P- and E-Selectin Use Common Sites for Carbohydrate Ligand Recognition and Cell Adhesion

• Published in: The Journal of cell biology Vol. 120; no. 5; pp. 1227 - 1235
• Main Authors: Erbe, David V., Watson, Susan R., Presta, Leonard G., Wolitzky, Barry A., Foxall, Carroll, Brandley, Brian K., Lasky, Laurence A.
• Format: Journal Article
• Language: English
• Published: New York, NY Rockefeller University Press 01-03-1993; The Rockefeller University Press
• Subjects: Amino Acid Sequence; Binding Sites; Biological and medical sciences; Cell Adhesion; Cell Adhesion Molecules - chemistry; Cell Adhesion Molecules - physiology; Cell interactions, adhesion; Cells; Cellular biology; Chimeras; E-Selectin; Flow Cytometry; Fundamental and applied biological sciences. Psychology; Glycolipids; Glycolipids - metabolism; Glycoproteins; Humans; In Vitro Techniques; Lectins; Ligands; Models, Molecular; Molecular and cellular biology; Molecular Sequence Data; Mutagenesis, Site-Directed; Neutrophils; P-Selectin; Platelet Membrane Glycoproteins - chemistry; Platelet Membrane Glycoproteins - physiology; Protein Structure, Tertiary; Recombinant Fusion Proteins - metabolism; Selectins; Structure-Activity Relationship; Sulfoglycosphingolipids; Tumor Cells, Cultured; Human; Cell line; Mutagenesis; Cell cell interaction; Carbohydrate; Binding site; Neutrophil; Adhesion; Recognition
• ISSN: 0021-9525; 1540-8140
• DOI: 10.1083/jcb.120.5.1227

The selectins are a family of three calcium-dependent lectins that mediate adhesive interactions between leukocytes and the endothelium during normal and abnormal inflammatory episodes. Previous work has implicated the carbohydrate sialyl Lewis x ( sLe x; sialic acid alpha 2-3 galactose beta 1-4 [Fucose alpha 1-3] N-acetyl glucosamine) as a component of the ligand recognized by E- and P-selectin. In the case of P-selectin, other components of the cell surface, including 2′6-linked sialic acid and sulfatide (galactose-4-sulfate ceramide), have also been proposed for adhesion mediated by this selectin. We have recently defined a region of the E-selectin lectin domain that appears to be directly involved with carbohydrate recognition and cell adhesion (Erbe, D. V., B. A. Wolitzky, L. G. Presta, C. R. Norton, R. J. Ramos, D. K. Burns, R. M. Rumberger, B. N. N. Rao, C. Foxall, B. K. Brandley, and L. A. Lasky. 1992. J. Cell Biol. 119:215-227). Here we describe a similar analysis of the P-selectin lectin domain which demonstrates that a homologous region of this glycoprotein's lectin motif is involved with carbohydrate recognition and cell binding. In addition, we present evidence that is inconsistent with a biological role for either 2′6-linked sialic acid or sulfatide in P-selectin-mediated adhesion. These results suggest that a common region of the E- and P-selectin lectin domains appears to mediate carbohydrate recognition and cell adhesion.