Involvement of sialylated poly-N-acetyllactosaminyl sugar chains of band 3 glycoprotein on senescent erythrocytes in anti-band 3 autoantibody binding.
When young and senescent erythrocytes, separated from freshly collected human blood, were incubated with 125I-goat anti-human IgG, binding of the IgG to the senescent cells was three times as high as that to the young cells. The release of the radioactivity from the anti-human IgG-bound senescent cells was enhanced by incubation with band 3 oligosaccharides but not by those digested with endo-beta-galactosidase or neuraminidase. The senescent cells whose surface band 3 saccharide chains were cleaved by endo-beta-galactosidase or totally removed by N-glycosidase F showed decreased binding of the anti-human IgG. The radioactivity was effectively released from the anti-human IgG-bound senescent cells by digestion with endo-beta-galactosidase. The results suggest that senescent erythrocytes bind anti-band 3 autoantibody, and the antigenic sites on the cell surface are sialylated poly-N-acetyllactosaminyl sugar chains of band 3 glycoprotein.
Ando
K
K
Tokyo College of Pharmacy, Japan.
Kikugawa
K
K
Beppu
M
M
D001457:Anion Exchange Protein 1, Erythrocyte / Q000276:immunology*; D001323:Autoantibodies / Q000276:immunology*; D002240:Carbohydrate Sequence; D000939:Epitopes / Q000276:immunology; D004905:Erythrocyte Aging / Q000276:immunology*; D006801:Humans; D007074:Immunoglobulin G / Q000276:immunology; D008954:Models, Biological; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000276:immunology*; D011134:Polysaccharides / Q000276:immunology*
D001457:Anion Exchange Protein 1, Erythrocyte; D001323:Autoantibodies; D000939:Epitopes; D007074:Immunoglobulin G; D009844:Oligosaccharides; D011134:Polysaccharides; C016735:sialooligosaccharides; C037199:poly-N-acetyllactosamine