Skip to main content
SpringerLink
Log in

Molecular Characteristics of the Blood Group Rho(D) Molecule

  • Chapter
Immunological Aspects

Part of the book series: Subcellular Biochemistry ((SCBI,volume 12))

Abstract

Already in the seventeenth century jaundice of newborn infants had been described. The condition was first thought to be similar to that of adults, which often was due to occlusion of the bile ducts. The fact, however, that there often were several cases in the same family argued against this view (Clarke, 1982).

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 169.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 219.00
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 219.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Abbott, R. E., and Schachter, D., 1976, Inactivation of the Rho(D) antigen of intact human erythrocytes by glutathione maleimide. J. Biol. Chem. 251: 7176–7183.

    PubMed  CAS  Google Scholar 

  • Anderson, R. A., and Lovrien, R. E., 1984, Glycophorin is linked by band 4.1 protein to the human erythrocyte skeleton. Nature 307: 655–658.

    PubMed  CAS  Google Scholar 

  • Anderson, R. A., and Marchesi, V. T., 1985, Regulation of the association of membrane skeletal protein 4.1 with glycophorin by a polyphosphoinositide. Nature 318: 295–298.

    PubMed  CAS  Google Scholar 

  • Andersson, L. C., Gahmberg, C. G., Teerenhovi, L., and Vuopio, P., 1979, Glycophorin A as a marker for early erythroid differentiation in acute leukemia. Int. J. Cancer 24: 717–720.

    PubMed  CAS  Google Scholar 

  • Ballas, S. K., Clark, M. R., Mohandas, N., Colfer, H. F., Caswell, M. S., Bergren, M. O., Perkins, H. A., and Shohet, S. B., 1984, Red cell membrane and cation deficiency in Rh null syndrome. Blood 63: 1046–1055.

    PubMed  CAS  Google Scholar 

  • Bennett, V., and Stenbuck, P. J., 1980, Human erythrocyte ankyrin. J. Biol. Chem. 255: 2540–2548.

    PubMed  CAS  Google Scholar 

  • Bretscher, M. S., 1972, Asymmetrical lipid bilayer structure for biological membranes. Nature New Biol. 236: 11–12.

    PubMed  CAS  Google Scholar 

  • Brock, C. J., Tanner, M. J. A., and Kempf, C., 1983, The human erythrocyte anoin-transport protein. Biochem. J. 213: 577–586.

    PubMed  CAS  Google Scholar 

  • Brown, P. J., Evans, J. P., Sinor, L. T., Tilzer, L. T., and Plapp, F. V., 1983, The rhesus D antigen. A dicyclohexyl-carbodiimide-binding proteolipid. Am. J. Pathol. 110: 127–134.

    PubMed  CAS  Google Scholar 

  • Cabantchik, Z. I., and Rothstein, A., 1974, Membrane protein related to anion permeability of human red blood cells. I. Localization of disulfonic stilbene binding sites in proteins involved in permeation. J. Membr. Biol. 15: 207–226.

    PubMed  CAS  Google Scholar 

  • Clarke, C. A., 1982, Rhesus haemolytic disease of the newborn and its prevention. Historical annotation. Br. J. Haematol. 52: 525–535.

    PubMed  CAS  Google Scholar 

  • Clarke, C. A., Finn, R., McConnell, R. B., and Sheppard, P. M, 1958, The protection afforded by ABO incompatibility against erythroblastosis due to rhesus anti-D. Int. Arch. Allergy 13: 380.

    Google Scholar 

  • Clarke, C. A., Donohoe, W. T. A., McConnell, R. B., Woodrow, J. C., Finn, R., Krevans, J. R., Kulke, W., Lehane, D., and Sheppard, P. M., 1963, Further experimental studies on the prevention of Rh haemolytic disease. Br. Med. J. i: 979–984.

    Google Scholar 

  • Colin, Y., Rahuel, C., London, J., Roméo, P.-H., d’Auriol, L., Galibert, F., and Cartron, J.-P., 1986, Isolation of cDNA clones and complete amino acid sequence of human erythorocyte C. J. Biol. Chem. 261: 229–233.

    PubMed  CAS  Google Scholar 

  • Correas, I., Leto, T. L., Speicher, D. W., and Marchesi, V. T., 1986, Identification of the functional site of erythrocyte protein 4.1 involved in spectrin-actin associations. J. Biol. Chem. 261: 3310–3315.

    PubMed  CAS  Google Scholar 

  • Crawford, D. H., Barlow, M. J., Harrison, J. F., Winger, L., and Huehns, E. R., 1983, Production of human monoclonal antibody to rhesus D antigen. Lancet i: 386–388.

    Google Scholar 

  • Cunningham, N. A., Zola, A. P., Hui, H. L., Taylor, L. M., and Green, R. A., 1985, Binding characteristics of anti-Rho(D) antibodies to Rho(D)-positive and Du red cells. Blood 66: 765–768.

    PubMed  CAS  Google Scholar 

  • Dahr, W., Uhlenbruck, G., Janssen, E., and Schmalisch, R., 1977, Different N-terminal amino acids in the MN glycoproteins from MM and NN erythrocytes. Hum. Genet. 35: 335–343.

    PubMed  CAS  Google Scholar 

  • Darrow, R., 1938, Icterus gravis (erythroblastosis) neonatorum. Arch. Pathol. 25: 378–417.

    Google Scholar 

  • Ekblom, M., Gahmberg, C. G., and Andersson, L. C., 1985, Late expression of M and N antigens on glycophorin A during erythroid differentiation. Blood 66: 233–236.

    PubMed  CAS  Google Scholar 

  • Evans, J. P., Sinor, L. T., Brown, P. J., Tilzer, L. L., and Plapp, F. V., 1982, Identification of Rho(D) antigen in Polyacrylamide gels by an enzyme-linked immunoassay. Mol. Immunol. 19: 671–675.

    PubMed  CAS  Google Scholar 

  • Evans, J. P., Brown, P. J., Sinor, L. T., Tilzer, L. L., Beck, M., and Plapp, F. V., 1983. Detection of an antigen on the inner surface of Rh negative erythrocytes which binds anti-D IgG. Mol. Immunol. 20: 529–536.

    PubMed  CAS  Google Scholar 

  • Falkenburg, J. H. F., Fibbe, W. E., van der Vaart-Duinkerken, N., Nichols, M. E., Rubinstein, P., and Jansen, J., 1985, Human erythroid progenitor cells express rhesus antigens. Blood 66: 660–663.

    PubMed  CAS  Google Scholar 

  • Finn, R., 1960, Erythroblastosis. Lancet i: 526.

    Google Scholar 

  • Finn, R., Clarke, C. A., Donohoe, W. T. A., McConnell, R. B., Sheppard, P. M., Lehane, D., and Kulke, W., 1961, Experimental studies on the prevention of Rh haemolytic disease. Br. Med. J. i: 1486–1490.

    Google Scholar 

  • Finne, J., 1980, Identification of the blood-group ABH-active glycoprotein components of human erythrocyte membrane. Eur. J. Biochem. 104: 181–189.

    PubMed  CAS  Google Scholar 

  • Folkerd, E. J., Ellory, J. C., and Hughes-Jones, N. C., 1977, A molecular size determination of Rh(D) antigen by radiation inactivation. Immunochemistry 14: 529–531.

    PubMed  CAS  Google Scholar 

  • Freda, V. J., Gorman, J. G., and Pollack, W., 1964, Successful prevention of experimental Rh sensitisation in man with an anti-Rh gammaglobulin antibody preparation. Transfusion 4: 26–32.

    PubMed  CAS  Google Scholar 

  • Fukuda, M., Fukuda, M. N., and Hakomori, S., 1979, Developmental change and genetic defect in the carbohydrate structure of band 3 glycoprotein of human erythrocyte membrane. J. Biol. Chem. 254: 5458–5465.

    PubMed  CAS  Google Scholar 

  • Furthmayr, H., 1978, Structural comparison of glycophorins and immunochemical analysis of genetic variants. Nature 271: 519–524.

    PubMed  CAS  Google Scholar 

  • Gahmberg, C. G., 1976, External labeling of erythrocyte glycoproteins. Studies with galactose oxidase and fluorography. J. Biol. Chem. 251: 510–515.

    PubMed  CAS  Google Scholar 

  • Gahmberg, C. G., 1982, Molecular identification of the human Rho(D) antigen. FEBSLett. 140: 93–97.

    CAS  Google Scholar 

  • Gahmberg, C. G., 1983, Molecular characterization of the human red cell Rho(D) antigen. EMBO J. 2: 223–227.

    PubMed  CAS  Google Scholar 

  • Gahmberg, C. G., and Hakomori, S., 1973, External labeling of cell surface galactose and galac-tosamine in glycolipid and glycoprotein of human erythrocytes. J. Biol. Chem. 248: 4211–4317.

    Google Scholar 

  • Gahmberg, C. G., and Karhi, K. K., 1984, Association of Rh„(D) polypeptides with the membrane skeleton in Rho(D)-positive human red cells. J. Immunol. 133:334–337.

    PubMed  CAS  Google Scholar 

  • Gahmberg, C. G., and Karhi, K. K., 1986, Chemistry of ABH/Ii, MN/Ss, and Rho(D) blood group-active proteins of the human red-cell membrane. In Receptors in Cellular Recognition and Developmental Processes (Gahmberg, C. G., and Karhi, K. K., ed.), pp. 251–266, Academic Press, New York.

    Google Scholar 

  • Gahmberg, C. G., Myllylä, 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.

    PubMed  CAS  Google Scholar 

  • Gahmberg, C. G., Jokinen, M., and Andersson, L. C., 1978, Expression of the major sialoglycoprotein (glycophorin) on erythroid cells in human bone marrow. Blood 52: 379–387.

    PubMed  CAS  Google Scholar 

  • Gahmberg, C. G., Jokinen, M., and Andersson, 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.

    PubMed  CAS  Google Scholar 

  • Gahmberg, C. G., Jokinen, M., Karhi, K. K., and Andersson, L. C., 1980. Effect of tunicamycin on the biosynthesis of the major human red cell sialoglycoprotein, glycophorin A, in the leukemia cell line K562. J. Biol. Chem. 255: 2169–2175.

    PubMed  CAS  Google Scholar 

  • Gahmberg, C. G., Jokinen, M., Karhi, K. K., Kämpe, O., Peterson, P. A., and Andersson, L. C., 1983, Glycophorin A, in vitro biogenesis and processing. Methods Enzymol. 96: 281–298.

    PubMed  CAS  Google Scholar 

  • Gahmberg, C. G., Ekblom, M., and Andersson, L. C., 1984, Differentiation of human erythroid cells is associated with an increased O-glycosylation of the major sialoglycoprotein, glycophorin A. Proc. Natl. Acad. Sci. U.S.A. 81: 6752–6756.

    PubMed  CAS  Google Scholar 

  • Gahmberg, C. G., Ekblom, M., and Andersson, L. C., 1986, Markers of normal and malignant erythroid differentiation: Role in clinical practice. In Tumour Markers: Concepts and Applications (Gahmberg, C. G., Ekblom, M., and Andersson, L. C., ed.), pp. 379–429, Blackwell Scientific, Oxford.

    Google Scholar 

  • Greaves, M. F., Sieff, C., and Edwards, P. A. W., 1983, Monoclonal antiglycophorin as a probe for erythroleukemias. Blood 61: 645–651.

    PubMed  CAS  Google Scholar 

  • Green, F. A., 1965, Studies on the Rh(D) antigen. Vox Sang. 10: 32–53.

    PubMed  CAS  Google Scholar 

  • Green, F. A., 1972, Erythrocyte membrane lipids and Rh antigen activity. J. Biol. Chem. 247: 881–887.

    PubMed  CAS  Google Scholar 

  • Green, F. A., Owens, N. A., Hui, J. L., Jung, C. Y., and Cuppoletti, J., 1983, Molecular size of the Rho(D) antigen of the human erythrocyte in situ by radiation inactivation. Mol. Immunol. 20: 361–365.

    PubMed  CAS  Google Scholar 

  • Hadley, T. J., David, P. H., McGinniss, M. H., and Miller, L. H., 1984, Identification of an erythrocyte component carrying the Duffy blood group Fya antigen. Science 223: 597–599.

    PubMed  CAS  Google Scholar 

  • Hakomori, S., 1981, Glycosphingolipids in cellular interaction, differentiation, and oncogenesis. Annu. Rev. Biochem. 50: 733–764.

    PubMed  CAS  Google Scholar 

  • Hakomori, S., and Kobata, A., 1975, Blood group antigens. In The Antigens (M. Sela, ed.), Vol. 2, p. 80, Academic Press, New York.

    Google Scholar 

  • Helenius, A., and Simons, K., 1975, Solubilization of membranes by detergents. Biochim. Biophys. Acta 415: 29–79.

    PubMed  CAS  Google Scholar 

  • Issitt, P. D., 1986, Biochemistry of the Rh blood group system. In Recent Advances in Blood Group Biochemistry (Issitt, P. D., eds.), pp. 105–138, American Association of Blood Banks, Arlington, VA.

    Google Scholar 

  • Jay, D. G., 1986, Glycosylation site of band 3, the human erythrocyte anion-exchange protein. Biochemistry 25: 554–556.

    PubMed  CAS  Google Scholar 

  • Järnefelt, J., Rush, J., Li, Y.-T., and Laine, R. A., 1978, Erythroglycan, a high molecular weight glycopeptide with the repeating structure (galactosyl(1–4)-2-deoxy-2-acetamidoglucosyl(1–3)) comprising more than one-third of the protein-bound carbohydrate of human erythrocyte stroma. J. Biol. Chem. 253: 8006–8009.

    PubMed  Google Scholar 

  • Jokinen, M., Andersson, L. C., and Gahmberg, C. G., 1985, Biosynthesis of the major human red cell sialoglycoprotein, glycophorin A. O-glycosylation. J. Biol. Chem. 260: 11314–11321.

    PubMed  CAS  Google Scholar 

  • Jokinen, M., Gahmberg, C. G., and Andersson, L. C., 1979, Biosynthesis of the major human red cell sialoglycoprotein, glycophorin A, in a continuous cell line. Nature 279: 604–607.

    PubMed  CAS  Google Scholar 

  • Jokinen, M., Ulmanen, I., Andersson, L. C., Kääriäinen, L., and Gahmberg, C. G., 1981, Cell-free synthesis and glycosylation of the major human red cell sialoglycoprotein, glycophorin A. Eur. J. Biochem. 114: 393–397.

    PubMed  CAS  Google Scholar 

  • Karhi, K. K., and Gahmberg, C. G., 1980, Identification of blood group A-active glycoproteins in the human erythrocyte membrane. Biochim. Biophys. Acta 622: 344–354.

    PubMed  CAS  Google Scholar 

  • Karhi, K. K., Andersson, L. C., Vuopio, P., and Gahmberg, C. G., 1981, Expression of blood group A antigens in human bone marrow cells. Blood 57: 147–151.

    PubMed  CAS  Google Scholar 

  • Kleeman, J. E., Masouredis, S. P., and Victoria, E. J., 1982, Exposure of the Rho(D) antigen on the surface and cytoplasmic domains of the red cell membrane. Immunology 45: 27–30.

    PubMed  CAS  Google Scholar 

  • Kopito, R. R., and Lodish, H. F., 1985, Primary structure and transmembrane orientation of the murine anion exchange protein. Nature 316: 234–238.

    PubMed  CAS  Google Scholar 

  • Krusius, T., Finne, J., and Rauvala, H., 1978, The poly(glycosyl) chains of glycoproteins. Characterization of a novel type of glycoprotein saccharides from human erythrocyte membranes. Eur. J. Biochem. 92: 289–300.

    PubMed  CAS  Google Scholar 

  • Kuypers, F., van Linde-Sibenius-Trip, M., Roelofsen, B., Tanner, M. J. A., Anstee, D. J., and Opden Kamp, J. A. F., 1984, Rhnull human erythrocytes have an abnormal membrane phospholipid organization. Biochem. J. 221: 931–934.

    PubMed  CAS  Google Scholar 

  • Lampio, A., Finne, J., Homer, D., and Gahmberg, C. G., 1984, Exposure of the major human red cell glycolipid, globoside, to galactose oxidase. Eur. J. Biochem. 145: 77–82.

    PubMed  CAS  Google Scholar 

  • Lampio, A., Rauvala, H., and Gahmberg, C. G., 1986, Exposure of major neutral glycolipids in red cells to galactose oxidase. Effect of neuraminidase. Eur. J. Biochem. 157: 611–616.

    PubMed  CAS  Google Scholar 

  • Landsteiner, K., and Wiener, A. S., 1940, An agglutinable factor in human blood recognised by immune sera for rhesus blood. Proc. Soc. Exp. Biol. Med. 43: 223.

    CAS  Google Scholar 

  • Lauf, P. K., and Joiner, C. H., 1976, Increased potassium transport and ouabain binding in human Rhnull red blood cells. Blood 48: 457–468.

    PubMed  CAS  Google Scholar 

  • Lee, J. S., Trowsdale, J., and Bodener, W. F., 1980, Synthesis of HLA antigens from membrane-associated messenger RNA. J. Exp. Med. 152: 3S-10S.

    CAS  Google Scholar 

  • Levine, P., 1943, Serological factors as possible causes in spontaneous abortions. J. Hered. 34: 71–80.

    CAS  Google Scholar 

  • Levine, P., and Stetson, R. E., 1939, An unusual case of intragroup agglutination. J. Am. Med. Assoc. 113: 126–127.

    Google Scholar 

  • Levine, P., Burnham, L., Katzin, W. M., and Vogel, P., 1941, The role of iso-immunization in the pathogenesis of erythroblastosis fetalis. Am. J. Obstet. Gynecol. 42: 925–937.

    Google Scholar 

  • Levine, P., Tripodi, D., Struck, J., Jr., Zmijewski, C. M., and Pollack, W., 1973, Hemolytic anemia associated with Rhnull but not with Bombay blood. Vox Sang. 24: 417–424.

    PubMed  CAS  Google Scholar 

  • Litten, J., Culpepper, R., and Bakerman, S., 1978, Studies on the characterization of the Rho(D) antigen. Biochem. Biophys. Acta 543: 226–234.

    PubMed  CAS  Google Scholar 

  • Lorusso, D. J., and Green, F. A., 1975, Reconstitution of Rh(D) antigen activity from human erythrocyte membranes solubilized by deoxycholate. Science 188: 66–67.

    PubMed  CAS  Google Scholar 

  • Mäkelä, O., and Cantell, K., 1958, Destruction of M and N blood group receptor of human red cells by some influenza viruses. Ann. Med. Exp. Biol. Fenn. 36: 366–374.

    Google Scholar 

  • Mallinson, G., Martin, P. G., Anstee, D. J., Tanner, M. J. A., Merry, A. H., Tills, D., and Sonneborn, H. H., 1986, Identification and partial characterization of the human erythrocyte membrane component(s) that express the antigens of the LW blood-group system. Biochem. J. 234: 649–652.

    PubMed  CAS  Google Scholar 

  • Marchesi, V. T., 1983, The red cell membrane skeleton: Recent progress. Blood 61: 1–11.

    PubMed  CAS  Google Scholar 

  • Marchesi, V. T., Furthmayr, H., and Tomita, M., 1976, The red cell membrane. Annu. Rev. Biochem. 45: 667–698.

    PubMed  CAS  Google Scholar 

  • Masouredis, S. P., Sudora, E. J., Mahan, L., and Victoria, E. J., 1976, Antigen site densities and ultrastructural distribution patterns of red cell Rh antigens. Transfusion 16: 94–106.

    PubMed  CAS  Google Scholar 

  • Mawby, W. J., and Findlay, J. B. C., 1983, Characterization and partial sequences of di-iodosulphophenyl siothiocyanate-binding peptide from human erythrocyte anion-transport protein. Biochem. J. 205: 465–475.

    Google Scholar 

  • Moore, S., 1983, Identification of red cell membrane components associated with rhesus blood group antigen expression. In Red Cell Membrane Glycoconjugates and Related Genetic Markers (Moore, S., eds.), pp. 97–106. Librarire Arnette, Paris.

    Google Scholar 

  • Moore, S., Woodrow, C. F., and McClelland, D. B. L., 1982, Isolation of membrane components associated with human red cell antigens Rh(D), (c), (E) and Fya. Nature 295: 529–531.

    PubMed  CAS  Google Scholar 

  • Mueckler, M., and Lodish, H. F., 1986, The human glucose transporter can insert posttranslationally into microsomes. Cell 44: 629–637.

    PubMed  CAS  Google Scholar 

  • Mueckler, M., Caruso, C., Baldwin, S. A., Panico, M., Blench, I., Morris, H. R., Allard, W. J., Lienhard, G. E., and Lodish, H. F., 1985, Sequence and structure of a human glucose transporter. Science 229: 941–945.

    PubMed  CAS  Google Scholar 

  • Nevanlinna, H. R., and Vainio, T., 1956, The influence of mother-child ABO incompatibility on Rh immunisation. Vox Sang. 1: 26–36.

    Google Scholar 

  • Nigg, E. A., Bron, C., Girardet, M., and Cherry, R. J., 1980, Band 3-glycophorin A association in erythrocyte membranes demonstrated by combining protein diffusion measurements with antibody-induced cross-linking. Biochemistry 19: 1887–1892.

    PubMed  CAS  Google Scholar 

  • Owen, M. J., Kissonerghis, A. M., and Lodish, H. F., 1980, Biosynthesis of HLA-A and HLA-B antigen in vivo. J. Biol. Chem. 255: 9678–9684.

    PubMed  CAS  Google Scholar 

  • Paradis, G., Bazin, R., and Lemieux, R., 1986, Protective effect of the membrane skeleton on the immunologic reactivity of the human red cell Rho(D) antigen. J. Immunol. 137: 240–244.

    PubMed  CAS  Google Scholar 

  • Parker, J. C., and Berkowitz, L. R., 1986, Genetic variants affecting the structure and function of the human red cell membrane. In Physiology of Membrane Disorders (T. E. Andreoli, J. F. Hoffman, J. C. Parker, L. R. Berkowitz, D. D. Fanestil, and S. G. Schultz, eds.), pp. 785–814, Plenum Press, New York.

    Google Scholar 

  • Plapp, F. V., Evans, J. P., and Tilzer, L. L., 1981, Detection of Rho(D) antigen on the inner surface of Rh negative erythrocyte membranes. Fed. Proc. 40: 208.

    Google Scholar 

  • Plapp, F. V., Kowalski, M. M., Tilzer, L., Brown, P. J., Evans, J., and Chiga, M., 1979, Partial purification of Rho(D) antigen from Rh positive and negative erythrocytes. Proc. Natl. Acad. Sci. U.S.A. 76: 2964–2968.

    PubMed  CAS  Google Scholar 

  • Ploegh, H. L., Cannon, L. E., and Strominger, J. L., 1979, Cell-free translation of the mRNAs for the heavy and light chains of HLA-A and HLA-B antigens. Proc Natl. Acad. Sci. U.S.A. 76: 2273–2277.

    PubMed  CAS  Google Scholar 

  • Race, R. R., and Sanger, R., 1950, Blood Groups in Man, pp. 234–236, Blackwell Scientific, Oxford.

    Google Scholar 

  • Rearden, A., and Chiu, P., 1983, Lack of rhesus antigen expression by human committed erythroid progenitors. Blood 61: 525–529.

    PubMed  CAS  Google Scholar 

  • Rearden, A., and Masouredis, S. P., 1981, Protease modification enhances anti-D binding to nucleated red blood cell precursors. Vox Sang. 41: 160–164.

    PubMed  CAS  Google Scholar 

  • Redman, C. M., Avellino, G., Pfeffer, S. R., Mukherjee, T. K., Nichols, M., Rubinstein, P., and Marsh, W. L., 1986, Kell blood group antigens are part of a 93,000-dalton red cell membrane protein. J. Biol. Chem. 261: 9521–9525.

    PubMed  CAS  Google Scholar 

  • Ridgwell, K., Roberts, S. J., Tanner, M. J. A., and Anstee, D. J., 1983, Absence of two membrane proteins containing extracellular thiol groups in Rhnull human erythrocytes. Biochem. J. 213: 267–269.

    PubMed  CAS  Google Scholar 

  • Ridgwell, K., Tanner, M. J. A., and Anstee, D. J., 1984, The rhesus (D) polypeptide is linked to the human erythrocyte cytoskeleton. FEBS Lett. 174: 7–10.

    PubMed  CAS  Google Scholar 

  • Robinson, J., Sieff, C., Delia, D., Edwards, P. A. W., and Greaves, M., 1981, Expression of cell-surface HLA-DR, HLA-ABC and glycophorin during erythroid differentiation. Nature 289: 68–71.

    PubMed  CAS  Google Scholar 

  • Sege, K., Rask, L., and Peterson, P. A., 1981, Role of β2-microglobulin in the intracellular processing of HLA antigens. Biochemistry 20: 4523–4530.

    PubMed  CAS  Google Scholar 

  • Shaklai, N., Yguerabide, J., and Ranney, H. M., 1977, Classification and localization of hemoglobin binding sites on the red blood cell membrane. Biochemistry 16: 5593–5597.

    PubMed  CAS  Google Scholar 

  • Shapiro, D. L., and Marchesi, V. T., 1977, Phosphorylation in membranes of intact human erythrocytes. J. Biol. Chem. 252: 508–517.

    PubMed  CAS  Google Scholar 

  • 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. U.S.A. 83: 1665–1669.

    PubMed  CAS  Google Scholar 

  • Sieff, C., Bicknell, D., Caine, G., Robinson, J., Lam, G., and Greaves, M. F., 1982, Changes in cell surface antigen expression during hemopoietic differentiation. Blood 60: 703–713.

    PubMed  CAS  Google Scholar 

  • Sinor, L. T., Brown, P. J., Evans, J. P., and Plapp, F. V., 1984, The Rh antigen specificity of erythrocyte proteolipid. Transfusion 24: 179–180.

    PubMed  CAS  Google Scholar 

  • Springer, G. F., and Ansell, N. J., 1958, Inactivation of human erythrocyte agglutinogens M and N by influenza viruses and receptor-destroying enzyme. Proc. Natl. Acad. Sci. U.S.A. 44: 182–189.

    PubMed  CAS  Google Scholar 

  • Steck, T. L., 1974, The organization of proteins in the human red blood cell membrane. A review. J. Cell Biol. 62: 1–19.

    PubMed  CAS  Google Scholar 

  • Steck, T. L., and Dawson, G., 1974, Topographical distribution of complex carbohydrates in the erythrocyte membrane. J. Biol. Chem. 249: 2135–2142.

    PubMed  CAS  Google Scholar 

  • Stern, K., and Berger, M., 1960, Experimental isosensitization to hemoantigens in man. Paper given at the 13th Annual Meeting of the American Association of Blood Banks, San Francisco.

    Google Scholar 

  • Strapazon, E., and Steck, T. L., 1976, Binding of rabbit muscle aldolase to band 3, the predominant polypeptide of the human erythrocyte membrane. Biochemistry 15: 1421–1424.

    PubMed  CAS  Google Scholar 

  • Sturgeon, P., 1970, Hematological observations in the anemia associated with blood type Rhnull. Blood 36: 310–320.

    PubMed  CAS  Google Scholar 

  • Takakuwa, Y., Tchernia, G., Rossi, M., Benabadji, M., and Mohandas, N., 1986, Restoration of normal membrane stability to unstable protein 4.1-deficient erythrocyte membranes by incorporation of purified protein. 4.1. J. Clin. Invest. 78: 80–85.

    PubMed  CAS  Google Scholar 

  • Tchernia, G., Mohandas, N., and Shohet, B., 1981, Deficiency of skeletal membrane protein band 4.1 in homozygous hereditary elliptocytosis: Implications for erythrocyte membrane stability. J. Clin. Invest. 68: 454–460.

    PubMed  CAS  Google Scholar 

  • Tomita, M., and Marchesi, V. T., 1975, Amino acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin. Proc. Natl. Acad. Sci. U.S.A. 72: 2964–2968.

    PubMed  CAS  Google Scholar 

  • Verkleij, A. J., Zwaal, R. F. A., Roelofsen, B., Confucius, P., Kastelijn, D., and van Deenen, L. L. M., 1973, The asymmetric distribution of phospholipids in the human red cell membrane. Biochim. Biophys. Acta 323: 178–193.

    PubMed  CAS  Google Scholar 

  • Victoria, E. J., Mahan, L. C., and Masouredis, S. P., 1981, Anti-Rho(D) binds to band 3 glycoprotein of the human erythrocyte membrane. Proc. Natl. Acad. Sci. U.S.A. 78: 2898–2902.

    PubMed  CAS  Google Scholar 

  • Vos, G. H., Vos, D., Kirk, R. L., and Sanger, R., 1961, A sample of blood with no detectable Rh antigens. Lancet i: 14–15.

    Google Scholar 

  • Wasniowska, K., Drzeniek, Z., and Lisowska, E., 1977, The amino acids of M and N blood group glycopeptides are different. Biochem. Biophys. Res. Commun. 76: 385–390.

    CAS  Google Scholar 

  • Wiener, A. S., and Peters, H. R., 1940, Hemolytic reactions following transfusions of blood of the homologous group, with three cases in which the same agglutinogen was responsible. Ann. Intern. Med. 13: 2306–2322.

    Google Scholar 

  • Yu, J., and Steck, T. L., 1975, Associations of band 3, the predominant polypeptide of the human erythrocyte membrane. J. Biol. Chem. 250: 9176–9184.

    CAS  Google Scholar 

  • Yurchenko, P. D., and Furthmayr, H., 1980, Expression of red cell membrane proteins in erythroid precursor cells. J. Supramol. Struct. 13: 255–269.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Gahmberg Department of Biochemistry, University of Helsinki, Helsinki, SF-00170, Finland

    Carl G. Gahmberg

Authors
  1. Carl G. Gahmberg
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. North East Thames Regional Transfusion Centre, Brentwood, Essex, England

    J. R. Harris

Rights and permissions

Reprints and permissions

Copyright information

© 1988 Springer Science+Business Media New York

About this chapter

Cite this chapter

Gahmberg, C.G. (1988). Molecular Characteristics of the Blood Group Rho(D) Molecule. In: Harris, J.R. (eds) Immunological Aspects. Subcellular Biochemistry, vol 12. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1681-5_3

Download citation

  • DOI: https://doi.org/10.1007/978-1-4899-1681-5_3

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4899-1683-9

  • Online ISBN: 978-1-4899-1681-5

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation