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- Title
Epithelial transport and deamidation of gliadin peptides: a role for coeliac disease patient immunoglobulin A.
- Authors
Rauhavirta, T.; Qiao, S.-W.; Jiang, Z.; Myrsky, E.; Loponen, J.; Korponay-Szabó, I. R.; Salovaara, H.; Garcia-Horsman, J. A.; Venäläinen, J.; Männistö, P. T.; Collighan, R.; Mongeot, A.; Griffin, M.; Mäki, M.; Kaukinen, K.; Lindfors, K.
- Abstract
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.
- Subjects
CELIAC disease; EPITHELIAL cells; DEAMINATION; IMMUNOGLOBULIN A; TRANSGLUTAMINASES; ENZYME kinetics; T cells; GLYCOPROTEINS
- Publication
Clinical & Experimental Immunology, 2011, Vol 164, Issue 1, p127
- ISSN
0009-9104
- Publication type
Article
- DOI
10.1111/j.1365-2249.2010.04317.x