Decreased glycosylation of band 3 and band 4.5 glycoproteins of erythrocyte membrane in congenital dyserythropoietic anaemia type II.
We report a study of HEMPAS erythrocyte membrane glycoproteins in relation to proteolytic digestion and surface labelling with galactose-oxidase/NaB[3H]4. The proteolytic digestion of band 3, the major intrinsic glycoprotein of the human erythrocyte membrane, reveals an abnormality in the outer glycosylated segment of this protein. 3H incorporation in band 3 and band 4.5 glycoproteins after treatment with galactose-oxidase/NaB[3H]4 is reduced in HEMPAS red cells suggesting a defective glycosylation of these proteins. These findings together with the persistence of i antigen and the normal presence of I antigen lead us to conclude that erythroblastic membrane features may persist in HEMPAS erythrocytes.
D000328:Adult; D000742:Anemia, Dyserythropoietic, Congenital / Q000097:blood*; D000745:Anemia, Hemolytic, Congenital / Q000097:blood*; D001894:Borohydrides / Q000378:metabolism; D002648:Child; D002918:Chymotrypsin / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D005692:Galactose Oxidase / Q000378:metabolism; D006023:Glycoproteins / Q000097:blood*; D006801:Humans; D014316:Tritium; D014357:Trypsin / Q000378:metabolism
D001894:Borohydrides; D006023:Glycoproteins; D014316:Tritium; C025364:sodium borohydride; D005692:Galactose Oxidase; D002918:Chymotrypsin; D014357:Trypsin