Abstract
We have previously demonstrated that patients with coeliac disease have a characteristic gliadin antibody pattern dominated by reactivity against a few polypeptides in the γ-fraction. Recent gliadin- and hordein- (the prolamin fractions of wheat and barley) immunoadsorbent studies have shown, that the prolamin reactivity originates from the same population of antibodies. The antibody reactivity against separated hordein polypeptides was therefore investigated by immunoblotting, but a characteristic pattern could not be connected to coellac disease.
The combination of these observations on basis of detailed comparison of available amino acid sequences leads to the speculation, that distinct antigenic epitopes characteristic for coeliac disease may reside within the N-terminal region of gliadins.
The antibodies in patients with coeliac disease does however not react with a typical α-gliadin expressed by E.coli, which extends the indications that the antigenic epitopes are in the γ-gliadin fraction.
A determination of the aetiologically active peptide domains and an elucidation of the initial events of the pathogenesis should nevertheless be based on direct studies of the enterocytes under in vivo resembling conditions.
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Friis, S., Sjöström, H., Norén, O. et al. 38 THE PEPTIDE DOMAINS OF AETIOLOGICAL IMPORTANCE IN COELIAC DISEASE MAY RESIDE WITHIN THE N-TERMINAL REGION OF γ-GLIADIN. Pediatr Res 24, 411 (1988). https://doi.org/10.1203/00006450-198809000-00061
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DOI: https://doi.org/10.1203/00006450-198809000-00061
