Changes in the distribution of endothelial surface glycoconjugates associated with altered permeability of brain micro-blood vessels.

Lectin-binding sites located on the endothelial cell (EC) surfaces in unaltered, leaking and resorbing micro-blood vessels (MBVs) in cryo-injured cat brain were studied. Lectin or glycoprotein-gold complexes and brain samples embedded in hydrophilic resin Lowicryl K4M were used. The lectins tested recognize the following residues: beta-D-galactosyl (Ricinus communis agglutinin 120, RCA and peanut agglutinin, PNA), sialyl (Limax flavus agglutinin), N-acetyl-D-galactosaminyl (Helix pomatia agglutinin and soybean agglutinin, SBA), alpha-D-glucosyl and alpha-D-mannosyl (concanavalin A). The luminal front was labeled with SBA, and both fronts of the EC were labeled with PNA only after neuraminidase digestion. The most abundant and regularly distributed on both fronts of the EC were beta-D-galactosyl residues (RCA). These residues were also most affected in altered MBVs. The labeling of sialic acid residues was less pronounced on both sides of the EC. Following alteration of the function of the blood-brain barrier by cold-lesion injury, in leaking MBVs which represent increased luminal transport, we observed a conspicuous diminution of the labeling of the luminal surface of the EC with some lectins. On the other hand, in resorbing blood vessels located in the area of edema, where a presumably reverse (abluminal) transport occurs, major changes in the distribution of lectin-binding sites occurred on the abluminal front of the EC and in the basement membrane. The results reported here indicate that luminal and abluminal fronts of the EC change their properties in various functional conditions of MBVs, and that these changes can also be a reflection of functional polarity of brain endothelium.