Differentiation of human erythroid cells is associated with increased O-glycosylation of the major sialoglycoprotein, glycophorin A.

Abstract

Glycophorin A, the major human erythrocyte sialoglycoprotein, is found exclusively on cells of the erythroid lineage. The amino acid sequence is known, and glycophorin A isolated from mature erythrocytes contains a single N-glycosidic and 15 O-glycosidic oligosaccharides. Monoclonal antibodies against erythrocyte glycophorin A reacted weakly with erythroid precursors, while a monospecific rabbit antiserum reacted strongly with immature and mature red cells. Glycophorin A was isolated from cells representing various stages of erythropoiesis in normal bone marrow, from blood cells of neonates with erythroblastosis fetalis, and from the erythroleukemic cell lines K562 and HEL before and after induced differentiation. Analysis of the oligosaccharides showed less O-glycosylation of glycophorin A in erythroid precursors. The degree of glycosylation increased concomitantly with differentiation.