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An important role for the alpha 1,3 fucosyltransferase, FucT-VII, in
leukocyte adhesion to E-selectin
AJ Wagers, JB Lowe and GS Kansas
Department of Microbiology-Immunology, Northwestern Medical School,
Chicago, IL 60611, USA.
E-selectin is an adhesion molecule expressed on the surface of activated
endothelial cells, which has been shown to be important in the initial
steps of leukocyte extravasation into inflamed tissues. E- selectin binds
neutrophils, monocytes, eosinophils, basophils, natural killer (NK) cells,
and subsets of lymphocytes, although the precise ligand(s) on these cells
have not been identified. Several studies have proposed certain
carbohydrate structures, including sLex and related structures, as
E-selectin ligands. In contrast to these studies, we report here the
identification of several human B cell lines that exhibit binding to
E-selectin without expression of any of the previously identified
E-selectin binding carbohydrate epitopes. The unique carbohydrate phenotype
of these B cell lines suggests that they may express a novel, sialylated
carbohydrate structure(s) that binds to E-selectin. To investigate the
enzymatic basis of this novel form of E- selectin binding, we examined the
expression of the two principal leukocyte alpha 1,3 fucosyltransferases,
FucT-IV and FucT-VII, in a panel of human hematopoietic cell lines.
FucT-VII was expressed in all E-selectin binding cell lines except one,
whereas FucT-IV was expressed by nearly all cell lines, regardless of their
ability to bind E- selectin. In addition, transfection of cells with cDNA
encoding FucT- VII conferred E-selectin binding ability. Taken together,
these data suggest that, regardless of surface carbohydrate phenotype,
E-selectin binding ability is determined largely by expression of FucT-VII.
Volume 88,
Issue 6,
pp. 2125-2132,
09/15/1996
Copyright © 1996 by The American Society of Hematology
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