Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens

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Title: Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens
Author: Agre, P; Anstee, D J; Spring, F A; Preston, G M; Smith, B L
Abstract: Blood group antigens are structural variants in surface carbohydrate or amino acid polymorphisms on extracellular domains of membrane proteins. The red cell water channel-forming integral protein (Aquaporin CHIP) is a homotetramer with only one N-glycosylated subunit, however no CHIP-associated blood group antigens have yet been identified. Immunoblotting, monosaccharide composition analysis, and selective glycosidase digestions revealed that the CHIP-associated oligosaccharide contains ABH determinants and resembles a band 3-type glycan that cannot be cleaved from intact membranes by Peptide:N-glycosidase F. The molecular structure of the Colton antigens was previously unknown, but CHIP was selectively immunoprecipitated with anti-Coa or anti-Co(b). The DNA sequence from Colton-typed individuals predicted that residue 45 is alanine in the Co(a+b-) phenotype and valine in the Co(a-b+) phenotype. The nucleotide polymorphism corresponds to a PflMI endonuclease digestion site in the DNA from Co(a-b+) individuals. These studies have defined antigens within two blood group systems on CHIP: (a) an ABH-bearing polylactosaminoglycan attached to a poorly accessible site in the native membrane; and (b) the Colton antigen polymorphism which may permit the identification of rare individuals with defective water channel expression.
Date: 1994-09
Citation: J Clin Invest. 1994 September; 94(3): 1043–1049. doi: 10.1172/JCI117418
Subject: Oligosaccharides/chemistry
Ion Channels/chemistry
Ion Channels/blood
Erythrocyte Membrane/chemistry
ABO Blood-Group System/chemistry

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