Sulfatide-binding proteins.
Sulfatides (galactosyl ceramide-I3-sulfate) and other sulfated glycolipids are found in many tissues. The cell adhesion proteins laminin, thrombospondin, and von Willebrand factor bind specifically to sulfated glycolipids. Methods for characterizing the specificity of these interactions using surface-adsorbed glycolipids are reviewed. The three proteins do not bind to other anionic lipids, including gangliosides, phospholipids, or cholesterol 3-sulfate. Binding to sulfatides is saturable and of relatively high affinity. Relative binding avidity depends on the oligosaccharide structure of the glycolipids. Binding to sulfatides in erythrocyte membranes can account for the hemagglutinating activities of the three proteins and may play a role in the interactions of these proteins with other cell types.
D000818:Animals; D002448:Cell Adhesion; D002845:Chromatography; D006017:Glycolipids / Q000378:metabolism*; D006023:Glycoproteins / Q000378:metabolism*; D006801:Humans; D007797:Laminin / Q000378:metabolism*; D011485:Protein Binding; D019699:Thrombospondins; D014841:von Willebrand Factor / Q000378:metabolism*
D006017:Glycolipids; D006023:Glycoproteins; D007797:Laminin; D019699:Thrombospondins; C011117:sulfoglycolipids; D014841:von Willebrand Factor