ELAM-1--dependent cell adhesion to vascular endothelium determined by a transfected human fucosyltransferase cDNA.
Adhesion of circulating leukocytes to the vascular endothelium during inflammation is mediated in part by their interaction with the endothelial-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 mammalian 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 sialylated Lewis x tetrasaccharide, whose biosynthesis 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.
Howard Hughes Medical Institute, University of Michigan Medical School, Ann Arbor 48109-0650.
J B
JB
Lowe
L M
LM
Stoolman
R P
RP
Nair
R D
RD
Larsen
T L
TL
Berhend
R M
RM
Marks
D000818:Animals; D002448:Cell Adhesion; D015815:Cell Adhesion Molecules / Q000502:physiology*; D002460:Cell Line; D003001:Cloning, Molecular; D019040:E-Selectin; D004730:Endothelium, Vascular / Q000166:cytology / Q000502:physiology*; D005434:Flow Cytometry; D005647:Fucosyltransferases / Q000235:genetics / Q000378:metabolism*; D005732:Gangliosides; D006168:Guinea Pigs; D006801:Humans; D016256:Lewis X Antigen; D009844:Oligosaccharides / Q000096:biosynthesis; D014162:Transfection
D015815:Cell Adhesion Molecules; D019040:E-Selectin; D005732:Gangliosides; D016256:Lewis X Antigen; D009844:Oligosaccharides; D005647:Fucosyltransferases