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. 1976 Sep 1;144(3):644–653. doi: 10.1084/jem.144.3.644

Status of blood group carbohydrate chains in ontogenesis and in oncogenesis

PMCID: PMC2190416  PMID: 60462

Abstract

Blood group ABH determinants in human erythrocytes are carried by four kinds of glycolipid carbohydrate chains, differing in their structural complexity. They are Aa, Ab, Ac, and Ad for A variants, and H1, H2, H3, and H4 for H variants (Table I and Fig 1). Based on the surface labeling of A variants and on the reactivity of erythrocytes to antibodies directed against H3 and against its degradation products, it is concluded that complex variants of A or H determinants (Ac and Ad/or H3 and H4) are absent or significantly low in fetal erythrocytes (80- 150 days after gestation) and in new born erythrocytes, whereas these complex structures are fully developed in adult erythrocytes. In contrast, A determinants linked to simpler carbohydrate chains (Aa, Ab variants) are fully developed before birth and do not show significant change after birth. The precursor of blood group carbohydrate chains seems to be abundant in fetal or newborn erythrocytes. This assumption is based on the higher reactivity of fetal or newborn erythrocytes to an antibody, which is directed against the precursor N- acetylglucosaminly beta1 leads to 3 galactosyl beta1 leads to 4 glucosylceramide than in adult erythorocytes. Reactions of glycolipids of gastrointestinal mucosa, with antibodies directed against H3 glycolipid and its degradation products, were compared to that of gastrointestinal tumors. The reaction to bela Glc NAc1 leads to 3 beta Gall leads to 4 Glc leads to ceramide (structure 4), which is the precursor of all blood group glycolipids, was consistently high in many cases of tumor glycolipid than that of normal glycolipid. This as well as other evidence supports a general concept that the process of ontogenesis of a blood group carbohydrate chain occurs as step-by-step elongation and arborization, and that blocking of such a development of a carbohydrate chain occurs in the process of oncogenesis.

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Selected References

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  1. Davidsohn I., Kovarik S., Ni L. Y. Isoantigens A, B, and H in benign and malignant lesions of the cervix. Arch Pathol. 1969 Mar;87(3):306–314. [PubMed] [Google Scholar]
  2. Feizi T., Kabat E. A., Vicari G., Anderson B., Marsh W. L. Immunochemical studies on blood groups. XLVII. The I antigen complex--precursors in the A, B, H, Lea, and leb blood group system--hemagglutination-inhibition studies. J Exp Med. 1971 Jan 1;133(1):39–52. doi: 10.1084/jem.133.1.39. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Feizi T., Turberville C., Westwood J. H. Blood-group precursors and cancer-related antigens. Lancet. 1975 Aug 30;2(7931):391–393. doi: 10.1016/s0140-6736(75)92899-8. [DOI] [PubMed] [Google Scholar]
  4. Gahmberg C. G., Hakomori S. I. External labeling of cell surface galactose and galactosamine in glycolipid and glycoprotein of human erythrocytes. J Biol Chem. 1973 Jun 25;248(12):4311–4317. [PubMed] [Google Scholar]
  5. Hakomori S. I., Koscielak J., Bloch K. J., Jeanloz R. W. Immunologic relationship between blood group substances and a fucose-containing glycolipid of human adenocarcinoma. J Immunol. 1967 Jan;98(1):31–38. [PubMed] [Google Scholar]
  6. Hakomori S. Structures and organization of cell surface glycolipids dependency on cell growth and malignant transformation. Biochim Biophys Acta. 1975 Mar 20;417(1):55–89. doi: 10.1016/0304-419x(75)90008-6. [DOI] [PubMed] [Google Scholar]
  7. MARSH W. L. Anti-i: a cold antibody defining the Ii relationship in human red cells. Br J Haematol. 1961 Apr;7:200–209. doi: 10.1111/j.1365-2141.1961.tb00329.x. [DOI] [PubMed] [Google Scholar]
  8. MASAMUNE H., KAWASAKI H., ABE S., OYAMA K., YAMAGUCHI Y. Molischpositive mucopolysaccharides of gastric cancers as compared with the corresponding components of gastric mucosae. 1. Fractionation procedure of gastric cancer and gastric mucosa. Tohoku J Exp Med. 1958 Jun 25;68(1):81–91. doi: 10.1620/tjem.68.81. [DOI] [PubMed] [Google Scholar]
  9. Marcus D. M., Cass L. E. Studies of blood group substances. 3. A caprine antiserum containing antibodies to two antigenic determinants on type H hog gastric mucin. J Immunol. 1967 Nov;99(5):987–993. [PubMed] [Google Scholar]
  10. Prendergast R. C., Toto P. D., Gargiulo A. W. Reactivity of blood group substances of neoplastic oral epithelium. J Dent Res. 1968 Mar-Apr;47(2):306–310. doi: 10.1177/00220345680470021801. [DOI] [PubMed] [Google Scholar]
  11. Richardson C. L., Baker S. R., Morré D. J., Keenan T. W. Glycosphingolipid synthesis and tumorigenesis. A role for the Golgi apparatus in the origin of specific receptor molecules of the mammalian cell surface. Biochim Biophys Acta. 1975 Dec 31;417(3-4):175–186. doi: 10.1016/0304-419x(75)90009-8. [DOI] [PubMed] [Google Scholar]
  12. SZULMAN A. E. The histological distribution of blood group substances A and B in man. J Exp Med. 1960 Jun 1;111:785–800. doi: 10.1084/jem.111.6.785. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Saito T., Hakomori S. I. Quantitative isolation of total glycosphingolipids from animal cells. J Lipid Res. 1971 Mar;12(2):257–259. [PubMed] [Google Scholar]
  14. Siddiqui B., Hakomori S. A ceramide tetrasaccharide of human erythrocyte membrane reacting with anti-type XIV pneumococcal polysaccharide antiserum. Biochim Biophys Acta. 1973 Dec 13;330(2):147–155. doi: 10.1016/0005-2736(73)90219-8. [DOI] [PubMed] [Google Scholar]
  15. Simmons D. A., Perlmann P. Carcinoembryonic antigen and blood group substances. Cancer Res. 1973 Feb;33(2):313–322. [PubMed] [Google Scholar]
  16. Springer G. F., Desai P. R. Human blood-group MN and precursor specificities: structural and biological aspects. Carbohydr Res. 1975 Mar;40(1):183–192. doi: 10.1016/s0008-6215(00)82680-4. [DOI] [PubMed] [Google Scholar]
  17. Stellner K., Hakomori S., Warner G. S. Enzymic conversion of "H1-glycolipid" to A or B-glycolipid and deficiency of these enzyme activities in adenocarcinoma. Biochem Biophys Res Commun. 1973 Nov 16;55(2):439–445. doi: 10.1016/0006-291x(73)91106-6. [DOI] [PubMed] [Google Scholar]
  18. Stellner K., Watanabe K., Hakomori S. Isolation and characterization of glycosphingolipids with blood group H specificity from membranes of human erythrocytes. Biochemistry. 1973 Feb;12(4):656–661. doi: 10.1021/bi00728a014. [DOI] [PubMed] [Google Scholar]
  19. Watanabe K., Laine R. A., Hakomori S. I. On neutral fucoglycolipids having long, branched carbohydrate chains: H-active and I-active glycosphingolipids of human erythrocyte membranes. Biochemistry. 1975 Jun 17;14(12):2725–2733. doi: 10.1021/bi00683a026. [DOI] [PubMed] [Google Scholar]
  20. Yang H. J., Hakomori S. I. A sphingolipid having a novel type of ceramide and lacto-N-fucopentaose 3. J Biol Chem. 1971 Mar 10;246(5):1192–1200. [PubMed] [Google Scholar]
  21. Yu R. K., Ledeen R. W. Gangliosides of human, bovine, and rabbit plasma. J Lipid Res. 1972 Sep;13(5):680–686. [PubMed] [Google Scholar]

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