Abstract Title:

Enamel defects associated with coeliac disease: putative role of antibodies against gliadin in pathogenesis.

Abstract Source:

Eur J Oral Sci. 2012 Apr ;120(2):104-12. PMID: 22409216

Abstract Author(s):

Florencia Muñoz, Natalia Del Río, Cecilia Sóñora, Inés Tiscornia, Alicia Marco, Ana Hernández

Article Affiliation:

Cátedra de Inmunología, Instituto de Química Biológica, Facultad de Ciencias, Universidad de la República Escuela Universitaria de Tecnología Médica, Facultad de Medicina, Universidad de la República Unidad de Biología Celular, Instituto Pasteur Montevideo Instituto de Pediatría, Facultad de Medicina, Universidad de la República, Montevideo. Uruguay.


Muñoz F, Del Río N, Sóñora C, Tiscornia I, Marco A, Hernández A. Enamel defects associated with coeliac disease: putative role of antibodies against gliadin in pathogenesis. Eur J Oral Sci 2012; 120: 104-112. © 2012 Eur J Oral Sci Enamel defects in the permanent teeth of patients with coeliac disease (CD) are often reported as an atypical manifestation, sometimes being suggestive of an undiagnosed atypical disease. We proposed to explore the pathogenesis of these oral defects, which are poorly studied. Sequence analyses of proteins from gluten (gliadins) and of proline-rich enamel proteins(amelogenin and ameloblastin) suggested the presence of common antigenic motifs. Therefore, we analyzed, by ELISA and western blotting, the reactivity of sera from patients with CD against gliadin and enamel-derived peptides. Correlation analyses between the levels of specific antibodies against gliadin and enamel derived peptides and inhibition experiments confirmed the presence of cross-reactive antibodies. Immunoblot analysis revealed that the most prominent component in enamel matrix derivative (of approximately 18.6 kDa), identified by an amelogenin-specific antibody, is recognized bysera from patients with CD; in addition, several fractions of pure gliadin were recognized by amelogenin-specific antibody. In agreement, sera from mice immunized with enamel matrix-derived proteins generated antibodies that recognized a peptide (of approximately 21.2 kDa) derived from gliadin. Inconclusion, antibodies against gliadin generated in patients with CD can react in vitro with a major enamel protein. The involvement of anti-gliadin serum in the pathogenesis of enamel defects in children with untreated CD can be hypothesized on the basis of these novel results.

Study Type : Human Study
Additional Links
Problem Substances : Gliadin : CK(821) : AC(118)

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