O-sialoglycoprotein endopeptidase caused up to an 84% reduction in L-selectin-dependent binding, indicating that sialylated glycoproteins containing O-linked glycans are essential for a large majority of adhesion via L-selectin.