C. Collett et Jm. Munro, Functional distribution and further characterization of human endothelial ligand for cellular L-selectin, TISSUE CELL, 31(1), 1999, pp. 39-44
In the present study we examine the functional distribution of the human en
dothelial L-selectin ligand, which determines the sites of extravasation of
L-selectin-positive cells, A murine cell line transfected with human L-sel
ectin adhered preferentially to the high endothelial venules (HEV) of human
peripheral lymph nodes compared to the HEV of mucosal lymphoid tissues (me
an of 0.83 compared to a mean of 0.07 cells per HEV respectively). In addit
ion, an antibody against L-selectin differentially inhibited the adhesion o
f human lymphocytes to peripheral lymphoid tissue versus mucosal lymphoid t
issue HEV (mean 41 and 5% inhibition respectively). Although both sulfogluc
uronyl-containing glycolipids and sialyl-Lewis X have been proposed as endo
thelial ligands for L-selectin, an antibody against the former did not bind
to peripheral lymph node endothelium, and an antibody against the latter d
id not block adhesion of L-selectin-expressing cells. The enzyme O-sialogly
coprotein endopeptidase caused up to an 84% reduction in L-selectin-depende
nt binding, indicating that sialylated glycoproteins containing O-linked gl
ycans are essential for a large majority of adhesion via L-selectin.