Abnormal expression of alpha-galactosyl epitopes in man. A trigger for autoimmune processes?

Lancet. 1989 Aug 12;2(8659):358-61. doi: 10.1016/s0140-6736(89)90539-4.

Abstract

1% of circulating IgG in man is anti-Gal antibody, which interacts specifically with the carbohydrate structure Gal alpha 1----3Gal beta 1----4GlcNAc-R on mammalian glycoconjugates (described throughout as the alpha-galactosyl epitope). This epitope is abundant on cell surface glycoconjugates of non-primate mammals, prosimians, and New World monkeys. It is not found on cells of Old World monkeys, apes, and man because of diminished alpha 1----3 galactosyltransferase enzyme activity. However, the alpha 1----3 galactosyltransferase gene seems to be present within the human genome. A mechanism that increases alpha 1----3 galactosyltransferase activity in human cells could trigger an autoimmune process mediated by anti-Gal binding to the newly synthesised alpha-galactosyl epitopes.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Autoantibodies / analysis*
  • Autoimmune Diseases / enzymology*
  • Biological Evolution
  • Epitopes / analysis*
  • Galactosyltransferases / genetics
  • Galactosyltransferases / immunology*
  • Galactosyltransferases / metabolism
  • Genes, Recessive
  • Glycoconjugates / immunology*
  • Humans
  • Immunoglobulin G / analysis*
  • Suppression, Genetic

Substances

  • Autoantibodies
  • Epitopes
  • Glycoconjugates
  • Immunoglobulin G
  • Galactosyltransferases