+1 Recommend
0 collections
      • Record: found
      • Abstract: found
      • Article: not found

      Intestinal digestive resistance of immunodominant gliadin peptides.

      American Journal of Physiology - Gastrointestinal and Liver Physiology
      Amino Acid Sequence, Animals, Cattle, Digestion, Dipeptidyl Peptidase 4, metabolism, Endopeptidases, Epitopes, chemistry, Female, Gliadin, immunology, Humans, Intestinal Mucosa, ultrastructure, Intestine, Small, Intestines, Microvilli, Pancreas, enzymology, Peptides, Rats, Serine Endopeptidases, Substrate Specificity, Swine

      Read this article at

          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.


          Two recently identified immunodominant epitopes from alpha-gliadin account for most of the stimulatory activity of dietary gluten on intestinal and peripheral T lymphocytes in patients with celiac sprue. The proteolytic kinetics of peptides containing these epitopes were analyzed in vitro using soluble proteases from bovine and porcine pancreas and brush-border membrane vesicles from adult rat intestine. We showed that these proline-glutamine-rich epitopes are exceptionally resistant to enzymatic processing. Moreover, as estimated from the residual peptide structure and confirmed by exogenous peptidase supplementation, dipeptidyl peptidase IV and dipeptidyl carboxypeptidase I were identified as the rate-limiting enzymes in the digestive breakdown of these peptides. A similar conclusion also emerged from analogous studies with brush-border membrane from a human intestinal biopsy. Supplementation of rat brush-border membrane with trace quantities of a bacterial prolyl endopeptidase led to the rapid destruction of the immunodominant epitopes in these peptides. These results suggest a possible enzyme therapy strategy for celiac sprue, for which the only current therapeutic option is strict exclusion of gluten-containing food.

          Related collections

          Author and article information


          Comment on this article