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.

Immunoreactivity of antibodies against transglutaminase-deamidated gliadins in adult celiac disease / M.L. Falini, L. Elli, R. Caramanico, M.T. Bardella, C. Terrani, L.R. Roncoroni, L. Doneda, F. Forlani. - In: DIGESTIVE DISEASES AND SCIENCES. - ISSN 0163-2116. - 53:10(2008 Oct), pp. 2697-2701.

Immunoreactivity of antibodies against transglutaminase-deamidated gliadins in adult celiac disease

M.L. Falini;L. Elli;R. Caramanico;M.T. Bardella;C. Terrani;L.R. Roncoroni;L. Doneda;F. Forlani
2008-10

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.
Anti-gliadin antibodies; Celiac disease; Gliadin; Transglutaminase
Settore MED/12 - Gastroenterologia
Settore BIO/13 - Biologia Applicata
DIGESTIVE DISEASES AND SCIENCES
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2434/43816
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