The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Intestinal digestive resistance of immunodominant gliadin peptides
Abstract
Two recently identified immunodominant epitopes from α-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 exogeneous 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.
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Cites
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Coeliac disease: dissecting a complex inflammatory disorder
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Celiac disease: pathogenesis of a model immunogenetic disease
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Self-citation
Metadata
- Authors
- Hausch, F., Shan, L., Santiago, N. A., Gray, G. M., & Khosla, C.
- Venue
- American Journal of Physiology-Gastrointestinal and Liver Physiology
- Publisher
- American Physiological Society
- Published
- 2002-10-01
- Volume
- 283
- Issue
- 4
- Pages
- G996-G1003
- ISSN
- 0193-1857 (ISSN-L)
- 1522-1547
- OpenAlex
- W2168800337
- Cited by
- 375
- References
- 17
- FWCI
- 10.60
- Type
- journal article
- Language
- en
- Open access
- closed
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