Mapping of the rat liver endothelial membrane with lectins and glycosylated ferritins.

We explored the luminal surface of liver sinus endothelium for the presence of lectin receptors and lectinlike substances capable of interacting with specific sugars. We used ferritin-conjugated lectins and glycosylated ferritins as probes. Incubation of small blocks of rat liver with these probes led to the binding of concanavalin A (on A), Ricinus communis (RCA), wheat germ agglutinin (WGA), phytohemagglutinin (PHA) and mannosyl ferritins to the luminal surface of endothelium. Ulex europaeus agglutinin I (UEA), fucosyl, galactosyl, and chitobiosyl-ferritins did not bind. The binding was patchy and sparse in the case of Con A and mannosyl-ferritins but uniform for others. Binding density did not correlate with hemagglutinability of lectins, suggesting that the difference in the hemagglutinability of these lectins did not account for the difference in their binding densities. Bindings were all completely inhibited in the presence of excess specific sugar inhibitors, indicating the specificity of binding. The distribution of binding was segregated on the endothelial membrane, being heaviest on luminal pits. To define the functional significance of this segregated distribution, sinus endothelium was compared to portal-vein endothelium in which endothelial fenestrations are also seen; and these fenestrations as well as pits may be covered by a thin diaphragm. Of interest was the total absence of binding to the diaphragm. The significance of these findings is discussed.