A detailed lectin analysis of IgG glycosylation, demonstrating disease specific changes in terminal galactose and N-acetylglucosamine

J Autoimmun. 1997 Feb;10(1):77-85. doi: 10.1006/jaut.1996.0104.

Abstract

Serum IgG from rheumatoid arthritis patients contains a decreased number of oligosaccharide structures ending in galactose and thus there is an increase in N-acetylglucosamine as the terminal sugar, compared with healthy individuals. The relationship between these two sugars varies depending on the disease examined: IgG from patients with rheumatoid arthritis, juvenile onset chronic arthritis and Crohn's disease are at one extreme, and exhibit a reciprocal galactose:N-acetylglucosamine relationship, while Sjögren's syndrome and osteoarthritis IgG are at the other extreme, exhibiting a parallel increase in the expression of both galactose and N-acetylglucosamine. These results may occur as a consequence of more than one glycosylation site which is differentially glycosylated, but more likely by changes in the level of bisecting N-acetylglucosamine.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylglucosamine / metabolism*
  • Adult
  • Aged
  • Aged, 80 and over
  • Arthritis, Rheumatoid / immunology
  • Arthritis, Rheumatoid / metabolism
  • Galactose / metabolism*
  • Glycosylation
  • Humans
  • Immunoglobulin G / metabolism*
  • Lectins / metabolism
  • Middle Aged
  • Oligosaccharides / metabolism
  • Sjogren's Syndrome / immunology
  • Sjogren's Syndrome / metabolism

Substances

  • Immunoglobulin G
  • Lectins
  • Oligosaccharides
  • Acetylglucosamine
  • Galactose