Abstract
There is considerable information on the structure and genetics of the peripheral regions of the complex carbohydrate chains of mucins which vary depending on blood group isotype specificity (1). However, much less is known of the detailed structures and biosynthetic control within the backbone and core regions of these chains. The backbones consist of either Type 1,
sequences (1) and they vary in length and branching. Type 2 sequences in the liner repeating structure
are recognized by anti-blood group i antibodies (2). Addition of a \({\rm{Ga1\beta 1}} \to 4{\rm{G1cNAc\beta 1}} \to 6\) branch onto the internal galactose of this structure confers blood group I activity (3). Type 1 sequences are apparently not involved in the Ii antigenic system. Species and individual differences in blood group I and i activities may therefore reflect differences in branching patterns and the proportions of Type 1 and Type 2 chain sequences. Ii activities may also be masked by further glycosylation, for example by the addition of sugar residues confering blood group ABH activities.
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Literature
W.M. Watkins, Biochemistry and genetics of the ABO, Lewis and P blood group systems, in: Advances in Human Genetics, Hirschhorn K, Harris, H., eds. Vol. 10. Plenum Publishing Co. pp 1 and 379 (1980).
H. Niemann, K. Watanabe, S. Hakomori, R.A. Childs, and T. Feizi, Blood group i and I activities of “Lacto-N-nor-hexaosyl-ceramide” and its analogues: the structural requirements for i-specificities. Biochem. Biophys. Res. Commun. 81: 1286 (1978).
T. Feizi, R.A. Childs, K. Watanabe, and S. Hakomori, Three types of blood group I specificity among monoclonal anti-I autoantibodies revealed by analogues of a branched erythrocyte glycolipid. J. Exp. Med. 149: 975 (1979).
R.N. Iyer and D.M. Carlson. Alkaline borohydride degradation of blood group H substance. Arch. Biochem. Biophys. 142: 101 (1971).
E.F. Hounsell, M. Fukuda, M.E. Powell, T. Feizi, and S. Hakomori. A new O-glycosidically linked tri-hexosamine core structure in sheep gastric mucin: a preliminary note. Biochem. Biophys. Res. Commun. 92: 1143 (1980).
V.A. Derevitskaya, N.P. Arbatsky, and N.K. Kochetkov. The structure of carbohydrate chains of blood-group substance. Eur. J. Biochem. 86: 423 (1978).
E.F. Hounsell, E. Wood, T. Feizi, M. Fukuda, M.E. Powell, and S. Hakomori. Hexa-octasaccharide fractions isolated from blood group I and i active sheep gastric glycoproteins Carbohyd. Res. 90: 283 (1981).
B.L. Slomiany and K. Meyer. Oligosaccharide produced by acetolysis of blood group active (A + H) sulfated glycoproteins from hog gastric mucin. J. Biol. Chem. 248: 2290 (1973).
J. Picard, D. Waldron-Edward, and T. Feizi. Changes in the expression of the blood group A,B,H, Lea and Leb antigens and the blood group precursor associated I(Ma) antigen in glycoprotein-rich extracts of gastric carcinomas. J. Clin. & Lab. Immunol. 1: 119 (1978).
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© 1982 Plenum Press, New York
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Hounsell, E.F., Lawson, A.M., Feizi, T. (1982). Structural and Antigenic Diversity in Mucin Carbohydrate Chains. In: Chantler, E.N., Elder, J.B., Elstein, M. (eds) Mucus in Health and Disease—II. Advances in Experimental Medicine and Biology, vol 144. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9254-9_3
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DOI: https://doi.org/10.1007/978-1-4615-9254-9_3
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