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.
Article| November 01 1982
Modification of cell surface glycoprotein: addition of fucosyl residues during epidermal differentiation.
J D Zieske
I A Bernstein
Online ISSN: 1540-8140
Print ISSN: 0021-9525
J Cell Biol (1982) 95 (2): 626–631.
J D Zieske, I A Bernstein; Modification of cell surface glycoprotein: addition of fucosyl residues during epidermal differentiation.. J Cell Biol 1 November 1982; 95 (2): 626–631. doi: https://doi.org/10.1083/jcb.95.2.626
Download citation file: