title: Studies on the structures of the Tm, Sj, M1, Can, Sext and Hu blood group antigens.
abstract: The Glycophorins (GPs = sialoglycoproteins) in erythrocyte membranes from various Black individuals, some of which exhibit the M1, Can, Sj, Tm, Sext and/or Hu antigens, and several Caucasian donors, including pooled fetal red cells, were studied. Using agglutination inhibition assays with GP fractions, GP fragments and chemically modified GPs as well as trypsin treatment of intact red cells, the antigens defined by anti-M1, anti-M+M1, anti-Can and anti-Tm sera were found to be located on the N-terminal tryptic peptide (T2, residues 1-31) of the major GP (GP A = MN sialoglycoprotein). Evidence was obtained that the N-terminal amino-acid residue, NeuNAc and/or (a) different sugar residue(s) are involved in the antigens. Amino-acid sequence and composition analyses excluded an amino-acid exchange within the N-terminal region (residues 1-31) of GP A. Carbohydrate analyses revealed the attachment of GlcNAc residues (up to about five, dependent on the strength of the above-mentioned antigens) to O-glycosidically linked oligosaccharides within the N-terminal portion (residues 1-31) of GP A. As judged from the carbohydrate compositions of peptides, the alteration of the O-glycosidic oligosaccharides is associated with a slight increase of the Gal and Fuc contents and a slight decrease of the NeuNAc level. Analyses of small, secondary cyanogen bromide and V8 proteinase peptides from the N-terminal region of GP A from Blacks, Caucasians and Caucasian fetal cells suggest that the variable attachment of small quantities of GlcNAc (about 0.03 to about 0.2 residues per peptide molecule) accounts, at least in part, for the polymorphisms detected by anti-Can and the original anti-Tm (serum Sheerin). Remarkably, the GlcNAc-containing O-glycosidic oligosaccharides occur only in small quantities, or not all at, within the positions 32-61 of GP A and the glycosylated domains of GP B and GP C.(ABSTRACT TRUNCATED AT 400 WORDS)
authors.affiliation: Abteilung für Transfusionswesen, Universitätskliniken Köln.
authors.forename: W
authors.initials: W
authors.lastname: Dahr
authors.forename: G
authors.initials: G
authors.lastname: Knuppertz
authors.forename: K
authors.initials: K
authors.lastname: Beyreuther
authors.forename: J J
authors.initials: JJ
authors.lastname: Moulds
authors.forename: M
authors.initials: M
authors.lastname: Moulds
authors.forename: S
authors.initials: S
authors.lastname: Wilkinson
authors.forename: C
authors.initials: C
authors.lastname: Capon
authors.forename: B
authors.initials: B
authors.lastname: Fournet
authors.forename: P D
authors.initials: PD
authors.lastname: Issitt
mesh_terms: D000117:Acetylglucosamine / Q000276:immunology / Q000378:metabolism; D000595:Amino Acid Sequence; D044383:Black People / Q000235:genetics; D002240:Carbohydrate Sequence; D004586:Electrophoresis; D004910:Erythrocyte Membrane / Q000276:immunology; D006021:Glycophorins / Q000276:immunology / Q000378:metabolism; D006023:Glycoproteins / Q000235:genetics / Q000276:immunology; D006801:Humans; D008951:MNSs Blood-Group System / Q000235:genetics / Q000276:immunology; D008969:Molecular Sequence Data; D019158:N-Acetylneuraminic Acid; D010455:Peptides / Q000276:immunology; D010641:Phenotype; D012794:Sialic Acids / Q000276:immunology / Q000378:metabolism; D044465:White People / Q000235:genetics
chemical_list: D006021:Glycophorins; D006023:Glycoproteins; D008951:MNSs Blood-Group System; D010455:Peptides; D012794:Sialic Acids; D019158:N-Acetylneuraminic Acid; D000117:Acetylglucosamine