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      ELAM-1 mediates cell adhesion by recognition of a carbohydrate ligand, sialyl-Lex.

      Science (New York, N.Y.)
      Animals, Antibodies, Monoclonal, pharmacology, Antigens, CD15, chemistry, physiology, Carbohydrate Conformation, Carbohydrate Sequence, Cell Adhesion, Cell Adhesion Molecules, immunology, Cell Line, Cricetinae, E-Selectin, Glycosylation, Humans, Ligands, Molecular Sequence Data, Neuraminidase, Neutrophils

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          Abstract

          Recruitment of neutrophils to sites of inflammation is mediated in part by endothelial leukocyte adhesion molecule-1 (ELAM-1), which is expressed on activated endothelial cells of the blood vessel walls. ELAM-1 is a member of the LEC-CAM or selectin family of adhesion molecules that contain a lectin motif thought to recognize carbohydrate ligands. In this report, cell adhesion by ELAM-1 is shown to be mediated by a carbohydrate ligand, sialyl-Lewis X (SLex; NeuAc alpha 2,3Gal beta 1,4(Fuc alpha 1,3)-GlcNAc-), a terminal structure found on cell-surface glycoprotein and glycolipid carbohydrate groups of neutrophils.

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