Isolation of cDNA clones and complete amino acid sequence of human erythrocyte glycophorin C (original) (raw)
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Molecular Genetics of Human Erythrocyte Sialoglycoproteins Glycophorins A, B, C, and D
Blood Cell Biochemistry, 1990
Nomenclature and Properties of the Major Red Cell Membrane Glycoproteins Red cell membrane glycophorinsa Properties Synonyms Fairbanks et al. (1971) Dahr et al. (1975) Anstee et al. (1979) Blood group antigens PAS-positive material(%) Apparent molecular mass (kDa)h Copies/cell (X J0-3)c Polypeptide chain (residues) 0-linked sugar chains N-linked sugar chains Percent solubilized by Triton X
Antigenicity of rat erythrocyte glycophorins
Immunology Letters, 1988
The relationship between rat red blood cell (RBC) glycophorins and the antigens recognised by anti-rat RBC antibodies was examined. Initially, murine monoclonal antibodies specific for surface epitopes on whole rat RBCs were tested for their reactivity with RBC membranes on Western blots and two were found which reacted with blotted antigens. These antibodies recognised two bands corresponding to the major PAS-stainable bands of rat RBC membranes (i.e., the glycophorins) and a number of minor bands, thus demonstrating that the bands are antigenically related. This band-pattern was remarkably similar to that obtained with mouse anti-rat RBC serum. Digestion with neuraminidase altered the electrophoretic mobility of most of the bands, providing additional evidence that they are sialoglycoproteins, although sialic acid was shown not to contribute to their antigenicity. The glycophorin nature of the major antigens was verified by reelectrophoresis and blotting of bands excised from SDS gels, which showed that they were interconvertible monomeric and dimeric forms of the same polypeptide chain. It is suggested that rat RBC glycophorins are a related family of sialoglycoproteins with the high molecular weight members being formed by dimerization of five lower molecular weight polypeptide chains in various combinations.
Monoclonal antibodies specific for the M- and N-forms of human glycophorin A
Molecular Immunology, 1983
Four mouse monoclonal antibodies directed against the red cell membrane protein glycophorin A have been isolated and characterized. They are produced by hybridomas derived from SP2/0 myeloma cells and spleen cells from Biozzi mice immunized with a mixture of human erythrocytes from homozygous blood group M and N individuals. These antibodies recognize and bind to purified glycophorin A and to glycophorin on the red cell surface. All are of the IgGl, kappa light chain subclass and bind to determinants presented on the 39 amino acid, trypsin-sensitive, N-terminal peptide of glycophorin A. Three display differential specificities for the two allelic forms of glycophorin A; two are exquisitely specific for the M-form and one preferentially binds the N-form. Treatment of red cells with neuraminidase, which removes N-acetylneuraminic acid from glycophorin A, abolishes the binding of these three antibodies. The binding of the N-specific antibody is also sensitive to modification of the amino-terminal residue of the antigen. The fourth antibody binds equally well to both the M-and N-forms as well as to neuraminidase-treated red cells; thus it recognizes a public, N-acetylneuraminic acid independent glycophorin A determinant.
European Journal of Biochemistry, 1989
Correspondence to J.-P. Cartron, Unit& INSERM U76, INTS, 6. ruc Alexandre Cahancl, F-75015 Paris, France Ahhrevialions. GPA, glycophorin A; GPB, glycophorin B; NaCI/ Cit, 0.15 M NaCI/O.IS M trisodium citratc, pH 7.0; Mi.V, Miltcnberger class V variant with abnormal expression ofglycophorin genes; PCR, polymerase chain reaction.
Ultrastructure of a transmembrane glycoprotein, glycophorin A
Tissue and Cell, 1988
The major sialoglycoprotcin of the human red cell membrane, glycophorin A. wa isolated and examined by rotary shadowing and transmlssion electron microscopy. 'I hc glycophorin A molecule appeared as a cloud-like structure with a short. dense cow within a larpi: cloud. Mild acid hydrolysis in 0.05 M HISO,. 80°C for I hr reduced the ac ot the cloud significantly hut left the dense core intact indicatmg that the orlginal cloud reprcsentcd the sialylated oligosaccharide chains of glycophorin A wth the dense core being the polypeptide chain and its associated linkage proteins. Incubating glycophorin A with cationized fcrrnin (Cl-') revealed that the CF was bound only to the cloud. a finding that supports the view that the clotld is comprised of the sialylated ohgosaccharide chains of the glycophorm A molecule SDSpolyacrylamide gel electrophoresis revealed that our preparation of glycophorin A. a\ well a\ commeraal preparations, consisted of monomers, dimera and ohgomers of glycophorin A wth trace amounts of the minor glycophorins and lmkage proteins. Knowledge of the ultraatructulc of this important integral protein will enable one to design studies to dcterminc its functional role in the membrane.
Localization of the gene for human erythrocyte glycophorin C to chromosome 2, q14–q21
Human Genetics, 1986
A complementary cDNA clone (900 bp) representing the 3′ untranslated region and almost the entire coding sequence of the human erythrocyte membrane glycophorin C has been used to determine the chromosomal location of the blood group Gerbich locus by in situ hybridization. The results indicate that this locus is assigned to the region q14–q21 of chromosome 2.
Identification of the Blood-Group ABH-Active Glycoprotein Components of Human Erythrocyte Membrane
European Journal of Biochemistry, 1980
The blood-group ABH-active components of the erythrocyte membrane were identified by incubation of polyacrylamide gels after electrophoresis with radio-iodinated blood-group-specific lectins. The anti-A and anti-B lectin of Bandeiraea simplicijoliu bound to components from A1, AB and B erythrocytes but not A2 or 0 erythrocytes, whereas the opposite was observed for the anti-H lectin of Lotus tetragonolobus. Both lectins revealed as major blood-group-active components band 3 and the region of band 4.5, which was resolved into at least two components. Smaller amounts of the lectins were bound to the low-molecular-weight region and the dye front, which contained the poly(glycosy1)ceramides. In addition to these components, the B. simplicifolia lectin also bound to the sialoglycoprotein bands 1 and 2 (stained with periodic acid/SchifT). The distribution of bound radioactivity, as determined with this lectin was: Band 3, 22-25 %; HI04/Schiff band-1, 10-15 %; band 4.5, 34-37 %; HI04/Schiff band-2, 12-15 x ; and the poly(glycosy1)ceramide region, 14-17 %. The different lectin-binding properties indicate a structural difference between the antigenic determinants of the sialoglycoproteins and of the other blood-group-active components. It is suggested that the antigenic determinants in the sialoglycoproteins are of the alkali-labile type previously characterized, and that the carbohydrate chains of bands 3 and 4.5 correspond to the previously isolated alkali-stable poly(glycosy1)peptides. The detection of two different groups of glycoproteins could thus explain the controversy concerning the nature of the blood-group ABH antigens in glycoproteins of the erythrocyte membrane. The blood-group ABH antigenic determinants of the erythrocyte membrane are known to occur both in glycolipids [l-61 and glycoproteins [7-181. The molecular nature of the glycolipids has been unequivocally established by the isolation and characterization of individual blood-group active molecules. The molecular nature of the protein-bound ABH antigens is still, however, not clear. By the approach of extraction and isolation of individual glycoproteins, the antigens have been associated with different sialoglycoprotein-bands of the erythrocyte membrane [9,11,12,14].