RH Blood Groups and Rh-Deficiency Syndrome

  • Jean-Pierre Cartron
  • Peter Agre
Part of the Blood Cell Biochemistry book series (BLBI, volume 6)


The discovery of the RH blood group system by Levine and his colleagues (1939, 1941a, b) was associated with the historical description of a fetomaternal alloimmunization responsible for the hemolytic disease of the newborn. The intrauterine fetal death was caused by a maternal antibody directed against an antigen on the surface of her infant’s red cells which was inherited from the father. This antibody had crossed the placenta and destroyed the fetal red cells.


Blood Group Blood Group Antigen Membrane Skeleton Blood Group System Antipeptide Antibody 
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.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Agre, P., and Cartron, J.-P., 1991, Molecular biology of Rh antigens. Blood 78: 551–563.PubMedGoogle Scholar
  2. Anstee, D. J., Holmes, C. H., Judson, P. A., and Tanner, M. J. A., 1992, Use of monoclonal antibodies to determine the tissue distribution of red cell surface antigens on human cells and tissues, Protein Blood Group Antigens of the Human Red Cell (P. Agre and J.-P. Cartron, eds.), pp. 170–181, Johns Hopkins University Press, Baltimore.Google Scholar
  3. Arce, M. A., Thompson, E. S., Wagner, S., Coyne, K. E., Ferdman, B. A., and Lublin, D. M., 1993, Molecular cloning of RhD cDNA derived from a gene present in RhD-positive, but not RhD-negative individuals, Blood 82: 651–655.PubMedGoogle Scholar
  4. Avent, N. D., Judson, P. A., Parsons, S. F., Mallinson, G., Anstee, D. J., Tanner, M. J. A., Evans, P. R., Hodges, E. E., Maciver, A. G., and Holmes, C., 1988a, Monoclonal antibodies that recognize different membrane proteins that are deficient in Rh-null human erythrocytes, Biochem. J. 251: 499–505.PubMedGoogle Scholar
  5. Avent, N. D., Ridgwell, K., Mawby, W. J., Tanner, M. J. A., Anstee, D. J., and Kumpel, B., 1988b, Protein-sequence studies of Rh-related polypeptides suggest the presence of at least two groups of proteins which associated in the human red-cell membrane, Biochem. J. 256: 1043–1046.PubMedGoogle Scholar
  6. Avent, N. D., Ridgwell, K., Tanner. M. J. A., and Anstee, D. J., 1990, cDNA cloning of a 30 kDa erythrocyte membrane protein associated with Rh (Rhesus)-blood-group-antigen expression, Biochem. J. 271: 821–825.Google Scholar
  7. Avent, N. D., Butcher, S. K., Liu. W., Mawby, W. J., Mallinson, G., Parsons, S. F., Anstee, D. J., and Tanner, M. J. A., 1992. Localization of the C termini of the Rh (Rhesus) polypeptides to the cytoplasmic face of the human erythrocyte membrane, J. Biol. Chem. 267: 15134–15139.Google Scholar
  8. Bailly, P., Cartron, J.-P., Wang, D., and Johnson, R. M., 1992, Hereditary stomatocytosis and Rh-deficient patients exhibit distinct molecular defects, Blood 50: 1624–1626.Google Scholar
  9. Bailly, P., Hermand, P., Callebaut, I., Sonneborn, H. H., Khamlichi, S., Mornon, J. P., and Cartron, J.-P., 1994, The LW blood group glycoprotein is homologous to intercellular adhesion molecules, Proc. Natl. Acad. Sci. USA 1: 5306–5310.CrossRefGoogle Scholar
  10. Ballas, S., Clark, M. R., Mohandas, N., Colfer, H. F., Caswell, M. S., Bergen, M. O., Perkins. H. A., and Shohet, S. B., 1984, Red cell membranes and cation deficiency in Rh-null syndrome, Blood 63: 1046–1055.Google Scholar
  11. Ballas, S. K., Flynn, J. C., Pauline, L. A., and Murphy, D. L., 1986, Erythrocyte Rh antigens increase with red cell age, Am. J. Hematol. 23: 19–24.PubMedCrossRefGoogle Scholar
  12. Basu, M. K., Flamm, M., Schacter, D., Bertles, J. F., and Maniatis, A., 1980, Effects of modulating erythrocyte membrane cholesterol, Biochem. Biophys. Res. Commun. 95: 887–893.PubMedCrossRefGoogle Scholar
  13. Bennett, P. R., Le Van Kim, C., Colin, Y., Warwick, R. M., Chérif-Zahar, B., Fisk, N. M., and Cartron, J.-P., 1993, Prenatal determination of fetal RhD type by DNA amplification, N. Engl. J. Med. 329: 607–610.PubMedCrossRefGoogle Scholar
  14. Bennett, V., 1990, Spectrin-based membrane-skeleton: A multipotential adaptor between plasma membrane and cytoplasm, Physiol. Rev. 70: 1029–1065.PubMedGoogle Scholar
  15. Blanchard, D., Bloy, C., Hermand, P., Cartron, J.-P., Saboori, A., Smith, B. L., and Agre, P., 1988. Two-dimensional iodopeptide mapping demonstrates erythrocyte Rh D, c. and E polypeptides are structurally homologous but nonidentical. Blood 72: 1424–1427.Google Scholar
  16. Blancher, A., Ruffié, J., and Socha, W. W., 1993, The R-C-E-F blood group system of chimpanzee: Serology and genetics, J. Med. Primatol. 22: 13–18.PubMedGoogle Scholar
  17. Bloy, C., Blanchard, D., Dahr, W., Beyreuther, K., Salmon, C., and Cartron, J.-P., 1988, Determination of the NH,-terminal sequence of human red cell Rh(D) polypeptide and demonstration that the Rh(D), (c) and (E) antigens are carried by distinct polypeptide chains, Blood 72: 661–666.PubMedGoogle Scholar
  18. Bloy, C., Blanchard, D., Hermand, P., Kordowicz, M., Sonneborn, H. H., and Cartron, J.-P., 1989, Properties of the blood group LW glycoprotein and preliminary comparison with Rh proteins, Mol. Immunol. 26: 1013–1019.PubMedCrossRefGoogle Scholar
  19. Bloy, C., Hermand, P., Blanchard, D., Chérif-Zahar, B., Goossens, D., and Cartron, J.-P., 1990a, Surface orientation and antigen properties of Rh and LW polypeptides of the human erythrocyte membrane, J. Biol. Chem. 265: 21482–21487.PubMedGoogle Scholar
  20. Bloy, C., Hermand, P., Chérif-Zahar, B., Sonneborn, H., and Cartron, J.-P., 1990b, Comparative analysis by two-dimensional iodopeptide mapping of the RhD protein and LW glycoprotein, Blood 75: 2245–2249.PubMedGoogle Scholar
  21. Blunt, T., Steers, F., Daniels, G., and Carritt, B., 1994, Lack of RHC/E expression in the Rhesus D-phenotype is the result of a gene deletion, Ann. Hum. Genet. 58: 19–24.PubMedCrossRefGoogle Scholar
  22. Brown, E., Hooper, L., Ho, T., and Gresham, H., 1990, Integrin-associated protein: A 50 kDa plasma membrane antigen physically and functionally associated with integrins, J. Cell Biol. 111: 2785–2794.PubMedCrossRefGoogle Scholar
  23. Campbell, I. G., Freemont, P. S., Foulkes, W., and Trowsdale, J., 1992, An ovarian tumor marker with homology to vaccinia virus contains an IgV-like region and multiple transmembrane domains, Cancer Res. 52: 5416–5420.PubMedGoogle Scholar
  24. Cartron, J.-P., and Agre, P., 1993, Rh blood group antigens: Protein and gene structure, Semin. Hematol. 30: 193–208.PubMedGoogle Scholar
  25. Cartron, J. P., and Rahuel, C., 1992, Human erythrocyte glycophorins: protein and gene structure analysis, Transfus. Med. Rev. 6: 63–92.PubMedCrossRefGoogle Scholar
  26. Chaudhuri, A., Polyakova, J., Zbrezzna, V., Gulati, W. K., and Pogo, A. O., 1993, Cloning of glycoprotein D cDNA, which encodes the major subunit of the Duffy blood group system and the receptor for the Plasmodium vivax malaria parasite. Proc. Natl. Acad. Sci. USA. 90: 10793–10797.PubMedCrossRefGoogle Scholar
  27. Chaudhuri, A., Zbrezezna, V., Poliakova, J., Pogo, A. O., Hesselgesser, J., and Horuk, R., 1994, Expression of the Duffy antigen in K562 cells. Evidence that it is the human erythrocyte chemokine receptor, J. Biol. Chem. 269: 7835–7838.PubMedGoogle Scholar
  28. Chérif-Zahar, B., Bloy, C., Le Van Kim, C., Blanchard, D., Bailly, P., Hermand, P., Salmon, C., Cartron, J.-P., and Colin, Y., 1990, Molecular cloning and protein structure of a human blood group Rh polypeptide, Proc. Natl. Acad. Sci. USA 87: 6243–6247.PubMedCrossRefGoogle Scholar
  29. Chérif-Zahar, B., Mattéi, M. G., Le Van Kim, C., Bailly, P., Cartron, J.-P., and Colin, Y., 1991, Localization of the human Rh blood group gene structure to chromosome 1p34.3—Ip36.I region by in situ hybridization, Hum. Genet. 86: 398–400.PubMedCrossRefGoogle Scholar
  30. Chérif-Zahar, B., Le Van Kim, C., Raynal, V., D’Ambrosio, A. M., Bailly, P., Cartron, J.-P., and Colin, Y., 1993, Structure and expression of the RH locus in the Rh-deficiency syndrome, Blood 82: 656–662.PubMedGoogle Scholar
  31. Chérif-Zahar, B., Le Van Kim, C., Rouillac, C., Raynal, V., Cartron, J.-P., and Colin, Y., 1994a, Organization of the gene encoding the human blood group RhCcEe antigens and characterization of the promoter region, Genomics 19: 68–74.PubMedCrossRefGoogle Scholar
  32. Chérif-Zahar, B., Raynal, V., D’Ambrosio, A. M., Cartron, J. P., and Colin, Y., 1994b, Molecular analysis of the structure and expression of the RH locus in individuals carrying the D-, Dc— and DC“— gene complexes, Blood,in press.Google Scholar
  33. Colin, Y., Chérif-Zahar, B., Le Van Kim, C., Raynal, V., Van Huffel, V., and Cartron, J.-P., 1991, Genetic basis of the RhD-positive and RhD-negative blood group polymorphism, Blood 78: 2747–2752.PubMedGoogle Scholar
  34. Connor, J., and Schroit, A. J., 1988, Transbilayer movement of phosphatidylserine in erythrocytes: Inhibition of transport and preferential labeling of a 31.000-dalton protein by sulfhydryl reactive reagents, Biochemistry 27: 848–851.PubMedCrossRefGoogle Scholar
  35. Connor, J., Bar-Eli, M., Gillum, K. D., and Schroit, A. J., 1992, Evidence for a structurally homologous Rh-like polypeptide in Rh, erythrocytes, J. Biol. Chem. 267: 26050–26055.PubMedGoogle Scholar
  36. Dahr, W., Kordowicz, M., Moulds, J., Gielen, W., Lebeck, L., and Krueger, J., 1987, Characterization of the Ss sialoglycoprotein and its antigens in Rh-null erythrocytes, Blut 54: 13–24.PubMedCrossRefGoogle Scholar
  37. Devaux, P. F., 1991, Static and dynamic lipid asymmetry in cell membranes, Biochemistry 30: 1163–1173.PubMedCrossRefGoogle Scholar
  38. De Vetten, M. P., and Agre, P., 1988, The Rh polypeptide is a major fatty acid acylated erythrocyte membrane protein, J. Biol. Chem. 263: 18193–18196.PubMedGoogle Scholar
  39. Ervasti, J. M., and Campbell, K. P., 1992, Membrane organization of the dystrophin—glycoprotein complex, Cell 66: 1121–1131.CrossRefGoogle Scholar
  40. Ervasti, J. M., Ohlendieck, K., Kahl, S. D., Gaver, M. G., and Campbell, K. P., 1990, Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle, Nature 345: 315–319.PubMedCrossRefGoogle Scholar
  41. Eyers, S., Ridgwell, K., Mawby, W. J., and Tanner, M. J. A., 1994, Topology and organization of the human Rh (Rhesus) blood group-related polypeptides, J. Biol. Chem. 269: 6417–6423.PubMedGoogle Scholar
  42. 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.PubMedGoogle Scholar
  43. Fisher, R. A., cited by Race, R. R., 1944, An ‘incomplete“ antibody in human serum. Nature 153: 771–772.Google Scholar
  44. Fisher, R. A., and Race, R. R., 1946, Rh gene frequencies in Britain, Nature 157: 48–49.PubMedCrossRefGoogle Scholar
  45. Fukuda, M., 1993, Molecular genetics of the glycophorin A gene cluster. Sem. Hematol. 30: 138–151.Google Scholar
  46. Gahmberg, C. G., 1982, Molecular identification of the human Rho(D)-antigen. FEBS Lett. 140: 93–97.PubMedCrossRefGoogle Scholar
  47. Gahmberg, C. G., 1983, Molecular characterization of the human red-cell Rho(D) antigen, EMBO J. 2: 223–227.PubMedGoogle Scholar
  48. Gahmberg, C. G., and Karhi, K. K., 1984, Association of Rho(D) polypeptides with the membrane skeleton in Rho(D)-positive human red cells, J. Immunol. 133: 334–337.PubMedGoogle Scholar
  49. Gardner, B., Anstee, D. J., Mawby, W. J., Tanner, M. J. A., and von dem Borne, A. E. G., 1991, The abundance and organization of polypeptides associated with antigens of the Rh blood group system, Transfus. Med. 1: 77–85.PubMedCrossRefGoogle Scholar
  50. Green, F. A., 1967, Erythrocyte membrane sulfhydryl groups and Rh antigen activity. Immunochemistry 4: 247–257.PubMedCrossRefGoogle Scholar
  51. Green, F. A., 1968, Phospholipid requirement for Rh antigen activity, J. Biol. Chem. 243: 5519–5521.PubMedGoogle Scholar
  52. Green, F. A., 1972, Erythrocyte membrane lipids and Rh antigen activity, J. Biol. Chem. 247: 881–887.PubMedGoogle Scholar
  53. Green, F. A., Hui, H. L., Green, L. A. D., Heubusch, P., and Pudlak, W., 1984. The phospholipid requirement for Rho(D) antigen activity: Mode of inactivation by phospholipases and protection by anti-Rho(D) antibody, Mol. Immunol. 21: 433–438.PubMedCrossRefGoogle Scholar
  54. Hartel-Schenk, S., and Agre, P., 1992, Mammalian red cell membrane Rh polypeptides are selectively palmitoylated subunits of a macromolecular complex, J. Biol. Chem. 267: 5569–5574.PubMedGoogle Scholar
  55. Hermand, P., Mouro, I., Huet, M., Bloy, C., Suyama, K., Golstein, J., Cartron, J.-P., and Bailly, P., 1993, Immunochemical characterization of Rh proteins with antibodies raised against synthetic peptides, Blood 82: 669–676.PubMedGoogle Scholar
  56. Horuk, R., Chitnis, C. E., Darbonne, W. C., Colby, T. J., Rybicki, A., Hadley, T. J., and Miller, L. H., 1993, A receptor for the malarial parasite Plasmodium vivax: the erythrocyte chemokine receptor, Science 261: 1182–1184.PubMedCrossRefGoogle Scholar
  57. Hughes-Jones, N. C., Gardner, B., and Lincoln, P. J., 1971, Observations of the number of available c, D, and E antigen sites on red cells, Vox Sang. 21: 210–216.CrossRefGoogle Scholar
  58. Hughes-Jones, N. C., Green, E. J., and Hunt, V. A., 1975, Loss of Rh antigen activity following the action of phospholipase A2 on red cell stroma, Vox Sang. 29: 184–191.PubMedCrossRefGoogle Scholar
  59. Hyland, C. A., Wolter, L. C., Liew, Y. W., and Saul, A., 1994a, A southern analysis of Rh blood group genes: association between restriction fragment length polymorphism and Rh serotypes, Blood 83: 566–572.PubMedGoogle Scholar
  60. Hyland, C. A., Wolter, L. C., and Saul, A., I994b, Three unrelated RhD gene polymorphisms identified among blood donors with Rhesus CCee (r’r’) phenotypes. Blood 84: 321–324.Google Scholar
  61. Issitt, P. D., 1989, The Rh blood group system, 1988: Eight new antigens in nine years and some observations on the biochemistry and genetics of the system. Transfus. Med. Rev. 3: 1–12.PubMedCrossRefGoogle Scholar
  62. Kajii, E., Umeneshi, F., Iwamoto, S., and lkemoto, S., 1993, Isolation of a new cDNA clone encoding an Rh polypeptide associated with Rh blood group system, Hum Genet. 91: 157–162.PubMedCrossRefGoogle Scholar
  63. Kuypers, F., van Linde-Sibenius-Trip, M., Roelofsen, B., Tanner, M. J. A., Anstee, D. J., and Opden Kamp, J. A. F., 1984. Rh-null human erythrocytes have an abnormal membrane phospholipid organization, Biochem. J. 221: 93l - 934.Google Scholar
  64. Landsteiner, K., and Wiener, A. S., 1940, An agglutinable factor in human blood recognized by immune sera for rhesus blood, Proc. Soc. Exp. Biol. Med. 43: 223.Google Scholar
  65. Lauf, P. K., and Joiner, C. H., 1976, Increased potassium transport and ouabain binding in human Rh-null red blood cells, Blood 48: 457–468.PubMedGoogle Scholar
  66. Le Van Kim, C., Chérif-Zahar, B., Raynal, V., Lopez, M., Cartron, J.-P., and Colin, Y., 1992a, Multiple Rh mRNAs isoforms are produced by alternative splicing and poly(A) site choice, Blood 80: 1074–1078.Google Scholar
  67. Le Van Kim, C., Mouro, I., Chérif-Zahar, B., Raynal, V., Cherrier, C., Cartron, J.-P., and Colin, Y., 1992b, Molecular cloning and primary structure of the human blood group RhD polypeptide. Proc. Natl. Acad. Sci. USA 89: 10925–10929.CrossRefGoogle Scholar
  68. Le Van Kim, C., Mouro, I., Brossard, Y., Chavinié, J., Cartron, J. P., and Colin, Y., 1994. PCRbased determination of Rhc and RhE status of fetuses at risk of Rhc and RhE haemolytic disease, Br. J. Haematol., 88: 193–195.CrossRefGoogle Scholar
  69. Levine, P., and Stetson, R. E., 1939, An unusual case of intragroup agglutination, J. Am. Med. Assoc. 113: 126–127.CrossRefGoogle Scholar
  70. Levine, P., Burnham, L., Katzin, E. M., and Vogel, P., 1941a, The role of isoimmunization in the pathogenesis of erythroblastosis fetalis, Am. J. Obstet. Gynecol. 42: 925–937.Google Scholar
  71. Levine, P., Katzin, E. M., and Burnham, L., 1941b, Isoimmunization in pregnancy, its possible bearing on the etiology of erythroblastosis fetalis, J. Am. Med. Assoc. 116: 825–827.CrossRefGoogle Scholar
  72. Levine, P., Celano, M., Fenichel, R., Pollack, W., and Singher, H., 1961, A ‘D-like’ antigen in rhesus monkey, human Rh positive and human Rh negative red blood cells, J. Immunol. 87: 747–752.PubMedGoogle Scholar
  73. Levine, P., Cellano, M. J., Wallace, J., and Sanger, R., 1963, A human “D-like” antibody. Nature 198: 596–597.CrossRefPubMedGoogle Scholar
  74. Lindberg, F. P., Lublin, D. M., Telen, M. J., Veile, R. A., Miller, Y. E., Donis-Keller, H., and Brown, E. J., 1994, Rh-related antigen CD47 is the signal transducer integrin-associated protein, J. Biol. Chem. 269: 1567–1570.PubMedGoogle Scholar
  75. Lo, Y. M. D., Bowell, P. J., Selinger, M., Mackenzie, I. Z., Chamberlain, P., Gillmer, M. D. G., Littlewood, T. J., Fleming, K. A., and Wainscoat, J. S., 1993, Prenatal determination of fetal RhD status by analysis of peripheral blood of rhesus negative mothers, Lancet 341: 1147–1148.PubMedCrossRefGoogle Scholar
  76. Lomas, C., McColl, K., and Tippett, P., 1993, Further complexities of the Rh antigen D disclosed by testing category DII cells with monoclonal anti-D, Transfus. Med. 3: 67–69.CrossRefPubMedGoogle Scholar
  77. 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.PubMedCrossRefGoogle Scholar
  78. McGuire, M., Smith, B. L., and Agre, P., 1988, Distinct variants of erythrocyte protein 4.1 inherited in linkage with elliptocytosis and Rh type in three Caucasian families, Blood 72: 287–293.PubMedGoogle Scholar
  79. 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) which express the antigens of the LW blood group system. Biochem. J. 234: 649–652.PubMedGoogle Scholar
  80. Mallinson, G., Anstee, D. J., Avent, N. D., Ridgwell, K., Tanner, M. J. A., Daniels, G. L., Tippett, P., and Von dem Borne, A. E. G., 1990, Murine monoclonal antibody MB-2D10 recognizes Rh-related glycoproteins in the human red cell membrane, Transfusion 30: 222–225.PubMedCrossRefGoogle Scholar
  81. Marsh, W. L., 1983, Deleted antigens of the Rhesus and Kell blood groups: Association with cell membrane defects, in Blood Group Antigens and Disease ( G. Garratty, ed.), pp. 165–185, American Association of Blood Banks, Arlington, VAGoogle Scholar
  82. Marsh, W. L., Chaganti, R. S. K., Gardner, F. G., Mayer, K., Nowell, P. C., and German, J., 1974, Mapping human autosomes: Evidence supporting assignment of Rhesus to the short arm of chromosome no. 1, Science 184: 966–968.CrossRefGoogle Scholar
  83. Merlie, J. P., 1984, Biogenesis of the acetylcholine receptor, a multisubunit integral membrane protein, Cell 36: 573–575.PubMedCrossRefGoogle Scholar
  84. Merry, A. H., Thomson, E. E., Anstee, D. J., and Stratton, F., 1984, The quantification or erythrocyte antigen sites with monoclonal antibodies, Immunology 51: 793–800.PubMedGoogle Scholar
  85. Miller, Y. E., Daniels, G. L., Jones, C., and Palmer, D. K., 1987, Identification of a cell-surface antigen produced by a gene on human chromosome 3 (cenq22) and not expressed by Rh-null cells, Am. J. Hum. Genet. 41: 1061–1070.PubMedGoogle Scholar
  86. Mollison, P. L., Engelfriet, C. P., and Contreras, M., 1992. Blood Transfusion in Clinical Medicine, 9th ed., Blackwell, Oxford.Google Scholar
  87. Moore, S., and Green, C., 1987, The identification of specific Rhesus polypeptide blood group ABH active glycoprotein complexes in the human red cell membrane, Biochem. J. 244: 735–741.PubMedGoogle Scholar
  88. Moore, S., Woodrow, C. F., and McClelland, D. B. L. 1982, Isolation of membrane components associated with human red cell antigens Rho(D), (c), (E), and Fy’. Nature 295: 529–531.PubMedCrossRefGoogle Scholar
  89. Mouro, I., Colin, Y., Chérif-Zahar, B., Cartron, J.-P., and Le Van Kim, C., 1993, Molecular genetic basis of the human Rhesus blood group system. Nature Genet. 5: 62–65.PubMedCrossRefGoogle Scholar
  90. Mouro, I., Le Van Kim, C., Chérif-Zahar, B., Salvignol, I., Blancher, A., Cartron, J.-P., and Colin, Y., 1994a. Molecular characterization of the Rh-like locus and gene transcripts from the rhesus monkey (Macaca mulatta), J. Mol. Evol. 38: 169–176.PubMedCrossRefGoogle Scholar
  91. Mouro, I., Le Van Kim, C., Rouillac, C., van Rhenen, D. J., Le Pennec, P. Y., Cartron, J.-P., and Colin, Y., 1994b, Rearrangements of the blood group RhD gene associated with the D’ category phenotype, Blood 83: 1129–1135.PubMedGoogle Scholar
  92. Nash, R., and Shojania, A. M., 1987, Hematological aspect of Rh deficiency syndrome: A case report and review of the literature. Am. J. Hematol. 24: 267–275.PubMedCrossRefGoogle Scholar
  93. Palek, J., and Jarolim, P., 1993, Clinical expression and laboratory detection of red blood cell membrane protein mutations, Semin. Hematol. 30: 249–283.PubMedGoogle Scholar
  94. 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.PubMedGoogle Scholar
  95. Poss, M. T., Swanson. J. L., Telen, M. J., Lasky, L. C., and Vallera, D. A., 1993, Monoclonal antibody recognizing a unique Rh-related specificity, Vox Sang. 64: 231–239.Google Scholar
  96. Race, R. R., 1965, Modern concepts of the blood group systems, Ann. N. Y. Acad. Sci. 127: 884–891.CrossRefGoogle Scholar
  97. Race, R. R., and Sanger, R., 1975, Blood Groups in Man, 6th ed. Blackwell, Oxford.Google Scholar
  98. Rearden, A., and Masouredis, S. P., 1977, Blood group D antigen content of nucleated red cell precursors, Blood 50: 981–986.PubMedGoogle Scholar
  99. Ridgwell, K., Roberts, S. J., Tanner, M. J. A., and Anstee, D. J., 1983. Absence of two membrane proteins containing extracellular thiol groups in Rh-null human erythrocytes, Biochem. J. 213: 267–269.PubMedGoogle Scholar
  100. 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.PubMedCrossRefGoogle Scholar
  101. Ridgwell, K., Spun, N. K., Laguda, B., Maggeoch, C., Avent, N. D., and Tanner, M. J. A., 1992. Isolation of cDNA clones for a 50 kDa glycoprotein of the erythrocyte membrane associated with Rh (Rhesus) blood-group antigen expression, Biochem. J. 287: 223–228.PubMedGoogle Scholar
  102. Ridgwell, K., Eyers, S., Mawby, W. J., Anstee, D. J., and Tanner, M. J. A., 1994, Studies on the glycoprotein associated with Rh (Rhesus) blood group antigen expression in the human red blood cell membrane, J. Biol. Chem. 269: 6410–6416.PubMedGoogle Scholar
  103. Saboori, A. M., Smith, B. L., and Agre, P., 1988, Polymorphism in the Mr 32,000 Rh protein purified from Rh(D) positive and negative erythrocytes, Proc. Natl. Acad. Sci. USA 85: 4042–4045.PubMedCrossRefGoogle Scholar
  104. Saboori, A., Denker, B. M., and Agre, P., 1989, Isolation of proteins related to the Rh polypeptides from non-human erythrocytes, J. Clin. Invest. 83: 187–191.PubMedCrossRefGoogle Scholar
  105. Salvignol, I., Calvas, P., Socha, W. W., Colin, Y., Le Van Kim, C., Bailly, P., Ruffié, J., Cartron, J. P., and Blancher, A., 1994, Structural analysis of the Rh-like blood group gene products in non human primates. Immuno genetics,in press.Google Scholar
  106. Salvignol, I., Blancher, A., Calvas, P., Socha, W. W., Colin, Y., Cartron, J.-P., and Ruffié, J., 1993, Relationship between chimpanzee Rh-like genes and the R-C-E-F blood group system, J. Med. Primatol. 32: 19–28.Google Scholar
  107. Schmidt, P. J., and Vos, G. H., 1967, Multiple phenotypic abnormalities associated with Rh-null (—), Vox Sang. 13: 18–20.PubMedCrossRefGoogle Scholar
  108. Schroit, A. J., Bloy, C., Connor, J., and Cartron, J.-P., 1990, Involvement of Rh blood group polypeptides in the maintenance of aminophospholipid asymmetry, Biochemistry 29: 10303–10306.PubMedCrossRefGoogle Scholar
  109. Schwartz, M. A., Brown, E., and Fazeli, B., 1993, A 50 kDa integrin-associated protein is required for integrin-regulated calcium entry in endothelial cells, J. Biol. Chem. 268: 19931–19934.PubMedGoogle Scholar
  110. Shinitzky, M., and Souroujon, M., 1979, Passive modulation of blood group antigens, Proc. Natl. Acad. Sci. USA 76: 4438–4440.PubMedCrossRefGoogle Scholar
  111. 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.PubMedGoogle Scholar
  112. Sistonen, P., 1984, Linkage of the LW blood group locus with the complement C3 and Lutheran blood group loci, Ann. Hum. Genet. 48: 239–242.PubMedCrossRefGoogle Scholar
  113. Smith, R. E., and Daleke, D. L., 1990, Phosphatidylserine transport in Rh-null erythrocytes, Blood 76: 1021–1027.PubMedGoogle Scholar
  114. Socha, W. W., and Rufflé, J., 1983, The rhesus system, in Blood Groups of Primates: Theory, Practice and Evolutionary Meaning, pp. 75–90. Liss. New York.Google Scholar
  115. Sonneborn, H. H., Ersat, M., Tills, D., Lomas, C. G., Gorick, B. D., and Hughes-Jones, N. C., 1990, Comparison of the reactions of the Rh-related murine monoclonal antibodies BS58 and R6A, Vox Sang. 58: 219–223.PubMedCrossRefGoogle Scholar
  116. Springer, T. A., 1990, Adhesion receptors of the immune system, Nature 346: 425–434.PubMedCrossRefGoogle Scholar
  117. Sturgeon, P., 1970. Hematological observations on the anemia associated with blood type Rh-null. Blood 36: 310–320.PubMedGoogle Scholar
  118. Sussman, J. J., Bonifacino, J. S., Lippincott-Schwartz, J., Weissman, A., Saito, T., Klausner, R. D., and Ashwell, J. D., 1988, Failure to synthesize the T cell CD3-zeta chain. Cell 52: 85–95.PubMedCrossRefGoogle Scholar
  119. Suyama, K., and Goldstein, J., 1988, Antibody produced against isolated Rh(D) polypeptide reacts with other Rh-related antigens, Blood 72: 1622–1626.PubMedGoogle Scholar
  120. Suyama, K., and Goldstein, J., 1992, Membrane orientation of the Rh(D) polypeptide and partial localization of its epitope-containing domain, Blood 79: 808–812.PubMedGoogle Scholar
  121. Suyama, K., Goldstein, J. Aebersold, R., and Kent, S., 1991, Regarding the size of Rh proteins, Blood 77: 411–412.Google Scholar
  122. Suyama, K., Roy, S., Lunn, R., and Goldstein, J., 1993. Expression of the 32-Kd polypeptide of the Rh antigen, Blood 82: 1006–1009.PubMedGoogle Scholar
  123. Szymanski, I. O., Araszkiewicz, P., Odgren, P., and Snyder, L. M., 1989, Decreased amount of the Rh antigen D in hereditary spherocytosis, Br. J. Haematol. 73: 537–540.PubMedCrossRefGoogle Scholar
  124. Tippett, P., 1986, A speculative model for the Rh blood groups, Ann. Hum. Genet. 50: 241–247.PubMedCrossRefGoogle Scholar
  125. Tippett, P., 1988, Subdivisions of the Rh(D) antigen, Med. Lab. Sci. 45: 88.PubMedGoogle Scholar
  126. Tippett, P., 1990a, Regulator genes affecting red cell antigens, Transfus. Med. Rev. 4: 56–68.PubMedCrossRefGoogle Scholar
  127. Tippett, P., 1990b. Serologically defined Rh determinants, J. Immunogenet. 17: 247–257.PubMedCrossRefGoogle Scholar
  128. Trask, B., Fertitta, A., Christensen, M., Youngblom, J., Bergmann, A., Copeland, A., de Jong, P., Mohrenweiser, H., Olsen, A., Carrano, A., and Tynan, K., 1993, Fluorescence in situ hybridization mapping of human chromosome 19: Cytogenetic band location of 540 cosmids and 70 genes or DNA markers, Genomics 15: 133–145.PubMedCrossRefGoogle Scholar
  129. Umenishi, F., Kajii, E., and Ikemoto, S., 1994, Molecular analysis of Rh polypeptides in a family with RhD-positive and RhD-negative phenotypes. Biochem. J. 299: 207–211.PubMedGoogle Scholar
  130. Victoria, E. J., Branks, M. J., and Masouredis, S. P., 1986, Rh antigen immunoreactivity after histidine modification, Mol. Immunol. 23: 1039–1044.PubMedCrossRefGoogle Scholar
  131. Von dem Borne, A. E. G., Bos, M. J. E., Lomas, C., Tippett, P., Bloy, C., Hermand, P., Cartron, J.-P., Admiraal, L. G., van de Graaf, J., and Overbeeke, M. A. M., 1990, Mutine monoclonal antibodies against a unique determinant of erythrocytes related to Rh and U antigens, Br. J. Haematol. 75: 254–261.CrossRefGoogle Scholar
  132. Wiener, A. S., 1944, The Rh series of allelic genes, Science 100: 595–597.PubMedCrossRefGoogle Scholar
  133. Wiener, A. S., Moor-Jankowski, J., and Gordon, E. B., 1964, Blood groups of apes and monkeys. IV. The Rh-Hr blood types of anthropoid apes, Am. J. Hum. Genet. 16: 246–253.PubMedGoogle Scholar
  134. Williams, A. F., and Barclay, A. N., 1988, The immunoglobulin superfamily. Domains for cell surface recognition. Annu. Rev. Immunol. 6: 381–405.PubMedCrossRefGoogle Scholar
  135. Williams, A. F., Davis, S. J., and Barclay, A. N., 1989, Structural diversity in domains of the immunoglobulin superfamily, Cold Spring Harbor Symp. Quant. Biol. 54: 637–647.PubMedCrossRefGoogle Scholar
  136. Wolter, L. C., Hyland, C. A., and Saul, A., 1993, Rhesus D genotyping using polymerase chain reaction, Blood 82: 1682–1683.PubMedGoogle Scholar
  137. Zachowski, A., and Devaux, P. F., 1990, Transmembrane movements of lipids, Experientia 46: 644–656.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • Jean-Pierre Cartron
    • 1
  • Peter Agre
    • 2
  1. 1.Unité de Recherche U76 de l’Institut National de la Santé et de la Recherche Médicale (INSERM)Institut National de la Transfusion SanguineParisFrance
  2. 2.Departments of Medicine and Cell Biology/AnatomyJohns Hopkins University School of MedicineBaltimoreUSA

Personalised recommendations