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Sid and Cad

  • Helmut Schenkel-Brunner

Abstract

The Sid antigen Sd a (ISBT Nr. 901 012) is inherited as a dominant autosomal character [32,45]. It is not confined to red cell membranes but also occurs in different tissues and body secretions. In about 96% of humans this specificity is present on erythrocytes and/or in secretions; 4% lack Sd a activity and contain anti-Sd a in their serum [38].

Keywords

Blood Group Carbohydrate Chain Helix Pomatia Blood Group Antigen Body Secretion 
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. 1.
    Afonso, A.M.M., Charlwood, 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 Sd“ 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. (1972): Cad and Sid. Vox Sang. 22, 362–363.PubMedCrossRefGoogle Scholar
  5. 5.
    Bird, G.W.G. & Wingham, J. (1974): Haemagglutinins from Salvia. Vox Sang. 26, 163–166.PubMedCrossRefGoogle Scholar
  6. 6.
    Bizot, M. & Cayla, J.P. (1972): Hétéroanticorps anti-Cad du poulet. Rev. Franc. Trans“. 15, 195–202.CrossRefGoogle Scholar
  7. 7.
    Blanchard, D., Cartron, J.P., Fournet B., Montreuil, J., van Halbeek, 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
  8. 8.
    Blanchard, D., Capon, C., Leroy, Y., Cartron, J.P. & Fournet, B. (1985): Comparative study of glycophorin A derived 0-glycans from human Cad, Sd(a+) and Sd(a-) erythrocytes. Biochem. J. 232, 813–818.PubMedGoogle Scholar
  9. 9.
    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
  10. 10.
    Cartron, J.P. & Blanchard, D. (1982): Association of human erythrocyte membrane glycoproteins with blood group Cad specificity. Biochem. J. 207, 497–504.PubMedGoogle Scholar
  11. 11.
    Cartron, J.P., Kornprobst, M., Lemonnier, M., Lambin, P., Piller, F. & Salmon, C. (1982): Isolation from human urines of a mucin with blood group Sd° activity. Biochem. Biophys. Res. Commun. 106, 331–337.PubMedCrossRefGoogle Scholar
  12. 12.
    Cartron, J.P., Prou, O., Luilier, M. & Soulier, J.P. (1983): Susceptibility to invasion by Plasmodium falciparum of some human erythrocytes carrying rare blood group antigens. Brit. J. Haemato/, 55, 639–647.CrossRefGoogle Scholar
  13. 13.
    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. Franc. Transf. 11, 209–221.CrossRefGoogle Scholar
  14. 14.
    Conzelmann, A. & Kornfeld, S. (1984): 13-linked N-acetylgalactosamine residues present at the nonreducing termini of 0-linked oligosaccharides of a cloned murine cytotoxic T lymphocyte line are absent in a Vicia villosa lectin-resistant mutant cell line. J. Biol Chem. 259, 12528–12535.PubMedGoogle Scholar
  15. 15.
    Conzelmann, A. & Bron, C., (1987): Expression of UDP-N-acetylgalactosamine:13-galactose 31,4-N-acetylgalactosaminyltransferase in functionally defined T-cell clones. B/ochem. J. 242, 817–824.Google 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 Sd°. J. Exp. Med. 167, 119–131.PubMedCrossRefGoogle Scholar
  17. 17.
    Dall’Olio, F., Malagolini, N. & Serafini-Cessi, F. (1987): Tissue distribution and age-dependent expression of 3–4-N-acetylgalactosaminyltransferase in guinea-pig. Bioscience. Rep. 7, 925–932.CrossRefGoogle Scholar
  18. 18.
    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 131,4-N-acetylgalactosaminyltransferase involved in the synthesis of Sd° antigen and of a2,6-sialyltransferase activity towards N-acetyl-lactosamine. Biochem. J. 270, 519–524.PubMedGoogle Scholar
  19. 19.
    Dohi, T., Hanai, N., Yamaguchi, K. & Oshima, M. (1991): Localization of UDP-GaINAc:NeuAc a2,3Gal-R 31,4(GaINAc to Gal) N-acetylgalactosaminyltransferase in human stomach. Enzymatic synthesis of a fundic gland-specific ganglioside and GM2. J. Biot. Chem. 266, 24038–24043.Google Scholar
  20. 20.
    Dohi, T., Nishikawa, A., Ishizuka, I., Totani, M., Yamaguchi, K., Nakagawa, K., Saitoh, 0., Ohshiba, S. & Oshima, M. (1992): Substrate specificity and distribution of UDP-GaINAc–sialylparagloboside N-acetylgalactosaminyltransferase in the human stomach. Blochern. J. 288, 161–165.Google Scholar
  21. 21.
    Donald, A.S.R., Soh, C.P.C., Watkins, W.M. & Morgan, W.T.J. (1982): N-Acetyl-D-galactosaminyl-3(1-*4)-D-galactose: A terminal non-reducing structure in human blood-group Sd° active Tamm-Horsfall urinary glycoprotein. Biochem. Biophys. Res. Commun. 104, 58–65.PubMedCrossRefGoogle Scholar
  22. 22.
    Donald, A.S.R, Yates, A.D., Soh, C.P.C., Morgan, W.T.J. & Watkins, W.M. (1983): A blood group Sd°-active pentasaccharide isolated from Tamm-Horsfall urinary glycoprotein. Biochem. Biophys. Res. Commun. 115, 625–631.PubMedCrossRefGoogle Scholar
  23. 23.
    Donald, A.S.R., Soh, C.P.C., Feeney, J. & Watkins, W.M. (1987): Genetic and enzymic basis of the Sd° negative phenotype. In: Glycoconjugates, Proceedings of the 6th International Symposium on Glycoconjugates, Lille 1987, Abstract F66.Google Scholar
  24. 24.
    Fletcher, A.P. (1972): The Tamm and Horsfail glycoprotein. In: Glycoproteins. Their Composition, Structure, and Function. (A. Gottschalk, ed.), Elsevier, Amsterdam, 2nd edn., pp. 892–908.Google Scholar
  25. 25.
    Gillard, B.K., Blanchard, D., Bouhours, J.F., Cartron, J.P., van Kiuk, J.A., Kamerling, 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
  26. 26.
    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
  27. 27.
    Hârd, K., van Zadelhoff, G., Moonen, P., Kamerling, J.P. & Vliegenthart, J.F.G. (1992): The Asn-linked carbohydrate chains of human Tamm-Horsfail glycoprotein of one male. Novel sulfated and novel N-acetylgalactosamine-containing N-linked carbohydrate chains. Eur. J. Biochem. 209, 895–915.PubMedCrossRefGoogle Scholar
  28. 28.
    Herkt, F., Parente, J.P., Leroy, Y., Fournet, B., Blanchard, D., Cartron, J.P., van Halbeek, 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. Blechern. 146, 125–129.CrossRefGoogle Scholar
  29. 29.
    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
  30. 30.
    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, IV“GaINAcGM,b, and IV4GaINAcGp1° as antigens for monoclonal immunoglobulin M in neuropathy associated with gammopathy. J. Biol. Chem. 263, 4369–4373.PubMedGoogle Scholar
  31. 31.
    Lopez, M., Gerbai, A., Bony, V. & Salmon, C. (1975): Cad antigen: comparative studies of 50 samples. Vox Sang. 28, 305–313.PubMedCrossRefGoogle Scholar
  32. 32.
    Macvie, S.I., Morton, J.A. & Pickles, M.M. (1967): The reactions and inheritance of a new blood group antigen, Sd°. Vox. Sang. 13, 485–492.CrossRefGoogle Scholar
  33. 33.
    Malagolini, N., Dall’Olio, F., Di Stefano, G., Minni, F., Marranao, D. & Serafini-Cessi, F. (1989): Expression of UDP-GaINAc:NeuAca2,3Ga18-R)31,4(GaINAc to Gal) N-acetylgalactosaminyltransferase involved in the synthesis of Sd° antigen in human large intestine and colorectal carcinomas. Cancer Res. 49, 6466–6470.PubMedGoogle Scholar
  34. 34.
    Malagolini, N., Dall’Olio, F. & Serafini-Cessi, F. (1991): UDP-Ga1NAc:NeuAca2,3Galj3-R (GaINAc to Gal) 131,4-N-acetylgalactosaminytransferase responsible for the Sd° specificity in human colon carcinoma CaCo-2 cell line. Biochem. Biophys. Res. Commun. 180, 681–686.PubMedCrossRefGoogle Scholar
  35. 35.
    Marsh, W.L., Johnson, C.L., Œyen, R., Nichols, M.E., Dinapoli, J., Young, H., Brassel, J., Cusamano, I., Bazaz, G.R., Haber, J.M. & Wolf, C.F.W. (1980): Anti-Sd`: A ‘new’ auto-agglutinin related to the Sd° blood group. Transfusion 20, 1–8.PubMedCrossRefGoogle Scholar
  36. 36.
    Morgan, W.T.J., Soh, C. & Watkins, W.M. (1979): Blood group Sd° specificity as a possible genetic marker on Tamm and Horsfall urinary glycoprotein. In: Glycoconjugates, Proceedings of the 5th International Symposium on Glycoconjugates, Kiel, FRG ( R. Schauer, P. Broer, E. Buddecke, M.F. Kramer, J.F.G. Vliegenthart & H. Wiegandt, eds.), Thieme, Stuttgart, pp. 582–583.Google Scholar
  37. 37.
    Morton, J.A. & Terry, A.M. (1970): The Sd° blood group antigen. Biochemical properties of urinary Sd°. Vox Sang. 19, 151–161.PubMedCrossRefGoogle Scholar
  38. 38.
    Morton, J.A., Pickles, M.M. & Terry, A.M. (1970): The Sd° blood group antigens in tissues and body fluids. Vox Sang 19, 472–482.PubMedCrossRefGoogle Scholar
  39. 39.
    Morton, J.A., Pickles, M.M. & van Hegan, R.I. (1988): The Sd° antigen in the human kidney and colon. Immunot. Invest. 17, 217–224.CrossRefGoogle Scholar
  40. 40.
    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
  41. 41.
    Pickles, M.M. & Morton, J.A. (1977): The Sd° blood group. In: Human Blood Groups, 5th International Convocation on Immunology, Buffalo, NY, 1976 ( J.F. Mohn, R.W. Plunkett, R.K. Cunningham & R.M. Lambert, eds.), Karger, Basel, 1977, pp. 277–286.Google Scholar
  42. 42.
    Piller, F., Cartron, J.P. & Tuppy, H. (1980): Increase of blood group A and loss of blood group Sd° activity in the mucus from human neoplastic colon. Blood Transf. lmmunohaematol.. 23, 599–611.Google Scholar
  43. 43.
    Piller, F., Blanchard, D., Huet, M. & Cartron, J.P. (1986): Identification of a a-NeuAc-(2-*3)-ß-D-galactopyranosyl N-acetyl-p-D-galactosaminyltransferase in human kidney. Carbohydr. Res. 149, 171–184.PubMedCrossRefGoogle Scholar
  44. 44.
    Race, R.R. & Sanger, R. (1975): The Sid groups. In: Blood Groups in Man, 6th edn., Blackwell, Oxford, pp. 395–405.Google Scholar
  45. 45.
    Renton, P.H., Howell, P., Ikin, E.W., Giles, C.M. & Goldsmith, K.L.G. (1967): Anti-Sd°, a new blood group antibody. Vox Sang. 13, 493–501.CrossRefGoogle Scholar
  46. 46.
    Sanger, R., Gavin, J., Tippett, P., Teesdale, P. & Eldon, K. (1971): Plant agglutinin for another human blood group. Lancet, 1130.Google Scholar
  47. 47.
    Serafini-Cessi, F. & Dall’Olio, F. (1983): Guinea pig kidney ß-N-acetylgalactosaminytransferase towards Tamm-Horsfall glycoprotein. Requirement of sialic acid in the acceptor for transferase activity. Biochem. J. 215, 483–489.PubMedGoogle Scholar
  48. 48.
    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. Bioscience Reports 4, 973–978.PubMedCrossRefGoogle Scholar
  49. 49.
    Serafini-Cessi, F., Dall’Olio, F. & Malagolini, N. (1986): Characterization of N-acetyl-jt-D-galactosaminyltransferase from guinea-pig kidney involved in the biosynthesis of Sd° antigen associated with Tamm-Horsfall glycoprotein. Carbohydr. Res. 151, 65–76.PubMedCrossRefGoogle Scholar
  50. 50.
    Serafini-Cessi, F., Malagolini, N. & Dall’Olio F. (1987): Partial purification of p(1–4)-N-acetylgalactosaminyltransferase from urine of Sd(a+) individuals. In: G/ycoconjugates, Proceedings of the 6th International Symposium on Glycoconjugates, Lille 1987, Abstract F9.Google Scholar
  51. 51.
    Serafini-Cessi, F., Malagolini, N. & Dall’Olio, F. (1988): Characterization and partial purification of p-N-acetylgalactosaminyltransferase from urine of Sd(a+) individuals. Arch. Biochem. B/ophys. 266, 573–582.CrossRefGoogle Scholar
  52. 52.
    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
  53. 53.
    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 Sd° activity of Tamm and Horsfall urinary glycoprotein. Biochem. B/ophys. Res. Commun. 93, 1132–1139.CrossRefGoogle Scholar
  54. 54.
    Soh, C.P.C., Donald, A.S.R., Feeney, J., Morgan, W.T.J. & Watkins, W.M. (1989): Enzymic synthesis, chemical characterization and Sd° activity of GaINAcp1–4[NeuAca2–3]Gal131–4GIcNAc and GaINAc131–4[NeuAca2–3]Galp1–4GIc. Glycoconjugate J. 6, 319–332.CrossRefGoogle Scholar
  55. 55.
    Svennerholm, L., Mânsson, J.E. & Li, Y.T. (1973): Isolation and structural determination of a novel ganglioside, a disialosylpentahexosylceramide from human brain. J. Blot Chem. 248, 740–742.Google Scholar
  56. 56.
    Takeya. A., Hosomi, O. & Kogure, T. (1987): Identification and characterization of UDP-GaINAc:NeuAca2–3Galp1–4GIc(NAc) 131–4(GaINAc to Gal) N-acetylgalactosaminyltransferase in human blood plasma. J. Biochem. 101, 251–259.Google Scholar
  57. 57.
    Tamm, I. & Horsfall, F.L. (1950): Characterization and separation of an inhibitor of viral hemagglutination present in urine. Proc. Soc. Exp. Blot Med. 74, 108–114.Google Scholar
  58. 58.
    Tamm, I. & Horsfall, F.L. (1952): A mucoprotein derived from human urine which reacts with influenza, mumps and newcastle disease viruses. J. Exp. Med. 95, 71–97.PubMedCrossRefGoogle Scholar
  59. 59.
    Tollefsen, S.E. & Kornfeld, R. (1984): The B4 lectin from Vicia villosa seeds interacts with N-acetylgalactos amine residues on erythrocytes with blood group Cad specificity. Biochem. B/ophys. Res. Commun. 123, 1099–1106.CrossRefGoogle Scholar
  60. 60.
    Uhlenbruck, G., Sprenger, I., Heggen, M. & Leseney, A.M. (1971): Diagnosis of the “Cad” blood group with agglutinins from snails and plants. Z Immun.-Forsch. 141, 290–291.Google Scholar
  61. 61.
    Williams, J., Marshall, R.D., van Halbeek, H. & Vliegenthart, J.F.G. (1984): Structural analysis of the carbohydrate moieties of human Tamm-Horsfall glycoprotein. Carbohydr. Res. 134, 141–155.PubMedCrossRefGoogle Scholar
  62. 62.
    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
  63. 63.
    Yates, A.D., Donald, A.S.R., Feeney, J. & Watkins, W.M. (1987): Blood group Sd°-active structures on erythrocytes. In: Glycoconjugates, Proceedings of the 6th International Symposium on Glycoconjugates, Lille 1987, Abstract F27.Google Scholar

Copyright information

© Springer-Verlag Wien 1995

Authors and Affiliations

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

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