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Immunoreactivity of Antibodies Against Transglutaminase-Deamidated Gliadins in Adult Celiac Disease

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Abstract

Background The significance of the presence of anti-gliadin antibodies in patients affected by celiac disease is still unclear. It is hypothesized that gliadin deamidation, catalysed by transglutaminase, plays a role in favoring the antigen presentation. Aim To determine the immunoreactivity of anti-gliadin antibodies from untreated celiac patients to transglutaminase deamidated gliadins. Materials and methods Gliadins from wheat flour underwent enzymatic digestion and were deamidated or cysteamine-transamidated by transglutaminase. Immunoreactivity of anti-gliadin antibodies from untreated adult celiac patients sera was evaluated by means of a competitive enzyme-linked immunosorbent assay (ELISA) method. Results Gliadin deamidation increased antibodies immunoreactivity from 25% to 50% while cysteamine incorporation into the gliadin peptides resulted in an immunoreactivity decrease. Conclusions Increased immunoreactivity of transglutaminase deamidated gliadins tested with anti-gliadin antibodies from untreated adult celiac patients supports the hypothesis of a pivotal role of gliadin deamidation in the pathomechanism of celiac disease.

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Acknowledgements

The authors particularly thank the Lombardy Section of the Italian Association for Celiac Disease for its support.

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Correspondence to Luca Elli.

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Falini, M.L., Elli, L., Caramanico, R. et al. Immunoreactivity of Antibodies Against Transglutaminase-Deamidated Gliadins in Adult Celiac Disease. Dig Dis Sci 53, 2697–2701 (2008). https://doi.org/10.1007/s10620-007-0191-9

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  • DOI: https://doi.org/10.1007/s10620-007-0191-9

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