Characterization of cell surface lectin-binding patterns of human airway epithelium

Glycosylated structures on the cell surface have a role in cell adhesion, m igration, and proliferation. Repair of the airway epithelium after injury r equires each of these processes, but the normal cell surface glycosylation of non-mucin producing airway epithelial cells is unknown. We examined cell surface glycosylation in human airway epithelial cells in tissue sections and in human airway epithelial cell lines in culture. Thirty-eight lectin p robes were used to determine specific carbohydrate residues by lectin-histo chemistry. Galactose or galactosamine-specific lectins labeled basal epithe lial cells, lectins specific for several different carbohydrate structures bound columnar epithelial cells, and fucose-specific lectins labeled all ai rway epithelial cells. The epithelial cell lines 1HAEo(-) and 16HBE14o(-) b ound lectins that were specific to basal epithelial cells. Flow cytometry o f these cell lines with selected lectins demonstrated that lectin binding w as to cell surface carbohydrates, and revealed possible hidden tissue antig ens on dispersed cultured cells. We demonstrate specific lectin-binding pat terns on the surface of normal human airway epithelial cells. The expressio n of specific carbohydrate residues may be useful to type epithelial cells and as a tool to examine cell events involved in epithelial repair.