Epithelial transport and deamidation of gliadin peptides: a role for coeliac disease patient immunoglobulin A

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In coeliac disease, the intake of dietary gluten induces small-bowel mucosal damage and the production of immunoglobulin (Ig)A class autoantibodies against transglutaminase 2 (TG2). We examined the effect of coeliac patient IgA on the apical-to-basal passage of gluten-derived gliadin peptides p31-43 and p57-68 in intestinal epithelial cells. We demonstrate that coeliac IgA enhances the passage of gliadin peptides, which could be abolished by inhibition of TG2 enzymatic activity. Moreover, we also found that both the apical and the basal cell culture media containing the immunogenic gliadin peptides were able to induce the proliferation of deamidation-dependent coeliac patient-derived T cells even in the absence of exogenous TG2. Our results suggest that coeliac patient IgA could play a role in the transepithelial passage of gliadin peptides, a process during which they might be deamidated.

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Original languageEnglish
Pages (from-to)127-136
Number of pages10
JournalClinical and Experimental Immunology
Issue number1
Early online date1 Jan 2011
Publication statusPublished - Apr 2011


  • amides, amino acid sequence, autoantibodies, caco-2 cells, celiac disease, cell proliferation, enzyme inhibitors, epithelial cells, GTP-binding proteins, gliadin, humans, immunoglobulin A, small intestine, peptide fragments, protein transport, T-lymphocytes, transglutaminases

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