Augmentation of galactose-specific glycoproteins during corneal epithelial migration in organ culture

The purpose of the present study was to identify galactose-specific glycoproteins that are synthesized in higher amounts or downregulated during the migratory process of corneal epithelium. Trichloroacetic-acid-precipitable proteins showed an increased incorporation of (3)H-galactose with time in migrating corneal epithelium in organ culture. Galactose oxidase treatment of immobilized 3-[(3-cholamidopropyl)dimethylamminio]-1-propanesulfonate-extractable glycoproteins of migrating and nonmigrating corneal epithelia resolved on sodium dodecylsulfate polyacrylamide gel electrophoresis was carried out. Two prominent terminally galactosylated protein bands (180 and 98 kD) were seen in the migrating epithelium but were absent in the nonmigrating epithelium. We conclude that during the migratory process of the corneal epithelium there is an increased utilization of galactose, and galactose-specific glycoproteins are synthesized in higher amounts.