Diversity of oat varieties in eliciting the early inflammatory events in celiac disease

Eur J Nutr. 2014 Aug;53(5):1177-86. doi: 10.1007/s00394-013-0617-4. Epub 2013 Nov 19.

Abstract

Purpose: Celiac disease (CD) is an autoimmune enteropathy, triggered by dietary gluten. The only treatment is a strict gluten-free diet. Oats are included in the list of gluten-free ingredients by European Regulation, but the safety of oats in CD is still a matter of debate. The present study examined the capability of different oat cultivars of activating the gliadin-induced transglutaminase-2 (TG2)-dependent events in some in vitro models of CD. In addition, we compared this capability with the electrophoresis pattern of peptic-tryptic digests of the proteins of the oat cultivars.

Methods: K562(S) cells agglutination, transepithelial electrical resistance of T84-cell monolayers, intracellular levels of TG2 and phosphorylated form of protein 42-44 in T84 cells were the early gliadin-dependent events studied.

Results: The results showed that the Nave oat cultivar elicited these events, whereas Irina and Potenza varieties did not. The ability of a cultivar to activate the above-described events was associated with the electrophoretic pattern of oat proteins and their reactivity to anti-gliadin antibodies.

Conclusion: We found significant differences among oat cultivars in eliciting the TG2-mediated events of CD inflammation. Therefore, the safety of an oat cultivar in CD might be screened in vitro by means of biochemical and biological assays, before starting a clinical trial to definitely assess its safety.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Avena / adverse effects*
  • Avena / chemistry
  • Avena / classification*
  • Celiac Disease / immunology*
  • Cell Line, Tumor
  • Child
  • Diet, Gluten-Free
  • Duodenum / pathology
  • Electrophoresis, Polyacrylamide Gel
  • Female
  • GTP-Binding Proteins / immunology
  • GTP-Binding Proteins / metabolism
  • Gliadin / chemistry*
  • Humans
  • K562 Cells
  • Male
  • Phosphorylation
  • Protein Glutamine gamma Glutamyltransferase 2
  • Transglutaminases / immunology
  • Transglutaminases / metabolism

Substances

  • Gliadin
  • Protein Glutamine gamma Glutamyltransferase 2
  • Transglutaminases
  • GTP-Binding Proteins