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Incomplete glycosylation of erythrocyte membrane proteins in congenital dyserythropoietic anaemia Type II (CDA II)
Author(s) -
Mawby W. J.,
Tanner M. J. A.,
Anstee D. J.,
Clamp J. R.
Publication year - 1983
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1983.tb01257.x
Subject(s) - sialoglycoproteins , glycophorin , sialoglycoprotein , band 3 , glycosylation , glycoprotein , biochemistry , membrane protein , microbiology and biotechnology , chemistry , sialic acid , biology , membrane
S ummary . 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 α (glycophorin A) as well as a general reduction in the intensity of staining of all the sialoglycoproteins by the PAS stain. Sialoglycoprotein α isolated from CDA II erythrocytes contained 30% less sialic acid than normal α. 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.