Galactosylation of serum IgA1 O-glycans in celiac disease

Academic Article

Abstract

  • In celiac disease, gluten ingestion provokes small-bowel mucosal injury and production of IgA autoantibodies against transglutaminase 2 (TG2). It has been suggested that in celiac patients IgA could mediate the transepithelial passage of gluten peptides in a mechanism involving the transferrin receptor. As IgA1 with galactose-deficient O-linked glycans has elevated affinity for the transferrin receptor, we assessed whether total serum IgA1 and IgA1 anti-TG2 autoantibodies in celiac patients are aberrantly glycosylated. We report that males with celiac disease have higher total serum levels of galactose-deficient IgA1 than non-celiac males. Furthermore, O-glycans of the disease-specific TG2 IgA1 autoantibodies in celiac patients exhibited elevated galactose deficiency. A gluten-free diet had no effect on the total serum levels of galactose-deficient IgA1, whereas the amount of galactose-deficient anti-TG2 IgA1 decreased. Thus, the undergalactosylated IgA1 molecules are not pathognomonic for celiac disease, but galactose deficiency in IgA1 could be an aggravating factor. © 2010 Springer Science+Business Media, LLC.
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    Digital Object Identifier (doi)

    Author List

  • Lindfors K; Suzuki H; Novak J; Collin P; Saavalainen P; Koskinen LLE; Mäki M; Kaukinen K
  • Start Page

  • 74
  • End Page

  • 79
  • Volume

  • 31
  • Issue

  • 1