ELAM-1-dependent cell adhesion to vascular endothelium determined by a transfected human fucosyltransferase cDNA

Abstract

Adhesion of circulating leukocytes to the vascular endothelium during inflammation is mediated in part by their interaction with the endothellal-leukocyte adhesion molecule ELAM-1. ELAM-1, a member of the LEC-CAM family of cell adhesion molecules, expresses an N-terminal carbohydrate recognition domain (CRD) homologous to various calcium-dependent mammallan lectins. However, the contribution of the CRD to cell adhesion and its carbohydrate binding specificity have not been elucidated. This study demonstrates that transfection of a human fucosyltransferase cDNA into nonmyeloid cell lines confers ELAM-1-dependent endothelial adhesion. Binding activity correlates with de novo cell surface expression of the slalylated Lewis x tetrasaccharide, whose blosynthesis is determined by the transfected fucosyltransferase cDNA. We propose that specific [alpha](1,3)fucosyltransferases regulate cell adhesion to ELAM-1 by modulating cell surface expression of one or more [alpha](2,3)sialylated, [alpha](1,3)fucosylated lactosaminoglycans represented by the sialyl Lewis x carbohydrate determinant.