Modification of cell surface glycoprotein: addition of fucosyl residues during epidermal differentiation

When cutaneous sections from the newborn rat were treated with alpha-fucosidase, Ulex europeus agglutinin I (UEA) binding to the cell surface of the differentiated cells in the epidermis was diminished and there was an appearance in these cell layers of binding by Bandeiraea simplicifolia I-B4 lectin (BS I-B4), which normally is specific for the basal cells. A similar treatment with alpha-galactosidase resulted in a loss of BS I-B4 binding, but had no effect on UEA binding. Glycoproteins isolated from the membranes of epidermal cells showed a threefold increase in the ratio of binding to UEA versus BS I-B4 affinity columns as the proteins were derived from the more differentiated cell populations. These data suggest that alpha-fucosyl residues are added to the glycoproteins on the cell surfaces of differentiated cells, thus blocking alpha-galactosyl residues and changing the lectin binding specificity as epidermal cells move out of the basal cell layer.