The α-Galactosyl Epitope on Human Normal and Autoimmune Thyroid Cells

References

• Galili U, Rachmilewilz E A, Peleg A, Flechncr I. A unique natural human IgG antibody with anti-α-galactosyl specificity. J Exp Meet 1984; 160: 1519–1531
   PubMed Web of Science ®Google Scholar
• Galili U, Macher B A, Buehler J, Shohet SB. Human natural ami-α-galactosyl IgG. II. The specific recognition of α(1–3) linked galactose residues. J Exp Med 1985; 162: 573–582
   PubMed Web of Science ®Google Scholar
• Galili U, Buehler J, Shohet S B, Macher BA. The human natural anti-Gal IgG. III. The subtlety of immune tolerance in man as demonstrated by crossreactivity between natural anti-Gal and anti-B antibodies. J Exp Med 1987; 165: 693–704
   PubMed Web of Science ®Google Scholar
• Wieslander J, Månsson O, Kallin E, Gabrielli A, Nowak H, Timple R. Specificity of human antibodies against Galαl→3-Gal carbohydrate epitope and distinction from natural antibodies reacting with Galαl→2Gal or Galαl→4Gal. Glycocon-jugate J 1990; 7: 85–100
   Web of Science ®Google Scholar
• Towbin H, Rosenfelder G, Wieslander J, Avila J L, Rojas M, Szarfman A, Esser K, Nowack H, Timple R. Circulating antibodies to mouse laminin in Chagas disease, American cutaneous Leishmaniasis and normal individuals recognize terminal galactosyl (αl-3) galactose epitopes. J Exp Med 1987; 166: 419–432
   PubMed Web of Science ®Google Scholar
• Davin J C, Malaise M, Foidart J M, Mahieu P. Anti-α-galactosyl antibodies and immune complexes in children with Henoch-Schpnlein purpura or IgA nephropathy. Kidney Int 1987; 31: 1132–1139
   PubMed Web of Science ®Google Scholar
• Galili U, Clark M R, Shohet S B, Buehler J, Macher BA. Evolutionary relationship between the anti-Gal antibody and the Galαl→3Gal epitope in primates. Proc Nail Acad Sci USA 1987; 84: 1369–1373
   PubMed Web of Science ®Google Scholar
• Galili U, Shohet S B, Kobrin E, Stults C LM, Macher BA. Man, apes, and Old World monkeys differ from other mammals in the expression of α-galactosyl epitopes on nucleated cells. J Biol Chem 1988; 263: 17755–17762
   PubMed Web of Science ®Google Scholar
• Thall A, Galili U. Distribution of Galαl→3GalβJ1→4GlcNAc residues on secreted mammalian glycoproteins (thyroglobulin, fibrinogen and immunoglobulin G) as measured by a sensitive radioimmunoassay. Biochemistry 1990; 29: 3959–3965
   PubMed Web of Science ®Google Scholar
• Ravindran B, Satapathy A K, Das MK. Naturally occurring anti-α-galactosyl antibodies in human Plasmodium falciparum infections-a possible role for autoantibodies in malaria. Immunol Lett 1988; 19: 137–142
   PubMed Web of Science ®Google Scholar
• Galili U, Mandrell R E, Hamadeh R M, Shohet S B, Griffiss JM. The interaction between the human natural anti-α-galactosyl IgG (anti-Gal) and bacteria of the human flora. Infect Immun 1988; 57: 1730–1737
   Google Scholar
• Joziasse D H, Shaper J H, Van den Eijnden D H, Van Tunen A H, Shaper NL. Bovine αl-3 galactosyltransferase: Isolation and characterization of a cDNA clone. Identification of homologous sequences in human genomic DNA. J Biol Chem 1989; 264: 14290–14297
   PubMed Web of Science ®Google Scholar
• Larsen R D, Rivera-Marrero C A, Ernest L E, Cummings R D, Lowe JB. Frameshift and nonsense mutations in a human genomic sequence homologous to a murine UDP-Gal: βD-Gal(l,4)-D-GlcNAcα(1,3)-galactosyltransferase cDNA. J Biol Chem 1990; 265: 7055–7061
   PubMed Web of Science ®Google Scholar
• Castronovo V, Parent B, Steeg P S, Colin C, Foidart J M, Lambotte R, Mahieu F. Human natural anti-Gal antibodies may play a role in the natural anti-tumor defense system. J Natl Cancer Inst 1989; 81: 212–216
   PubMed Web of Science ®Google Scholar
• Kagawa Y, Takasaki S, Utsumi J, Hasoi K, Shimizu H, Kochibe N, Kobata A. Comparative study of the asparagine-linked sugar chains of natural human interferon-β1 and recombinant human interferon-β1 produced by three different mammalian. cells. J Biol Chem 1988; 263: 17508–17515
   PubMed Web of Science ®Google Scholar
• Galili U, Clark M R, Shohet SB. Excessive binding of the natural anti-α-galactosyl IgG to sickle red cells may contribute to extravascular cell destruction. J Clin Invest 1986; 77: 27–33
   PubMed Web of Science ®Google Scholar
• Galili U. Abnormal expression of α-galactosyl epitopes in man: A trigger for autoimmune processes. Lancet 1989; ii: 358–361
   Google Scholar
• Etienne-Decerf J, Mahieu P, Malaise M, Winand R. Measurement of anti-α-galactosyl antibodies in the course of various thyroid disorders and isolation of an antigenic glycopeptide fraction. Thyroid Autoimmunity, A Pinchera, SH Ingbar, JM McKenzie, GF Fenzi. Plenum Press. 1987; 297–301
   Google Scholar
• Etienne-Decerf J, Malaise M, Mahieu P, Winand R. Elevated anti-α-galactosyl antibody tilers. A marker of progression in autoimmune thyroid disorders and in endocrine ophthalmology. Acta Endocrinol 1987; 115: 67–74
   PubMedGoogle Scholar
• Im W B, Christensen H N, SportÍs B. Amino acid stimulation of ATP cleavage by two Ehrlich cell membrane preparations in the presence of ouabain. Biochim Biophys Acta 1979; 436: 424–430
   Google Scholar
• Elices M, Goldstein U. Glycosyltransferase activities of Ehrlich ascites tumor cells: Detection, isolation and characterization using oligosaccharide-Synsorb beads. Arch Biochem Biophys 1987; 254: 329–341
   PubMed Web of Science ®Google Scholar
• Peterson GL. A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal Biochem 1977; 83: 346–356
   PubMed Web of Science ®Google Scholar
• Edge A SB, Spiro RG. Thyroid cell surface glycoproteins. Nature and disposition of carbohydrate units and elevation of their blood group I activity. J Biol Chem 1985; 260: 15332–15338
   PubMed Web of Science ®Google Scholar
• Hakomori S. Tumor-associated carbohydrate antigens. Ann Rev Immunol 1984; 2: 103–126
   PubMed Web of Science ®Google Scholar
• Wilkin T. Autoimmunity: Attack or defence? (The case for a primary lesion theory.). Autoimmunity 1989; 3: 57–73
   PubMed Web of Science ®Google Scholar