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Department of Microbiology-Immunology, Northwestern Medical School, Chicago, IL 60611; and
Department of Pathology, University of Michigan, Ann Arbor, MI 48109
Selectins are carbohydrate-binding cell adhesion molecules that
play a key role in the initiation of inflammatory responses. Several
studies have suggested that the sialylated, fucosylated tetrasaccharide
sialyl Lewis X (sLex) is an important component of leukocyte ligands
for E- and P-selectin. We have identified a stable variant of the HL60
cell line, HL60var, which displays a nearly complete absence of
staining with several mAb directed against sLex and/or sLex-related
structures. HL60var also exhibits a concomitant increase in reactivity
with mAb directed against the unsialylated Lewis X (Lex/CD15)
structure. Despite this sLex deficiency, HL60var binds well to both E-
and P-selectin. No significant differences in expression of
1,3-fucosyltransferases, C2GnT (Core2 transferase), or P-selectin
glycoprotein ligand-1 between HL60var and typical sLexhigh
HL60 cells were detected. Although the precise molecular basis for the
sLex-/low phenotype of HL60var remains uncertain,
flow cytometric analysis with the sialic acid-specific Limax
flavus lectin revealed a sharp reduction in HL60var surface
sialylation. Thus, the loss in mAb reactivity may result from a loss of
sialic acid residues from the mAb carbohydrate epitope. However,
binding of HL60var to E- and P-selectin remains sensitive to
neuraminidase treatment. Taken together, these data indicate that high
levels of surface sLex and/or related epitopes are not essential for
interactions with vascular selectins, implying that as yet unidentified
sialylated, fucosylated structures serve as physiologically relevant
ligands for E- and P-selectin.
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