Incomplete glycosylation of erythrocyte membrane proteins in congenital dyserythropoietic anaemia type II (CDA II).

The alterations in the erythrocyte membrane proteins of individuals with congenital dyserythropoietic anaemia (CDA II) were studied. Alterations were observed in both the erythrocyte sialoglycoproteins and erythrocyte anion transport protein (Band 3). There was a decrease in the apparent molecular weight of the major sialoglycoprotein alpha (glycophorin A) as well as a general reduction in the intensity of staining of all the sialoglycoproteins by the PAS stain. Sialoglycoprotein alpha isolated from CDA II erythrocytes contained 30% less sialic acid than normal alpha. The anion transport protein of CDA II erythrocytes migrated as a band with a lower molecular weight than the normal protein on SDS-gel electrophoresis. The CDA II anion transport protein had a substantially reduced content of N-acetylglucosamine and galactose, which probably reflects a reduction in the number of N-acetyl-lactosamine units carried by the protein. Our results suggest that there is a general defect in glycosylation of the major membrane glycoproteins of CDA II erythrocytes. We suggest that this glycosylation defect is a consequence of bone marrow stress.