Con A- and WGA-binding glycoproteins of stationary and migratory corneal epithelium.

When stratified corneal rat epithelium becomes migratory in response to a wound, an increase in binding by the lectins concanavalin A (Con A) and wheat germ agglutinin (WGA) is seen. These lectins bind the membranes of the cells of the leading edge of the migrating sheet more intensely than normal epithelium and epithelium behind the leading edge, suggesting a change in cell surface properties during migration. In the present study, analysis of cell surface proteins using lactoperoxidase-catalyzed iodination followed by SDS-PAGE indicates the appearance of a 70 K protein in epithelium migrating to cover a wound. Con A-affinity chromatography shows that two bands, 70 K and 155 K, increase 4.0- and 2.9-fold, respectively, in epithelium that is migrating. WGA-binding glycoproteins increased 1.61-fold following wounding with the major band present at 155 K in SDS-PAGE. The data suggest that these glycoproteins are responsible for the increase in Con A and WGA binding to cell membranes in migratory corneal epithelium.