Sid and Cad

  • Helmut Schenkel-Brunner


The Sid antigen Sd a (ISBT Nr. 901 012) is inherited as a dominant autosomal character [38,55]. It is not confined to red cell membranes but occurs also in different tissues and body secretions. In about 96% of humans this specificity is present on erythrocytes and/or in secretions as well; 4% lack Sd a activity and contain strong anti-Sd a in their serum [44].


Blood Group Helix Pomatia Blood Group Antigen Human Gastric Mucosa Body Secretion 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Afonso, A. M. M., Charuwood, P. A. & Marshall, R. D. (1981): Isolation and characterization of glycopeptides from digests of Tamm-Horsfall glycoprotein. Carbohydr. Res. 89, 309–319.PubMedCrossRefGoogle Scholar
  2. 2.
    Bass, L. S., Rao, A. H., Goldstein, J. & Marsh, W. L (1983): The Sdx antigen and antibody: biochemical studies on the inhibitory property of human urine. Vox Sang. 44, 191–196.PubMedCrossRefGoogle Scholar
  3. 3.
    Bird, G. W. G. (1970): Comparative serological studies of the T, Tn, and Cad receptors. Blut 21, 366–370.PubMedCrossRefGoogle Scholar
  4. 4.
    Bird, G. W. G. & Wingham, J. (1971): Some serological properties of the Cad receptor. Vox Sang. 20, 55–61.PubMedCrossRefGoogle Scholar
  5. 5.
    Bird, G. W. G. & Wingham, J. (1972): Cad and Sid. Vox Sang. 22, 362–363.PubMedCrossRefGoogle Scholar
  6. 6.
    Bird, G. W. G. & Wingham, J. (1974): Haemagglutinins from Salvia. Vox Sang. 26, 163–166.PubMedCrossRefGoogle Scholar
  7. 7.
    Blzot, M. & Cayla, J. P. (1972): Hétéroanticorps anti-Cad du poulet. Rev. Fr. Transfus. 15, 195–202.CrossRefGoogle Scholar
  8. 8.
    Blanchard, D., Capon, C., Leroy, Y., Cartron, J. P. & Fournet, B. (1985): Comparative study of glycophorin A derived O-glycans from human Cad, Sd(a+), and Sd(a-) erythrocytes. Biochem. J. 232, 813–818.PubMedGoogle Scholar
  9. 9.
    Blanchard, D., Cartron, J. P., Fournet, B., Mountreuil, J., VanHalbeek, H. & Vliegenthart, J. F. G. (1983): Primary structure of the oligosaccharide determinant of blood group Cad specificity. J. Biol. Chem. 258, 7691–7695.PubMedGoogle Scholar
  10. 10.
    Blanchard, D., Piller, F., Gillard, B., Marcus, D. & Cartron, J. P. (1985): Identification of a novel ganglioside on erythrocytes with blood group Cad specificity. J. Biol. Chem. 260, 7813–7816.PubMedGoogle Scholar
  11. 11.
    Cartron, J. P. & Blanchard, D. (1982): Association of human erythrocyte membrane glycoproteins with blood-group Cad specificity. Biochem. J. 207, 497–504.PubMedGoogle Scholar
  12. 12.
    Cartron, J. P., Kornprobst, M., Lemonnier, M., Lambin, P., Piller, F. & Salmon, C. (1982): Isolation from human urines of a mucin with blood group Sda activity. Biochem. Biophys. Res. Commun. 106, 331–337.PubMedCrossRefGoogle Scholar
  13. 13.
    Cartron, J. P., Prou, O., Luilier, M. & Soulier, M. (1983): Susceptibility to invasion by Plasmodium falciparum of some human erythrocytes carrying rare blood group antigens. Brit. J. Haematol. 55, 639–647.CrossRefGoogle Scholar
  14. 14.
    Cazal, R., Monis, M., Caubel, J. & Brives, J. (1968): Polyagglutinabilité héréditaire dominante: antigène privé (Cad) correspondant à un anticorps public et à une lectine de Dolichos biflorus. Rev. Fr. Transfus. 11, 209–221.PubMedCrossRefGoogle Scholar
  15. 15.
    Conzelmann, A. & Bron, C. (1987): Expression of UDP-N-acetylgalactosamine:β-galactose β1,4-N-acetylgalactosaminyltransferase in functionally defined T-cell clones. Biochem. J. 242, 817–824.PubMedGoogle Scholar
  16. 16.
    Conzelmann, A. & Lefrançois, L. (1988): Monoclonal antibodies specific for T cell-associated carbohydrate determinants react with human blood group antigens Cad and Sda. J. Exp. Med. 167, 119–131.PubMedCrossRefGoogle Scholar
  17. 17.
    Dall’olio, F., Malagolini, N., Di Stefano, G., Ciambella, M. & Serafini-Cessi, F. (1990): Postnatal development of rat colon epithelial cells is associated with changes in the expression of the β1,4-N-acetylgalactosaminyltransferase involved in the synthesis of Sda antigen and of α2,6-sialyltransferase activity towards N-acetyl-lactosamine. Biochem. J. 270, 519–524.Google Scholar
  18. 18.
    Dall’olio, F., Malagolini, N. & Serafini-Cessi, F. (1987): Tissue distribution and age-dependent expression of α-4-N-acetylgalactosaminyltransferase in guinea-pig. Biosci. Rep. 7, 925–932.CrossRefGoogle Scholar
  19. 19.
    Dohi, T., Hanai, N., Yamaguchi, K. & Oshima, M. (1991): Localization of UDP-GalNAc: NeuAca2,3Gal-R β1,4(GalNAc to Gal) N-acetylgalactosaminyltransferase in human stomach. Enzymatic synthesis of a fundic gland-specific ganglioside and GM2. J. Biol. Chem. 266, 24038–24043.PubMedGoogle Scholar
  20. 20.
    Dohi, T., Nlshikawa, A., Ishizuka, I., Totani, M., Yamaguchi, K., Nakagawa, K., Saitoh, O., Ohshiba, S. & Oshima, M. (1992): Substrate specificity and distribution of UDP-GalNAc: sialylparagloboside N-acetylgalactosaminyltransferase in the human stomach. Biochem. J. 288, 161–165.PubMedGoogle Scholar
  21. 21.
    Dohi, T., Ohta, S., Hanai, N., Yamaguchi, K. & Oshima, M. (1990): Sialylpentaosylceramide detected with anti-GM2 monoclonal antibody. Structural characterization and complementary expression with GM2 in gastric cancer and normal gastric mucosa. J. Biol. Chem. 265, 7880–8885.PubMedGoogle Scholar
  22. 22.
    Dohi, T., Yuyama, Y., Natori, Y., Smith, P. L., Lowe, J. B. & Oshima, M. (1996): Detection of N-acetylgalactosaminyltransferase mRNA which determines expression of Sda blood group carbohydrate structure in human gastrointestinal mucosa and cancer. Int. J. Cancer 67, 626–631.PubMedCrossRefGoogle Scholar
  23. 23.
    Donald, A. S. R. & Feeney, J. (1986): Oligosaccharides obtained from a blood-group-Sd(a+) Tamm-Horsfall glycoprotein. An n.m.r. study. Biochem. J. 236, 821–828.PubMedGoogle Scholar
  24. 24.
    Donald, A. S. R., Soh, C. P. C., Feeney, J. & Watkins, W. M. (1987): Genetic and enzymic basis of the Sda negative phenotype. In: Glycoconjugates, Proceedings of the 6th Int. Symposium on Glycoconjugates, Lille 1987, Abstract F 66.Google Scholar
  25. 25.
    Donald, A. S. R., Soh, C. P. C., Watkins, W. M. & Morgan, W. T. J. (1982): N-Acetyl-D-galactosaminyl-β-(1→4)-D-galactose: a terminal non-reducing structure in human blood-group Sda active Tamm-Horsfall urinary glycoprotein. Biochem. Biophys. Res. Commun. 104, 58–65.PubMedCrossRefGoogle Scholar
  26. 26.
    Donald, A. S. R., Yates, A. D., Soh, C. P. C., Morgan, W. T. J. & Watkins, W. M. (1983): A blood group Sda-active pentasaccharide isolated from Tamm-Horsfall urinary glycoprotein. Biochem. Biophys. Res. Commun. 115, 625–631.PubMedCrossRefGoogle Scholar
  27. 27.
    Fletcher, A. P. (1972): The Tamm and Horsfall glycoprotein. In: Glycoproteins. Their Composition, Structure, and Function (A. Gottschalk, ed.). Elsevier, Amsterdam, pp. 892–908.Google Scholar
  28. 28.
    Fredman, P., Mansson, J. E., Wikstrand, C. J., Vrionis, F. D., Rynmark, B. M., Bigner, D. D. & Svennerholm, L. (1989): A new ganglioside of the lactotetraose series, GalNAc-3′-isoLM1, detected in human meconium. J. Biol. Chem. 264, 12122–12125.PubMedGoogle Scholar
  29. 29.
    Gillard, B. K., Blanchard, D., Bouhours, J. F., Cartron, J. P., VanKuik, J. A., Kamerung, J. P., Vliegenthart, J. F. G. & Marcus, D. M. (1988): Structure of a ganglioside with Cad blood group antigen activity. Biochemistry 27, 4601–4606.PubMedCrossRefGoogle Scholar
  30. 30.
    Hammarström, S., Murphy, L. A., Goldstein, I. J. & Etzler, M. E. (1977): Carbohydrate binding specificity of four N-acetyl-D-galactosamine-“specific” lectins: Helix pomatia A hemagglutinin, soy bean agglutinin, lima bean lectin, and Dolichos biflorus lectin. Biochemistry 16, 2750–2755.PubMedCrossRefGoogle Scholar
  31. 31.
    Hard, K., VanZadelhoff, G., Moonen, P., Kamerling, J. P. & Vliegenthart, J. F. G. (1992): The Asn-linked carbohydrate chains of human Tamm-Horsfall glycoprotein of one male. Novel sulfated and novel N-acetylgalactosamine-containing N-linked carbohydrate chains. Eur. J. Biochem. 209, 895–915.PubMedCrossRefGoogle Scholar
  32. 32.
    Herkt, F., Parente, J. P., Leroy, Y., Fournet, B., Blanchard, D., Cartron, J. P., VanHalbeek, H. & 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.PubMedCrossRefGoogle Scholar
  33. 33.
    Hession, C., Decker, J. M., Sherblom, A. P., Kumar, S., Yue, S. S., Mattaliano, R. J., Tizard, R., Kawashima, E., Schmeissner, U., Heletky, S., Chow, E. P., Burne, C. A., Shaw, A. & Muchmore, A. V. (1987): Uromodulin (Tamm-Horsfall glycoprotein): a renal ligand for lymphokines. Science 237, 1479–1484.PubMedCrossRefGoogle Scholar
  34. 34.
    Hiraiwa, N., Tsuyuoka, K., Li, Y. T., Tanaka, M., Seno, T., Okubo, Y., Fukuda, Y., Imura, H. & Kannagi, R. (1990): Gangliosides and sialoglycoproteins carrying a rare blood group antigen determinant, Cad, associated with human cancers as detected by specific monoclonal antibodies. Cancer Res. 50, 5497–5503.PubMedGoogle Scholar
  35. 35.
    Hunt, J. S., Mcgiven, A. R., Qroufsky, A., Lynn, K. L. & Taylor, M. C (1985): Affinity-purified antibodies of defined specificity for use in a solid-phase microplate radioimmunoassay of human Tamm-Horsfall glycoprotein in urine. Biochem. J. 227, 957–963.PubMedGoogle Scholar
  36. 36.
    Ilyas, A. A., Li, S. C., Chou, D. K. H., Li, Y. T., Jungalwala, F. B., Dalakas, M. C. & Quarles, R. H. (1988): Gangliosides GM2 IV4GalNAcGM1b, and IV4GalNAcGD1a as antigens for monoclonal immunoglobulin M in neuropathy associated with gammopathy. J. Biol. Chem. 263, 4369–4373.PubMedGoogle Scholar
  37. 37.
    Lopez, M., Gerbal, A., Bony, V. & Salmon, C. (1975): Cad antigen: comparative studies of 50 samples. Vox Sang. 28, 305–313.PubMedCrossRefGoogle Scholar
  38. 38.
    Macvie, S. I., Morton, J. A. & Pickles, M. M. (1967): The reactions and inheritance of a new blood group antigen Sda. Vox Sang. 13, 485–492.CrossRefGoogle Scholar
  39. 39.
    Malagolini, N., Dall'olio, F., Di Stefano, G., Minni, F., Marrano, D. & Serafini-Cessi, F. (1989): Expression of UDP-GalNAc:NeuAc-α-2,3Gal-β-R α-1,4(GalNAc to Gal) N-acetylgalactosaminyl-transferase involved in the synthesis of Sda antigen in human large intestine and colorectal carcinomas. Cancer Res. 49, 6466–6470.PubMedGoogle Scholar
  40. 40.
    Malagolini, N., Dall’olio, F., Guerrini, S. & Serafini-Cessi, F. (1994): Identification and characterization of the Sda β1,4,N-acetylgalactosaminyltransferase from pig large intestine. Glycocon. J. 11, 89–95.CrossRefGoogle Scholar
  41. 41.
    Malagolini, N., Dall’olio, F. & Serafini-Cessi, F. (1991): UDP-GalNAc:NeuAcα2,3Galβ-R (GalNAc to Gal) β1,4-N-acetylgalactosaminyltransferase responsible for the Sda specificity in human colon carcinoma CaCo-2 cell line. Biochem. Biophys. Res. Commun. 180, 681–686.PubMedCrossRefGoogle Scholar
  42. 42.
    Marsh, W. L., Johnson, C. L., 0Yen, R., Nichols, M. E., Dinapoli, J., Young, H., Brassel, J., Cusamano, I., Bazaz, G. R., Haber, J. M. & Wolf, C. F. W. (1980): Anti-Sdx: a “new” auto-agglutinin related to the Sda blood group. Transfusion 20, 1–8.PubMedCrossRefGoogle Scholar
  43. 43.
    Morgan, W. T. J., Soh, C. & Watkins, W. M. (1979): Blood group Sda specificity as a possible genetic marker on Tamm and Horsfall urinary glycoprotein. In: Glycoconjugates (R. Schauer, P. Broer, E. Buddecke, M. F. Kramer, J. F. G. Vliegenthart, and H. Wiegandt, eds.), Thieme, Stuttgart, pp. 582–583.Google Scholar
  44. 44.
    Morton, J. A., Pickles, M. M. & Terry, A. M. (1970): The Sda blood group antigens in tissues and body fluids. Vox Sang. 19, 472–482.PubMedCrossRefGoogle Scholar
  45. 45.
    Morton, J. A., Pickles, M. M. & VanHegan, R. I. (1988): The Sda antigen in the human kidney and colon. Immunol. Invest. 17, 217–224.PubMedCrossRefGoogle Scholar
  46. 46.
    Morton, J. A. & Terry, A. M. (1970): The Sda blood group antigen. Biochemical properties of urinary Sda. Vox Sang. 19, 151–161.PubMedCrossRefGoogle Scholar
  47. 47.
    Muchmore, A. V. & Decker, J. M. (1985): Uromodulin: a unique 85-kilodalton immunosuppressive glycoprotein isolated from urine of pregnant women. Science 229, 479–481.PubMedCrossRefGoogle Scholar
  48. 48.
    Muchmore, A. V. & Decker, J. M. (1986): Uromodulin. An immunosuppressive 85-kilodalton glycoprotein isolated from human pregnancy urine is a high affinity ligand for recombinant interleukin 1a. J. Biol. Chem. 261, 13404–13407.PubMedGoogle Scholar
  49. 49.
    Parkkinen, J., Virkola, R. & Korhonen, T. K. (1988): Identification of factors in human urine that inhibit the binding of Escherichia coli adhesins. Infect. Immun. 56, 2623–2630.PubMedGoogle Scholar
  50. 50.
    Pennica, D., Kohr, W. J., Kuang, W. J., Glaister, D., Aggarwal, B. B., Chen, E. Y. & Goeddel, D. V. (1987): Identification of human uromodulin as the Tamm-Horsfall urinary glycoprotein. Science 236, 83–88.PubMedCrossRefGoogle Scholar
  51. 51.
    Pickles, M. M. & Morton, J. A. (1977): The Sda blood group. In: Human Blood Groups (J. F. Mohn, R. W. Plunkett, R. K. Cunningham, and R. M. Lambert, eds.). S. Karger, Basel, pp. 277–286.Google Scholar
  52. 52.
    Piller, F., Blanchard, D., Huet, M. & Cartron, J. P. (1986): Identification of a α-NeuAc-(2→3)-β-D-galactopyranosyl N-acetyl-β-D-galactosaminyltransferase in human kidney. Carbohydr. Res. 149, 171–184.PubMedCrossRefGoogle Scholar
  53. 53.
    Piller, F., Cartron, J. P. & Tuppy, H. (1980): Increase of blood group A and loss of blood group Sda activity in the mucus from human neoplastic colon. Blood Transfus. Immunohaematol. 23, 599–611.CrossRefGoogle Scholar
  54. 54.
    Race, R. R. & Sänger, R. (1975): The Sid groups. In: Blood Groups in Man. Blackwell Scientific Publications, Oxford, pp. 395–405.Google Scholar
  55. 55.
    Renton, P. H., Howell, P., Ikin, E. W., Giles, C. M. & Goldsmith, K. L. G. (1967): Anti-Sda, a new blood group antibody. Vox Sang. 13, 493–501.CrossRefGoogle Scholar
  56. 56.
    Rindler, M. J., Naik, S. S., Li, N., Hoops, T. C. & Peraldi, M. N. (1990): Uromodulin (Tamm-Horsfall glycoprotein / uromucoid) is a phosphatidylinositol-linked membrane protein. J. Biol. Chem. 265, 20784–20789.PubMedGoogle Scholar
  57. 57.
    Sanger, R., Gavin, J., Tippett, P., Teesdale, P. & Eldon, K. (1971): Plant agglutinin for another human blood group. Lancet i, 1130.CrossRefGoogle Scholar
  58. 58.
    Serarni-Cessi, F. & Dall’olio, F. (1983): Guinea pig kidney α-N-acetylgalactosaminyltransferase towards Tamm-Horsfall glycoprotein. Requirement of sialic acid in the acceptor for transferase activity. Biochem. J. 215, 483–489.Google Scholar
  59. 59.
    Serafini-Cessi, F., Dall’olio, F. & Malagolini, N. (1986): Characterization of N-acetyl-β-D-galactosaminyltransferase from guinea-pig kidney involved in the biosynthesis of Sda antigen associated with Tamm-Horsfall glycoprotein. Carbohydr. Res. 151, 65–76.PubMedCrossRefGoogle Scholar
  60. 60.
    Serafini-Cessi, F., Malagolini, N. & Dall’olio, F. (1984): A tetraantennary glycopeptide from human Tamm-Horsfall glycoprotein inhibits agglutination of desialylated erythrocytes induced by leucoagglutinin. Biosci. Rep. 4, 973–978.PubMedCrossRefGoogle Scholar
  61. 61.
    Serafini-Cessi, F., Malagolini, N. & Dall’olio, F. (1988): Characterization and partial purification of α-N-acetylgalactosaminyltransferase from urine of Sd(a+) individuals. Arch. Biochem. Biophys. 266, 573–582.PubMedCrossRefGoogle Scholar
  62. 62.
    Serafini-Cessi, F., Malagolini, N., Guerrini, S. & Turrini, I. (1995): A soluble form of Sda-β1,4-N-acetylgalactosaminyltransferase is released by differentiated human colon carcinoma CaCo-2 cells. Glycoconj. J. 12, 773–779.PubMedCrossRefGoogle Scholar
  63. 63.
    Sikri, K. L., Foster, C. L., Bloomfield, F. J. & Marshall, R. D. (1979): Localization by immunofluorescence and by light-and electron-microscopic immunoperoxidase techniques of Tamm-Horsfall glycoprotein in adult hamster kidney. Biochem. J. 181, 525–532.PubMedGoogle Scholar
  64. 64.
    Smith, P. L. & Lowe, J. B. (1994): Molecular cloning of a murine N-acetylgalactosamine transferase cDNA that determines expression of the T lymphocyte-specific CT oligosaccharide differentiation antigen. J. Biol. Chem. 269, 15162–15171.PubMedGoogle Scholar
  65. 65.
    Soh, C. P. C., Donald, A. S. R., Feeney, J., Morgan, W. T. J. & Watkins, W. M. (1989): Enzymic synthesis, chemical characterization and Sda activity of GalNAcβ1-4[NeuAcα2-3]Galβ1-4GlcNAc and GalNAcβ1-4[NeuAcα2-3]Galβ1-4Glc. Glycoconj. J. 6, 319–332.PubMedCrossRefGoogle Scholar
  66. 66.
    Soh, C. P. C., Morgan, W. T. J., Watkins, W. M. & Donald, A. S. R. (1980): The relationship between the N-acetylgalactosamine content and the blood-group Sda activity of Tamm and Horsfall urinary glycoprotein. Biochem. Biophys. Res. Commun. 93, 1132–1139.PubMedCrossRefGoogle Scholar
  67. 67.
    Svennerholm, L., Mansson, J. E. & Li, Y. T. (1973): Isolation and structural determination of a novel ganglioside, a disialosylpentahexosylceramide from human brain. J. Biol. Chem. 248, 740–742.PubMedGoogle Scholar
  68. 68.
    Takeya, A., Hosomi, O. & Kogure, T. (1987): Identification and characterization of UDP-GalNAc: NeuAcα2-3Galβ1-4Glc(NAc) β1-4(GalNAc to Gal) N-acetylgalactosaminyltransferase in human blood plasma. J. Biochem. 101, 251–259.PubMedGoogle Scholar
  69. 69.
    Tamm, I. & Horsfall, F. L. (1950): Characterization and separation of an inhibitor of viral hemagglutination present in urine. Proc. Soc. Exp. Biol. Med. 74, 108–114.Google Scholar
  70. 70.
    Tamm, I. & Horsfall, F. L. (1952): A mucoprotein derived from human urine which reacts with influenza, mumps, and newcastle disease virus. J. Exp. Med. 95, 71–97.PubMedCrossRefGoogle Scholar
  71. 71.
    Tollefsen, S. E. & Kornfeld, R. (1984): The B4 lectin from Vicia villosa seeds interacts with N-acetylgalactosamine residues on erythrocytes with blood group Cad specificity. Biochem. Biophys. Res. Commun. 123, 1099–1106.PubMedCrossRefGoogle Scholar
  72. 72.
    Toma, G., Bates, J. M. & Kumar, S. (1994): Uromodulin (Tamm-Horsfall Protein) is a leukocyte adhesion molecule. Biochem. Biophys. Res. Commun. 200, 275–282.PubMedCrossRefGoogle Scholar
  73. 73.
    Uhlenbruck, G. (1971): Diagnosis of the “cad” blood group with agglutinins from snails and plants. Z. Immun.-Forsch. 141, 290–291.Google Scholar
  74. 74.
    Williams, J., Marshall, R. D., VanHalbeek, H. & Vliegenthart, J. F. G. (1984): Structural analysis of the carbohydrate moieties of human Tamm-Horsfall glycoprotein. Carbohydr. Res. 134, 141–155.PubMedCrossRefGoogle Scholar
  75. 75.
    Yamaguchi, H., Okubo, Y., Ogawa, Y. & Tanaka, M. (1973): Japanese families with group O and B red cells agglutinable by Dolichos biflorus extracts. Vox Sang. 25, 361–369.PubMedCrossRefGoogle Scholar
  76. 76.
    Yates, A. D., Donald, A. S. R., Feeney, J. & Watkins, W. M. (1987): Blood group Sda-active structures on erythrocytes. In: Proceedings of the IXth Int. Symp. on Glycoconjugates, Lille 1987, Abstract F 27.Google Scholar

Copyright information

© Springer-Verlag Wien 2000

Authors and Affiliations

  • Helmut Schenkel-Brunner
    • 1
  1. 1.Institut für Medizinische BiochemieUniversität WienViennaAustria

Personalised recommendations