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Antigenic Properties of Human Erythrocyte Glycophorins

  • Elwira Lisowska
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 228)

Abstract

The name of glycophorin was given by Marchesi et al. (1972) to the major sialoglycophorin of human erythrocyte membranes, known earlier as the glycoprotein carrying blood group M and N determinants and receptors for agglutinins of influenza viruses (Baranowski et al., 1959; Romanowska 1959; Klenk & Uhlenbruck, 1960; Kathan et al., 1961; Springer et al., 1966). Fractionation of the erythrocyte membranes by sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and visualization of sialoglycoproteins with periodic acid-Schiff (PAS) reagent give a complex pattern of bands which may differ in details, depending on electro- phoretic conditions. It has been now accepted that there are at least four distinct sialoglycoproteins in human erythrocyte membranes. Furthmayr et al. (1975) designated three of them as glycophorin A, B and C, in order of their decreasing amount in the membrane. Anstee et al. (1979) denoted them glycoprotein α, β, γ and δ, in order of their decreasing molecular weight. Dahr et al. (1978c) used other designations. The more numerous bands seen in SDS-PAGE correspond to monomers of the sialoglycoproteins and to homo- and heterodimers (and higher oligomers) formed by the most abundant glycophorins A and B (Fig. 1).

Keywords

Blood Group Human Erythrocyte Sialic Acid Residue Blood Group Antigen Oligosaccharide Chain 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Adamany, A.M., Blumenfeld, O.O., Sabo, B. and McCreary, J. (1983): A carbohydrate structural variant of MM glycoprotein (glycophorin A). J. Biol. Chem. 258:11537–11545.PubMedGoogle Scholar
  2. Adams, J., Broviac, M., Brooks, W., Johnson, N.R. and Issitt, P.D. (1971): An antibody in the serum of a Wr(a+) individual reacting with an antigen of very high frequency. Transfusion 11:290–291.PubMedGoogle Scholar
  3. Allen, R.W., Nunley, N., Kimmeth, M.E. Wallhermfechtel, M., and Vengelen-Tyler, V (1984): Isolation and serological characterization of a monoclonal antibody recognizing the N blood group antigen. Transfusion 24:136–140.PubMedGoogle Scholar
  4. Alloisio, N., Morlè, L., Bachir, D., Guertani, D., Colonna, P., and Delaunay J. (1985): Red cell membrane sialoglycoprotein β in homozygous and heterozygous 4.1(-) hereditary elliptocytosis. Biochem. Biophys. Acta 816:57–62.PubMedGoogle Scholar
  5. Anderson, L.C., Gahmberg, C.G., Teerenhovi, L. and Vuopio, P. (1979): Glycophorin A as a cell surface marker of early erythroid differentiation in acute leukemia. Int. J. Cancer 24:717–720.Google Scholar
  6. Anstee, D.J. and Edwards, P.A.W. (1982): Monoclonal antibodies to human erythrocytes. Eur. J. Immunol. 12:228–232.PubMedGoogle Scholar
  7. Anstee, D.J. and Tanner, M.J.A. (1975): Separation of ABH, I, Ss antigenic activity from the MN-active sialoglyco- protein of the human erythrocyte membrane. Vox Sang. 29:378–389.PubMedGoogle Scholar
  8. Anstee, D.J. and Tanner, M.J.A. (1978): Genetic variants involving the major membrane sialoglycoprotein of human erythrocytes. Studies on erythrocytes of type Mk, Mitenberger class V and MS. Biochem. J. 175:149–157.PubMedGoogle Scholar
  9. Anstee, D.J., Barker, D.M., Judson, P.A. and Tanner, M.J.A. (1977): Inherited sialoglycoprotein deficiencies in human erythrocytes of type En(a-). Brit. J. Haemat. 35:309–320.PubMedGoogle Scholar
  10. Anstee, D.J., Mawby, W.J. and Tanner, M.J.A. (1979): Abnormal blood group Ss-active sialoglycoproteins in the membrane of Miltenberger class III, IV and V human erythrocytes. Biochem. J. 183: 193–203.PubMedGoogle Scholar
  11. Anstee, D.J., Mawby, W.J., Parsons, S.F., Tanner, M.J.A. and Giles, C.M. (1982a): A novel hybrid sialoglycoprotein in Sta-positive human erythrocytes. J. Immunogenet. 9:51–55.PubMedGoogle Scholar
  12. Anstee, D.J., Mawby, W.J. and Tanner, M.J.A. (1982b): Structural variation in human erythrocyte sialoglycoproteins. Membranes and Transport, Martonosi, A.N., ed., Plenum Press, New York, NY, pp. 427–433.Google Scholar
  13. Anstee, D.J., Parsons, S.F., Ridgwell, K., Tanner, M.J.A., Merry, A.H., Thomson, E.E., Judson, P.A., Johnson, P., Bates, S. and Fraser, I.D. (1984a): Two individuals with elliptocytic red cells apparently lack three minor erythrocyte membrane sialoglycoproteins. Biochem. J. 218:615–619.PubMedGoogle Scholar
  14. Anstee, D.J., Ridgwell, K., Tanner, M.J.A., Daniels, G.L. and Parsons, S.F. (1984b): Individuals lacking the Gerbich blood group antigen have alterations in the human erythrocyte membrane sialoglycoproteins β and γ. Biochem. J. 221:97–104.PubMedGoogle Scholar
  15. Baranowski, T. and Lisowska, E. (1963): Studies on blood group antigens M and N. VIII. Fractionation of the products of proteolytic digestion. Arch. Immunol. Ther. Exp. 11:631–640.Google Scholar
  16. Baranowski, T., Lisowska, E., Morawiecki, A., Romanowska, E. and Strozecka, K. (1959): Studies on blood group antigens M and N. III. Chemical composition of purified antigens. Arch. Immunol. Ther. Exp. 7:15–27.Google Scholar
  17. Barsoum, A.L., Czuczman, M.S., Bhavanandan, V.P. and Davidson, E.A. (1984): Epitopes immunologically related to glyco- phorin A on human malignant and nonmalignant cells in culture. Int. J. Cancer 34:789–795.PubMedGoogle Scholar
  18. Barsoum, A.L., Bhavanandan, V.P. and Davidson, E. A. (1985): Monoclonal antibodies to cyanogen bromide fragments of glycophorin A. Mol. Immunol. 22:361–367.PubMedGoogle Scholar
  19. Berger, E.G. and Kozdrowski, I. (1978): Permanent mixed-field polyagglutinable erythrocytes lack galactosyltransferase activity. FEBS Lett. 93:105–108.PubMedGoogle Scholar
  20. Bigbee, W.L., Vanderlaan, M., Fong, S.S.N, and Jensen, R.H. (1983): Monoclonal antibodies specific for the M- and N- forms of human glycophorin A. Mol. Immunol. 20:1353–1362.PubMedGoogle Scholar
  21. Bigbee, W.L., Langlois, R.G., Vanderlaan, M. and Jensen, R.H. (1984): Binding specificities of eight monoclonal antibodies to human glycophorin A - studies with MCM, and MkEn(UK) variant human erythrocytes and M- and MNv-type chimpanzee erythrocytes. J. Immunol. 133:314 9–3155.Google Scholar
  22. Blanchard, D., Cartron, J. P., Rouger, P. and Salmon, C. (1982): Pj variant, a new hybrid MNSs glycoprotein of the human red cell membrane. Biochem. J. 203:419–426.Google Scholar
  23. Blanchard, D., Cartron, J.P., Fournet, B., Montreuil, J., van Halbeek, H. and Vliegenthart, J.F.G. (1983): Primary structure of the oligosaccharide determinant of blood group Cad specificity. J. Biol. Chem. 258:7691–7695.PubMedGoogle Scholar
  24. Blumenfeld, O.O. and Adamany, A.M. (1978): Structural polymorphism within the amino-terminal region of MM, NN and MN glycoproteins (glycophorins) of the human erythrocyte membrane. Proc. Natl. Acad. Sci. USA 75:2727–2731.PubMedGoogle Scholar
  25. Blumenfeld, O.O., Adamany, A.M. and Puglia, K.V. (1981): Amino acid and carbohydrate structural variants of glycoprotein products (M-N glycoproteins) of the M-N allelic locus. Proc. Natl. Acad. Sci. USA 78:747–751.PubMedGoogle Scholar
  26. Bunn, H.F. and Higgins, P.J. (1981): Reaction of monosaccharides with proteins: possible evolutionary significance. Science 213:222–224.PubMedGoogle Scholar
  27. Carlsson, S.R. and Fukuda, M. (1985): Isolation and characterization of leukosialin, the major cell surface sialo- glycoprotein on human leukocytes, and demonstration of its cell specific glycosylation. Glycoconjugates, Proc. Vlllth Intern. Symp. (Houston, TX.), pp. 540–541.Google Scholar
  28. Carter, D.R., Hardy, E.R., Lannom, H.K., Dill, K., Ferrari, B. and Pavia, A.A. (1984): 13C n.m.r. study of the pH behavior of N-methylated peptides related to the NH2-terminus of glycophorins. Int. J. Biol. Macromol. 6:348–352.Google Scholar
  29. Cleghorn, T.E. (1962): Two human blood group antigens Sta(Stones) and Ria(Ridley) closely related to the MNSs blood group system. Nature (London) 195:895.Google Scholar
  30. Cleghorn, T.E. (1966): A memorandum on the Miltenberger blood groups. Vox Sang. 11:219–222.PubMedGoogle Scholar
  31. Colin, Y., Rahuel, C., London, J., Romeo, P.H., d’Auriol, L., Galibert, F. and Cartron, J.P. (1986) Isolation of cDNA clones and complete amino acid sequence of human erythrocyte glycophorin C. J. Biol. Chem. 261: 229–233.PubMedGoogle Scholar
  32. Contreras, M., Green, C., Humphreys, J., Tippett, P., Daniels, G., Teesdale, P., Armitage, S. and Lubenko, A. (1984): Serology and genetics of MNSs-associated antigen Dantu. Vox Sang. 46:377–386.PubMedGoogle Scholar
  33. Dahr, W. (1981): Serology, genetics and chemistry of the MNSs blood group system. Blood Transf. Immunohaemat. 24:85–95.Google Scholar
  34. Dahr, W. (1983): Biochemical studies of erythrocyte membrane glycoprotein variants. In Red Cell Membrane Glycoconjugates and Related Genetic Markers, Cartron, J.P., Rouger, P. and Salmon, C., eds., Librairie Arnette, Paris, pp. 27–36.Google Scholar
  35. Dahr, W. and Beyreuther, K. (1985) A revison of the N-terminal structure of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes. Biol. Chem. Hoppe Seyler 366: 1067.PubMedGoogle Scholar
  36. Dahr, W. and Moulds, J. (1981): An immunochemical study on anti-N antibodies from dialysis patients. Immunol. Commun. 10:173–183.PubMedGoogle Scholar
  37. Dahr, W. and Uhlenbruck, G. (1978): Structural properties of the human M and N blood group system antigen receptor sites. Hoppe-Seyler’s Z. Physiol. Chem. 359:835–843.PubMedGoogle Scholar
  38. Dahr, W., Uhlenbruck, G. and Bird, G.W.G. (1975a): Influence of free amino and carboxyl groups on the specificity of plant anti-N. Vox Sang. 28:389–391.PubMedGoogle Scholar
  39. Dahr, W., Uhlenbruck, G., Gunson, H.H. and van der Hart, M. (1975b): Molecular basis of Tn polyagglutinability. Vox Sang. 29:36–50.PubMedGoogle Scholar
  40. Dahr, W., Uhlenbruck, G., Issitt, P. and Allen, F.H. (1975c): SDS-polyacrylamide gel electrophoretic analysis of the membrane glycoproteins from S-s-U- erythrocytes. J. Immunogenet. 2: 24 9–251.Google Scholar
  41. Dahr, W., Uhlenbruck, G. and Knott, H. (1975d): Immunochemical aspects of the MNSs blood group system. J. Immunogenet. 2:87–100.Google Scholar
  42. Dahr, W., Uhlenbruck, G., Leikola, J., Wagstaff, W. and Landfried, K. (1976a): Studies on the membrane glycoprotein defect of En(a-) erythrocytes. I. Biochemical aspects. J. Immunogenet. 3:329–346.PubMedGoogle Scholar
  43. Dahr, W., Uhlenbruck, G., Wagstaff, W. and Leikola, J. (1976b): Studies on the membrane glycoprotein defect of En(a-) erythrocytes. II. MN antigenic properties of En(a-) erythrocytes. J. Immunogenet. 3:383–394.PubMedGoogle Scholar
  44. Dahr, W., Uhlenbruck, G., Janssen, E. and Schmalisch R. (1977a): Different N-terminal amino acids in the MN glycoprotein from MM and NN erythrocytes. Human Genet. 35:335–343.Google Scholar
  45. Dahr, W., Uhlenbruck, G. and Knott, H. (1977b): The defect of Mk erythrocytes as revealed by sodium dodecysulfate polyacrylamide gel electrophoresis. J. Immunogenet. 4:191–200.PubMedGoogle Scholar
  46. Dahr, W., Issitt, P., Moulds, J. and Pavone, B. (1978a): Further studies on the membrane glycoprotein defects of S-s- and En(a-) erythrocytes. Hoppe-Seyler’s Z. Physiol. Chem. 359:1217–1224.Google Scholar
  47. Dahr, W., Longster, G., Uhlenbruck, G. and Schumacher, K. (1978b): Studies on Miltenberger class III, V, Mv and Mk red cells. I. Sodium dodecylsulfate polyacrylamide gel electrophoretic investigations. Blut 37:129–138.PubMedGoogle Scholar
  48. Dahr, W., Uhlenbruck, G., Leikola, J. and Wagstaff, W. (1978c): Studies on the membrane glycoprotein defect of En(a-) erythrocytes. III. N-terminal amino acids of sialoglycoproteins from normal and En (a-) red cells. J. Immunogenet. 5:117–127.PubMedGoogle Scholar
  49. Dahr, W., Gielen, W., Beyreuther, K. and Kruger, J. (1980a): Structure of the Ss blood group antigens. I. Isolation of Ss-active glycopeptides and differentiation of the antigens by modification of methionine. Hoppe-Seyler’s Z. Physiol. Chem. 361:145–152.PubMedGoogle Scholar
  50. Dahr, W., Beyreuther, K., Steinbach, H., Gielen, W. and Krüger, J. (1980b): Structure of the Ss blood group antigens. II. A methionine/threonine polymorphism within the N-terminal sequence of the Ss glycoprotein. Hoppe- Seyler’s Z. Physiol. Chem. 361:895–906.Google Scholar
  51. Dahr, W., Beyreuther, K., Gallasch, E., Krüger, J. and Morel, P. (1981a): Amino acid sequence of the blood group Mg- specific major human erythrocyte membrane sialogly- coprotein. Hoppe-Seyler’s Z. Physiol. Chem. 362:81–85.Google Scholar
  52. Dahr, W., Kordowicz, M., Beyreuther, K. and Krüger, J. (1981b): The amino acid sequence of the Mc-specific major red cell membrane sialoglycoprotein- an intermediate of the blood group M- and N-active molecules. Hoppe-Seyler’s Z. Physiol. Chem. 362:363–366.Google Scholar
  53. Dahr, W., Beyreuther, K., Kordowicz, M. and Krüger, J. (1982): N-terminal amino acid sequence of siologlycoprotein D. (glycophorin C) from human erythrocyte membranes. Eur. J. Biochem. 125:57–62.PubMedGoogle Scholar
  54. Dahr, W., Kordowicz, M., Judd, W.J., Moulds, J., Beyreuther, K. and Krüger, J. (1984a): Structural analysis of the Ss sialoglycoprotein specific for Henshaw blood group from human erythrocyte membranes. Eur. J. Biochem. 141:51–55.PubMedGoogle Scholar
  55. Dahr, W., Newman, R.A., Contreras, M., Kordowicz, M., Teesdale, P., Beyreuther, K. and Krüger, J. (1984b): Structures of Miltenberger class I and II specific human erythrocyte membrane glycoproteins. Eur. J. Biochem. 138:259–265.PubMedGoogle Scholar
  56. Dahr, W., Moulds, J., Baumeister, G., Moulds, M., Kiedrowski, S. and Hummel, M. (1985a): Altered membrane sialoglyco- proteins in human erythrocytes lacking the Gerbich blood group antigens. Biol. Chem. Hoppe-Seyler 366:201–211.PubMedGoogle Scholar
  57. Dahr, W., Müller, T., Moulds, J., Baumeister, G., Issitt, P.D., Wilkinson, S. and Garratty, G. (1985b): High frequency antigens of human erythrocyte membrane sialo- glycoproteins. I. Ena receptors in the glycosylated domain of the MN sialoglycoprotein. Biol. Chem. Hoppe- Seyler 366:41–51.PubMedGoogle Scholar
  58. Dahr, W., Blanchard, D., Hummel, M., Cartron, J.P. and Beyreuther, K. (1985c): Preparative purification of the Ss and D sialoglycoproteins (glycophorins B and C) from human erythrocyte membranes by high performance liquid chromatography and amino acid sequence analysis of their intramembranous domains. Glycoconjugates, Proc. VIIIth Intern. Symp. (Houston, TX.), pp.21–22.Google Scholar
  59. Dahr, W., Moulds, J., Unger, D., Blanchard, D. and Cartron, J.P. (1985d): Structural analysis and properties of a blood group Dantu-active hybrid sialoglycoprotein (glycophorin) from human red cell membranes. Glycocon jugates, Proc. Vlllth Intern. Symp. (Houston, TX.), pp. 543–544.Google Scholar
  60. Darnborough, H., Dunsford, I. and Wallace, J.A. (1969): The Ena antigen and antibody. A genetical modification of human red cells affecting their blood grouping reactions. Vox Sang. 17:241–255.PubMedGoogle Scholar
  61. Drzeniek, Z. (1983): Purification of antibody reacting with nonenzymatically glycosylated blood group M determinants. Immunol. Lett. 6:179–183.PubMedGoogle Scholar
  62. Drzeniek, Z., Kusnierz, G. and Lisowska, E. (1981): A human antiserum reacting with modified blood group M determinants. Immunol. Commun. 10:185–197.PubMedGoogle Scholar
  63. Dybkjaer, E., Poole, J. and Giles, C.M. (1981): A new Miltenberger class detected by a second example of Anek type serum. Vox Sang. 41:302–305.PubMedGoogle Scholar
  64. Ebert, W., Met z, J. and Roelcke, D. (1972): Modification of N-acetylneuraminic acid and their influence on the antigen reactivity of erythrocyte glycoproteins. Eur. J. Biochem. 27: 470–472;PubMedGoogle Scholar
  65. Edelman, L., Blanchard, D., Rouger, P., Doinel, C., Cartron, J.P., Salmon, C. and Reviron, J. (1984): A monoclonal antibody directed against the homologous N-terminal domain of glycophorin A and B, Exp. Clin. Immunogenet. 1:129–139.Google Scholar
  66. Edwards, P.A.W. (1980): Monoclonal antibodies that bind to the human erythrocyte membrane glycoproteins glycophorin A and Band 3. Biochem. Soc. Trans. 8:334–335.PubMedGoogle Scholar
  67. Fairbanks, G., Steck, T.L. and Wallach, D.F.H. (1971): Electrophoretic analysis of human erythrocyte membrane. Biochemistry 10:2606–2616.PubMedGoogle Scholar
  68. Fletcher, A. and Harbour, C. (1984): An interesting monoclonal anti-N produced following immunization with human group Or NN erythrocytes. J. Immunogenet. 11:121–126.PubMedGoogle Scholar
  69. Fraser, R.H., Munro, A.C., Williamson, A.R., Barrie, E.K., Hamilton, E.A. and Mitchell, R. (1982): Mouse monoclonal anti-N. I. Production and serological characterization. II. Physicochemical characterization and assessment for routine blood grouping. J. Immunogenet. 9:295–309.PubMedGoogle Scholar
  70. Fraser, R.H., Inglis, G., Mackie, A., Munro, A.C., Alia, E.K., Mitchell, R., Sonneborn, H.H. and Uthemann, H. (1985): Mouse monoclonal antibodies reacting with M blood group- related antigens. Transfusion 25:261–266.PubMedGoogle Scholar
  71. Fujita, S. and Cleve, H. (1975): Isolation and partial characterization of two minor glycoproteins from human erythrocyte membranes. Biochim. Biophys. Acta 382:172–180.PubMedGoogle Scholar
  72. Furthmayr, H. (1978): Structural comparison of glycophorins and immunochemical analysis of genetic variants. Nature (London) 271:519–524.Google Scholar
  73. Furthmayr, H., Tomita, M. and Marchesi, V.T. (1975): Fractionation of the major sialoglycopeptides of the human red cell membrane. Biochem. Biophys. Res. Commun. 65:113–121.PubMedGoogle Scholar
  74. Furthmayr, H., Metaxas, M.N. and Metaxas-Buhler, M. (1981): Mg and Mc: mutations within the amino terminal region of glycophorin A. Proc. Natl. Acad. Sci. USA 78:631–635.PubMedGoogle Scholar
  75. Furuhjelm, U., Meyllyla, G., Nevanlinna, H.R., Nordling, S., Pirkola, A., Gavin, J., Gooch, A., Sanger, R. and Tippett, P. (1969): The red cell phenotype En(a-) and anti-Ena: serological and physicochemical aspects. Vox Sang. 17:256–278.PubMedGoogle Scholar
  76. Gahmberg, C.G., Myllyla, G., Leikola, J., Pirkola, A. and Nordling, S. (1976): Absence of the major sialoglycoprotein in the membrane of human En(a-) erythrocytes and increased glycosylation of Band 3. J. Biol. Chem. 251:6108–6116.PubMedGoogle Scholar
  77. Gahmberg, C.G., Jokinen, M. and Anderson, L.C. (1979): Expression of the major red cell sialoglycoprotein, glycophorin A, in the human leukemic cell line K562. J. Biol. Chem. 254: 7442–7448.PubMedGoogle Scholar
  78. Gahmberg, C.G., Ekblom, M. and Anderson, L.C. (1984): Differentiation of human erythroid cells is associated with increased glycosylation of the major sialoglycoprotein, glycophorin A. Proc. Natl. Acad. Sci. USA 81:6752–6756.PubMedGoogle Scholar
  79. Greaves, M.F., Sieff, C. and Edwards, P.A.W. (1983): Monoclonal antiglycophorin as a probe for erythroleukemias. Blood 61:645–651.PubMedGoogle Scholar
  80. Hanisch, F.G., Farrar, G.H., Schmalisch, R. and Uhlenbruck, G. (1983): Immunochemistry of O-glycosidically-linked Gal (β1–3) GalNAc on fragments of human glycophorin A. Immunobiology 165:147–160.PubMedGoogle Scholar
  81. Herkt, F., Párente, J.P., Leroy, Y., Fournet, B., Blanchard, D., Cartron, J.P., van Haibeek, H. and Vliegenthart, J.F.G. (1985): Structure determination of oligosaccharides isolated from Cad erythrocyte membranes by permethylation analysis and 500 MHZ 1H-NMR spectroscopy. Eur. J.Biochem. 146:125–129.PubMedGoogle Scholar
  82. Huprikar, S.V. and Springer, G.F. (1970): Structural aspects of human blood group M and N specificity. In Blood and Tissue Antigen’s Aminoff, D., ed., Academic Press, New York-London, PP. 327–335.Google Scholar
  83. Irimura, T., Tsuji, T., Tagami, S., Yamamoto, K. and Osawa, T. (1981): Structure of a complex type sugar chain of human glycophorin A. Biochemistry 20:560–566.PubMedGoogle Scholar
  84. Issitt, P.D. (1981): The MN blood group system, Montgomery Scientific Publications, Cincinnati, OH.Google Scholar
  85. Issitt, P.D. and Wilkinson, S.L. (1983): Further studies on the dependence of some examples of anti-M and anti-N on the presence of red cell-borne sialic acid. Transfusion 23:117–119.PubMedGoogle Scholar
  86. Issitt, P.D., Pavone, B.G., Goldfinger, D. and Zwicker, H. (1975): An En (a-) red cell sample that types as Wr(a-b-). Transfusion 15:353–355.PubMedGoogle Scholar
  87. Issitt, P.D., Pavone, B.G., Wagstaff, W. and Goldfinger, D. (1976): The phenotypes En (a-), Wr(a-b-) and En(a+), Wr(a+b+), and further studies on the Wright and En blood group systems. Transfusion 15:396–407.Google Scholar
  88. Issitt, P.D., Daniels, G. and Tippet, P. (1981): Proposed new terminology for Ena. Transfusion 21:473.PubMedGoogle Scholar
  89. Judd, W.J., Issitt, P.D., Pavone, B.G., Anderson, J. and Aminoff, D. (1979): Antibodies that define NANA- independent MN-system antigens. Transfusion 10:12–18.Google Scholar
  90. Judd, W.J., Geisland, J.R., Issitt, P.D., Wilkinson, S.L., Anstee, D.J., Shin, C. and Glidden, H. (1983): Studies on the blood of an Miv/Mk proposita and her family. Transfusion 23:33–36.PubMedGoogle Scholar
  91. Kathan, R.H., Winzler, R.J. and Johnson, C.A. (1961): Preparation of an inhibitor of viral hemagglutination from human erythrocytes. J. Exp. Med. 113:37–45.PubMedGoogle Scholar
  92. Klenk, E. and Uhlenbruck, G. (1960): Uber neuraminsäure- haltige Mucoide aus Menschenerythrozytenstroma: ein Bietrag zur Chemie der Agglutiriogene. Hoppe-Seyler’s Z. Physiol. Chem. 319:151–160.Google Scholar
  93. Kordowicz, M. and Lisowska, E. (1978): Antisera against polypeptide chains derived from M and N blood group glycoproteins. Arch. Immunol. Ther. Exp. 26:145–149.Google Scholar
  94. Langley, J.W., Issitt, P.D., Anstee, D.J., McMahan, M., Smith, N., Pavone, B.G., Tessel, J.A. and Carlin, M. A. (1981): Another individual (J.R.) whose red blood cells appear to carry a hybrid MNSs sialoglycoprotein. Transfusion 21:15–24.PubMedGoogle Scholar
  95. Langlois, R.G., Bigbee, W.L. and Jensen, R.H. (1985): Flow cytometric characterization of normal and variant cells with monoclonal antibodies specific for glycophorin A. J. Immunol. 134:4009–4017.PubMedGoogle Scholar
  96. Levene, C., Sela, R., Lacser, M., BarShany, S., Giles, C.M. and Poole, J. (1984): Further examples of human anti-Me found in sera of Israeli donors. Vox Sang. 46:207–210PubMedGoogle Scholar
  97. Liao, T.H., Gallop, P.M. and Glumenfeld, O.O. (1973): Modification of sialyl residues of sialoglycoprotein(s) of the human erythrocyte surface. J. Biol. Chem. 258:8247–8253.Google Scholar
  98. Lisowska, E. (1977): Chemistry of M and N blood group antigens. In Clinical Laboratory Science, Seligson, D., ed., Section D:Blood Banking, Vol. I, Greenwalt, T. J. and Steane, E.A., eds., CRC Press Inc., Cleveland, OH. pp. 281–299.Google Scholar
  99. Lisowska, E. (1981): Biochemistry of M and N blood group specificities. Blood Transf. Immunohaemat. 24:75–84.Google Scholar
  100. Lisowska, E. and Duk, M. (1972): The reaction of products of sequential periodate oxidation of human erythrocyte glycoproteins with hemagglutinin fromHelix pomatia. Arch. Immunol. Ther. Exp. 20:869–875.Google Scholar
  101. Lisowska, E. and Duk, M. (1975a): Effect of modification of amino groups of human erythrocytes on M, N and Nvg blood group specificities. Vox Sang. 28:392–397.PubMedGoogle Scholar
  102. Lisowska, E. and Duk, M. (1975b): Modification of amino groups of human erythrocyte glycoproteins and the new concept on the structural basis of M and N blood group specificity. Eur. J. Biochem. 54:469–474.PubMedGoogle Scholar
  103. Lisowska, E. and Duk, M. (1976): The effect of gradual mild acid hydrolysis on serological activities of glycoproteins from human erythrocytes. Arch. Immunol. Ther. Exp. 24:39–45.Google Scholar
  104. Lisowska, E. and Jeanloz, R.W. (1973): Composition and distribution of carbohydrate chains in glycoproteins of human erythrocyte membrane. Carbohyd. Res. 29:181–191.Google Scholar
  105. Lisowska, E. and Kordowicz. (1977a): Specific antibodies for desialized M and N blood group antigens. Vox Sang. 33:164–169.PubMedGoogle Scholar
  106. Lisowska, E. and Kordowicz, M. (1977b): Immunochemical properties of M and N blood group antigens and their degradation products. In Human Blood Groups, Mohn, F., ed., Karger, Basel, pp. 188–196.Google Scholar
  107. Lisowska, E. and Morawiecki, A. (1967): The role of free amino groups in the blood group activity of M and N mucoids. Eur. J. Biochem. 3:237–241.PubMedGoogle Scholar
  108. Lisowska, E. and Roelcke, D. (1973): Differentiation of anti- Pr1 and anti-Pr2 sera with periodate-oxidized erythrocyte glycoproteins. Blut 26:339–341.PubMedGoogle Scholar
  109. Lisowska, E. and Wasniowska, K. (1978): Immunochemical characterization of cyanogen bromide degradation products of M and N blood group glycopeptides. Eur. J. Biochem. 88:247–252.PubMedGoogle Scholar
  110. Lisowska, E., Drzeniek, Z. and Klis, W. (1979): Structural requirements for the interaction of M and N glycopeptides with anti-M and anti-N antibodies andVicia graminea lectin. Glycoconjugates, Proc. Vth Intern. Syrrp. (Kiel), pp. 512–513.Google Scholar
  111. Lisowska, E., Duk, M. and Dahr, W. (1980): Comparison of alkali-labile oligosaccharide chains of M and N blood group glycopeptides from human erythrocyte membrane. Carbohydr. Res. 78:103–113.Google Scholar
  112. Liszka, K., Majdic, O., Bettelheim, P. and Knapp, W. (1983): Glycophorin A expression in malignant hematopoiesis. Amer. J. Hemat. 15:219–226.Google Scholar
  113. Longenecker, B.M., Rahman, A.F.R., Leigh, J. B., Purser, R.A., Greenberg, A.H., Willans, D.J., Keller, O. Petrik, P.K., Thay, T.Y., Suresh, M.R. and Noujaim, A.A. (1984): Monoclonal antibody against a cryptic carbohydrate antigen of murine and human lymphocytes. I. Antigen expression in non-cryptic or unsubstituted form oncertain murine lymphomas, on a spontaneous murine mammary carcinoma, and on several human adenocarcinomas. Int. J. Cancer 33:123–129.PubMedGoogle Scholar
  114. Lynen, R., Rothe, M. and Gallasch, E. (1983): Characterization of formaldehyde-related antibodies encountered in hemodialysis patients at different stages of immunization. Vox Sang. 44:81–89.PubMedGoogle Scholar
  115. Makela, O. and Cantell, K. (1958): Destruction of M and N blood group receptors of human red cells by some influenza viruses. Ann. Med. Biol. Fenn. 36:366–374.Google Scholar
  116. Marchesi, V.T., Tillack, T.W., Jackson, R.L., Segrest, J.P. and Scott, R.E. (1972): Chemical characterization and surface orientation of the major glycoprotein of the human erythrocyte membrane. Proc. Natl. Acad, Sci. USA 69:1445–1449.Google Scholar
  117. Mawby, W.J., Anstee, D.J. and Tanner, M.J.A. (1981): Immunochemical evidence for hybrid sialoglycoproteins of human erythrocyte. Nature (London) 291:161–162.Google Scholar
  118. McDougall, D.C.J, and Jenkins, W.J. (1981): The first human example of anti-Me. Vox Sang. 40:412–415.PubMedGoogle Scholar
  119. Merry, A.H., Thomson, E.E., Anstee, D.J. and Stratton, F. (1984): The quantification of erythrocyte antigen sites with monoclonal antibodies. Immunology 51:7 93–800.Google Scholar
  120. Merz, W. and Roelcke, D. (1971): Biochemische Differenzierung der Pri/Pr2 determinierenden von der MN-determinierenden N-acetyl-Neuraminsaure durch Acetylierungversuche mit Erythrocytenglykoproteinen. Eur. J. Biochem. 23:30–35.PubMedGoogle Scholar
  121. Morawiecki, A. (1964): Dissociation of M and N-group mucoproteins into sub-units in detergent solution. Biochim. Biophys. Acta 83:339–347.PubMedGoogle Scholar
  122. Morel, P.A., Bergren, M.O., Hill, V., Garratty, G. and Perkins, H.A. (1981): M and N specific agglutinins of human erythrocytes stored in glucose solutions. Transfusion 21:652–662.PubMedGoogle Scholar
  123. Moulds, J.J. (1983): Immunochemistry of the MNSs blood group system. In Red Cell Membrane Glycoconjugates and Related Genetic Markers, Cartron, J.P., Rouger, P. and Salmon, C., eds., Librairie Arnette, Paris, pp. 17–26.Google Scholar
  124. Mueller, T.J. and Morrison, M. (1981): Glycoconnectin (PAS- 2), a membrane attachment site for the human erythrocyte cytoskeleton., In Erythrocyte Membranes, 2. Recent Clinical and Experimental Advances, Kruckenberg, W.C., Eaton, J.E. and Brewer, G.J., Eds., A.R. Liss Inc., New York, NY., pp. 95–112.Google Scholar
  125. Nichols, M.E., Rosenfield, R.E. and Rubinstein, P. (1985): Two blood group M epitopes disclosed by monoclonal antibodies. Vox Sang. 49:138–143.PubMedGoogle Scholar
  126. Ochiai, T., Furthmayr, H. and Marcus, D.M. (1983): Diverse in specificities of five monoclonal antibodies reactive with glycophorin A of human erythrocytes. J. Immunol. 131:864–868.PubMedGoogle Scholar
  127. Ogata, S. and Lloyd, K.O. (1982): GpllO - a major sialoglycoprotein of human cells: Isolation and partial characterization from a malignant melanoma cell line. Arch. Biochem. Biophys. 217:665–673.PubMedGoogle Scholar
  128. Owens, J.W., Meuller, T.J. and Morrison, M. (1980): A minor sialoglycoprotein of the human erythrocyte membrane. Arch. Biochem. Biophys. 204:247–254.PubMedGoogle Scholar
  129. Papayannopoulou, T., Yokochi, T. and Martin, P. (1983): The surface antigen profile of HEL cells. In Globin Gene Expression and Hemopoietic Differentiation, Stamatoyannopoulos, G. and Nienhuis, A.W., eds., Alan R. Liss, New York, NY., pp. 277–292.Google Scholar
  130. Pavone, B.G., Pirkola, A., Nevanlinna, H.R. and Issitt, P.D.(1978): Demonstration of anti-Wrb in a second serum containing anti-Ena. Transfusion 18:155–159.PubMedGoogle Scholar
  131. Pavone, B.G., Billman, R., Bryant, J., Sniecinski, I. and Issitt, P.D. (1981): An auto-anti-Ena, inhibitable by MN sialoglycoprotein. Transfusion 21:25–31.PubMedGoogle Scholar
  132. Petryniak, J., Petryniak, B., Wasniowska, K. and Krotkiweski, H. (1980): Isolation and immunochemical characterization of the Euonymus europaeus lectin receptor from the major sialoglycoprotein of human O erythrocytes. Eur. J. Biochem. 105:335–341.PubMedGoogle Scholar
  133. Prohaska, R., Koerner, T.A.W., Armitage, I.M. and Furthmayr, H. (1981): Chemical and carbon-13 nuclear magnetic resonance studies of the blood group M and N active sialoglycopeptides from human glycophorin A. J. Biol. Chem. 256:5781–5791.Google Scholar
  134. Rahman, A.F.R. and Logenecker, B.M. (1982): A monoclonal antbody specific for the Thomsen-Friedenreich cryptic T antigen. J. Immunol. 129:2021–2024.PubMedGoogle Scholar
  135. Rearden, A. (1985): Phospholipid dependence of Wrb antigen expression in human erythrocyte membranes. Vox Sang. 49:3466–353.Google Scholar
  136. Rearden, A., Nachtscheim, D.A., Frisman, D.M., Chiu, P., Elmajian, D. A. and Baird, S.M. (1983): Altered cell surface antigen expression in bladder carcinoma detected by a new hemagglutinating monoclonal antibody. J. Immunol. 131:3073–3077.PubMedGoogle Scholar
  137. Rearden, A., Elmajian, D.A. and Baird, S.M. (1984): Comparison of human and siamang ABH and MN blood groups using monoclonal antibodies. J. Med. Primatol. 13:315–325.PubMedGoogle Scholar
  138. Rearden, A., Taetle, R., Elmajian, D.A., Majda, J.A. and Baird, S.M. (1985): Glycophorin A on normal and leukemia cells detected by monoclonal antibodies, including a new monoclonal antibody reactive with glycophorins A and B. Mol. Immunol. 22:369–378.PubMedGoogle Scholar
  139. Reid, M.E., Ellisor, S.S., Barker, J.M., Lewis, T. and Avoy, D.R. (1981): Characteristics of an antibody causing agglutination of M-positive non-enzymatically glycosylated human red cells. Vox Sang. 41:85–90.PubMedGoogle Scholar
  140. Ridgwell, K., Tanner, M.J.A. and Anstee, D.J. (1983): The Wrb antigen, a receptor for Plasmodium falciparum malaria, is located on a helical region of the major membrane sialoglycoprotein of human red blood cells. Biochem. J. 209:273–276.PubMedGoogle Scholar
  141. Ridgwell, K., Tanner, M.J.A. and Anstee, D.J. (1984): The Wrb antigen in Sta. positive and Dantu-positive human erythrocytes. J. Immunogenet. 11:365–370.PubMedGoogle Scholar
  142. Rimmer, E.F. and Horton, M.A. (1984): Expression of myeloid- specific antigens on two human erythroleukemia cell lines, HEL and K562. Leukemia Res. 8:207–211.Google Scholar
  143. Roelcke, D. (1981): Pr and Gd antigens. Blood Transf. Immunohaemat. 24:27–36.Google Scholar
  144. Roelcke, D. (1984): Kälteagglutinine: humane monoclonale Antikörper gegen Glykokonjugat-Antigene von Zelloberflächen. Funkt. Biol. Med. 3:106:127.Google Scholar
  145. Roelcke, D. and Kreft, H. (1984): Characterization of various anti-Pr cold agglutinins. Transfusion 24:210–213.PubMedGoogle Scholar
  146. Roelcke, D. and Uhlenbruck, G. (1969): Letter to the editor. Vox Sang. 18:478–479.Google Scholar
  147. Roelcke, D., Ebert, W., Metz, J. and Weicker, H. (1971): I-, MN- and Prl/Pr2-activity of human erythrocyte glycoprotein fractions obtained by ficin treatment. Vox Sang. 21:352–361.PubMedGoogle Scholar
  148. Roelcke, D., Ebert, W. and Geisen, H.P. (1976): Anti-Pr3: serological and immunochemical identification of a new anti-Pr specificity. Vox Sang. 30:122–133.PubMedGoogle Scholar
  149. Romanowska, E. (1959): Studies on blood group antigens M and N. IV. Action of influenza virus enzyme on the blood group substances M and N. V. The M and N blood group substances as inhibitors of influenza virus haemagglut- ination. Arch. Immunol. Ther. Exp. 7:749–764.Google Scholar
  150. Salder, J.E., Paulson, J.C. and Hill, R.L. (1979): The role of sialic acid in the expression of human MN blood group antigens. J. Biol. Chem. 254:2112–2119.Google Scholar
  151. Schulte, T.H. and Marchesi, V.T. (1979): Conformation of human erythrocyte glycophorin A and its constituent peptides. Biochemistry 18:275–280.PubMedGoogle Scholar
  152. Siebert, P.D. and Fukuda, M. (1986): Isolation and characterization of human glycophorin A cDNA clones by a synthetic oligonucleotide approach: nucleotide sequence and mRNA structure. Proc. Natl. Acad. Sci. USA 83: 1665–1669.PubMedGoogle Scholar
  153. Sonneborn, H.H., Uthemann, H., Munro, A.C., Bruce, M., Fraser, R.H. and Inglis, G. (1984): Reactivity of monoclonal antibodies directed against blood group antigens M and N. Develop. Biol. Standard. 57:61–68.Google Scholar
  154. Springer, G.F. and Ansell, N. (1958): Inactivation of human erythrocyte agglutinogens M and N by influenza viruses and receptor-destroying enzyme. Proc. Natl. Acad. Sci. USA 44:182–189.PubMedGoogle Scholar
  155. Springer, G.F. and Desai, P.R. (1975): Human blood group MN and precursor specificities: structural and biological aspects. Carbohyd. Res. 40:183–192.Google Scholar
  156. Springer, G.F. and Desai, P.R. (1982): Extent of desialylation of blood group MM, NN and MN antigens required for reactivity with human anti-T antibody andArachis hypogea lectin. J. Biol. Chem. 257:2744–2746.Google Scholar
  157. Springer G.F., Nagai, Y. and Tegtmeyer, H. (1966): Isolation and properties of human blood group NN and meconium Vg antigens. Biochemistry 5:3254–3272.PubMedGoogle Scholar
  158. Steuden, I., Duk, M., Czerwinski, M., Radzikowski, C. and Lisowska, E. (1985): The monoclonal antibody anti- asialoglycophorin from human erythrocytes specific for β-D-Gal-(1–3)-αD-GalNAc- chains (Thomsen-Friedenreich receptors). Glycoconjugate J. 2:303–314.Google Scholar
  159. Suttajit, M. and Winzler, R.J. (1971): Effect of modification of N-acetyl-neuraminic acid on the binding of glycoproteins to influenza virus and on susceptibility to cleavage by neuraminidase. J. Biol. Chem. 24 6:3398–3402.Google Scholar
  160. Tabilio, A., Rosa, J.P., Testa, U., Kieffer, N., Nurden, A.T., Del Canizo, M.C., Breton-Gorius, J. and Vainchenker, W. (1984): Expression of platelet membrane glycoproteins and α-granule proteins by a human erythroleukemia cell line (HEL). EMBO J. 3:453–459.Google Scholar
  161. Takasaki, S. and Kobata, A. (1976): Chemical charactarerization and distribution of ABO blood group active glycoprotein in human erythrocyte membrane. J. Biol. Chem 251:3610–3615.PubMedGoogle Scholar
  162. Taliano, V., Guévin R.M., Hébert, D., Daniels, G.L., Tippett, P., Anstee, D.J., Mawby, W.J. and Tanner, M.J.A. (1980): The rare phenotype En(a-) in a French canadien family. Vox Sang. 38:87–93.PubMedGoogle Scholar
  163. Tanner, M.J.A. and Anstee, D.J. (1976): The membrane change in En(a-) human erythrocytes. Absence of the major sialoglycoprotein. Biochem J. 153:271–277.PubMedGoogle Scholar
  164. Tanner, M.J.A., Jenkins, R.E., Anstee, D.J. and Clamp, J.R. (1976): Abnormal carbohydrate composition of the major penetrating membrane protein of En(a-) erythrocytes. Biochem. J. 155:701–703.PubMedGoogle Scholar
  165. Tanner, M.J.A., Anstee, D.J. and Judson, P.A. (1977): A carbohydrate-deficient membrane glycoprotein in human erythrocytes of phenotype S-s-. Biochem. J. 165:157–161.PubMedGoogle Scholar
  166. Tanner, M.J.A., Anstee, D.J. and Mawby, W.J. (1980): A new human erythrocyte variant (Ph) containing an abnormal sialoglycoprotein. Biochem. J. 187:493–500.PubMedGoogle Scholar
  167. Thomas, D. B. and Winzler, R.J. (1969): Structural studies on human erythrocyte glycoproteins. Alkali-labile oligosaccharides. J. Biol. Chem. 244:5943–5946.Google Scholar
  168. Tokunaga, E., Sasakawa, S., Tamaka, K., Kawamata, H., Giles, C.M., Ikin, E.W., Poole, J., Anstee, D.J., Mawby, W.J. and Tanner M.J.A. (1979): Two apparently healthy Japanese individuals of type MkMk have erythrocytes which lack both the blood group MN and Ss-active sialoglycoproteins. J. Immungenet. 6:383–390.Google Scholar
  169. Tomita, M. and Marchesi, V.T. (1975): Amino acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin. Proc. Natl. Acad. Sci. USA 72:2964–2968.PubMedGoogle Scholar
  170. Tomita, M., Furthmayr, H. and Marchesi, V.T. (1978): Primary structure of human erythrocyte glycophorin A. Isolation and characterization of peptides and complete amino acid sequence. Biochemistry 17:4756–4769.Google Scholar
  171. Uhlenbruck, G. (1981): The Thomsen-Friedenreich (TF) receptors - an old history with new mystery. Immunol. Commun. 10:251–264.PubMedGoogle Scholar
  172. Uhlenbruck, G., Dahr, W., Schmalisch, R. and Janssen, E. (1976): Studies on the receptors of the MNSs blood group system. Blut 32:163–170.PubMedGoogle Scholar
  173. Vaith, P. and Uhlenbruck, G. (1977): The Thomsen agglutination phenomenon: a discovery revisited 50 years later. Z. Immun. -Forsch. 154:1–14.Google Scholar
  174. Vengelen-Tyler, V., Anstee, D.J., Issitt, P.D., Pavone, B.G., Ferguson, S.J., Mawby, W.J., Tanner, M.J.A., Blajchman, M.A. and Lorque, P. (1981): Studies on the blood of an Miv homozygote. Transfusion 21:1–14.PubMedGoogle Scholar
  175. Wasniowska, K. and Lisowska, E. (1981): Products of digestion of tryptic M and N blood group glycopeptides with pronase. Arch. Immunol. Ther. Exp. 29:551–558.Google Scholar
  176. Wasniowska, K., Drzeniek, Z. and Lisowska, E. (1977): The amino acids of M and N blood group glycopept ides are different. Biochem. Biophys. Res. Commun. 76:385–390.Google Scholar
  177. Wasniowska, K., Reichert, C.M., Minniss, M.H., Schroer, K.R., Zopf, D., Lisowska, E., Messeter, L. and Lundblad, A. (1985): Two monoclonal antibodies highly specific for the blood group N determinant. Glycoconjugate J. 2:163–176.Google Scholar
  178. Wiener, A.S. and Rosenfield, R.E. (1961): Me, a blood group factor common to the antigenic properties M and He. J. Immunol. 87:37 6–378.Google Scholar
  179. Yoshima, H., Furthmayr, H. and Kobata, A. (1980): Structures of the asparagine-linked sugar chains of glycophorin A. J. Biol. Chem. 255:9713–9718.PubMedGoogle Scholar

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© Plenum Press, New York 1988

Authors and Affiliations

  • Elwira Lisowska
    • 1
  1. 1.Department of ImmunochemistryInstitute of Immunology and Experimental Therapy Polish Academy of SciencesPoland

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