Functional distribution and further characterization of human endothelial ligand for cellular L-selectin.
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.
Collett
C
C
Department of Histopathology, University College London Medical School, UK.
Munro
J M
JM
D000818:Animals; D002236:Carbohydrate Conformation; D002460:Cell Line; D004729:Endothelium, Lymphatic / Q000378:metabolism*; D006801:Humans; D007150:Immunohistochemistry; D019041:L-Selectin / Q000378:metabolism*; D051379:Mice; D013583:Synovial Membrane / Q000378:metabolism; D014162:Transfection
D019041:L-Selectin