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  • Title: Band 3 glycoprotein and glycophorin A from erythrocytes of children with congenital disorder of glycosylation type-Ia are underglycosylated.
    Author: Zdebska E, Musielak M, Jaeken J, Kościelak J.
    Journal: Proteomics; 2001 Feb; 1(2):269-74. PubMed ID: 11680873.
    Abstract:
    Band 3 and PAS-1 (a dimer of glycophorin A) from erythrocyte membranes of three children with congenital disorder of glycosylation, type Ia (CDG-Ia), aged 1 month, 3 years and 10 years respectively, were examined by a new technique that allowed determination of carbohydrate molar composition of glycoproteins separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis. In CDG children a single N-glycan of band 3 glycoprotein was hypoglycosylated and its mannose content was normal or elevated. Glycophorin A which is the major carrier of erythrocyte sialic acid, was deficient in N-acetylgalactosamine, and sialic acid residues. This finding indicated a partial unglycosylation of O-glycans in glycophorin A. In keeping with the results of PAS-1 analysis, total sialic acid in erythrocyte membranes from CDG children was reduced to 40-56% of normal values. A possible molecular mechanism of hypo- and unglycosylation of band 3 and glycophorin A, respectively, in CDG is discussed.
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