title: Lectin binding sites in kidney. A comparative study of 14 animal species.
abstract: Six fluorochrome-coupled lectins with different sugar specificities were used to stain frozen tissue sections of kidneys from 14 animal species including mammals, avians, reptiles, and fresh water fish. Each lectin seemed to have a species-, but not strain-, specific binding pattern. Some lectins, however, bound to the same parts of the nephron in all animals studied. Wheat germ agglutinin (WGA) bound prominently to glomeruli in all kidneys. Dolichos biflorus agglutinin (DBA) seemed to bind to only a group of distal tubules in most animals, whereas either proximal or distal tubules were revealed with soybean (SBA) and peanut (PNA) agglutinins. Heterogeneity of basement membranes in different nephron parts was seen in the binding of some lectins. Ulex europeus agglutinin (UEA I), binding specifically to endothelial cells in human tissues, did not react with the endothelium of any other species, but SBA and PNA seemed to prominently stain vascular endothelia of cow and hen vessels, respectively. These results show a species-specific compartmentalization of saccharides to certain parts of the nephron, while there appears to be some common features in saccharide distribution between different animal species as well.
mesh_terms: D000818:Animals; D001665:Binding Sites; D006017:Glycolipids / Q000032:analysis*; D006023:Glycoproteins / Q000032:analysis*; D006801:Humans; D007668:Kidney / Q000032:analysis*; D037102:Lectins; D013045:Species Specificity
chemical_list: D006017:Glycolipids; D006023:Glycoproteins; D037102:Lectins