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.
D000818:Animals; D002454:Cell Differentiation; D002469:Cell Separation; D000078404:Epidermal Cells; D004817:Epidermis / Q000378:metabolism; D005643:Fucose / Q000378:metabolism*; D006023:Glycoproteins / Q000302:isolation & purification / Q000378:metabolism*; D037102:Lectins; D008565:Membrane Proteins / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats; D000519:alpha-Galactosidase / Q000494:pharmacology; D005644:alpha-L-Fucosidase / Q000494:pharmacology
D006023:Glycoproteins; D037102:Lectins; D008565:Membrane Proteins; D005643:Fucose; D000519:alpha-Galactosidase; D005644:alpha-L-Fucosidase