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• W4213065850 abstract "Celiac disease (CD) arises in genetically susceptible individuals in response to gliadin peptides found in gluten-containing cereals. There is evidence that these peptides are both toxic and immunostimulatory. For instance, peptide 31–49 (spanning amino acids 31 to 49) appears to have cytotoxic properties both in vitro and in vivo, whereas peptide 57–68 may be an immunostimulant to DQ2-restricted gliadin-specific intestinal CD4+ T cells found in most patients with CD. Many peptides containing these epitopes are generated from hydrolysis of gliadin by pancreatic and intraluminal peptidases, e.g., an alpha-2 gliadin-derived 33-mer peptide containing not only the 57–68 sequence but also 2 other major T cell- recognized epitopes resistant to intraluminal degradation. In normal subjects, these peptides may be further degraded intracellularly, thus preventing their absorption. In CD, however, it is possible that defective hydrolysis of these peptides results in sufficient quantity being absorbed to activate immunomodulatory lymphocytes in the lamina propria. This study therefore investigates the possibility that a defect in the transport and/or processing of gliadin peptides by intestinal epithelial cells participates in the pathogenesis of CD. Studies were performed in duodenal biopsy specimens from control subjects and from patients with active celiac disease (ACD) and treated celiac disease (TCD), the latter group representing patients in remission after treatment with a gluten-free diet. Biopsy specimens were mounted in Ussing chambers, devices that allow measurement of electrical resistance (R), mucosal to serosal radiolabeled-peptides fluxes, and peptide processing during transport using radio-RP-HPLC (Figure 1). In ACD patients, the transport of peptide 31–49 was significantly increased compared with control and TCD patients, whereas no increases were observed for peptide 57–68 or 56–89 (33-mer). This increase was not caused by the overall decrease in barrier function of the mucosa, because there were no changes in transport of the other 2 peptides. Of note, peptide 57–68 was found to be partially degraded by brush-border peptidases in controls but not in CD patients, and was totally degraded after intestinal transport in all groups. Peptides 31–49 and 56–89 were resistant to brush-border peptidases in all groups of patients, but were totally degraded by mucosal cells in controls and patients with TCD. In contrast, 50% of peptide 31–49 was transported intact in patients with ACD and only partial degradation of the 33-mer was observed. These data therefore suggest that gliadin peptides, although poorly or not digested by intraluminal enzymes, are fully digested by mucosal cells of controls and patients with TCD. In contrast, there is only partial degradation of the 33-mer and increased transport of peptide 31–49 in patients with ACD. These changes increase the likelihood of the peptides in reaching the lamina propria, thereby exerting immunostimulatory and toxic effects that may result in the development of CD. These data are potentially exciting, providing insights that require further study." @default.
• W4213065850 created "2022-02-24" @default.
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• W4213065850 date "2003-09-01" @default.
• W4213065850 modified "2023-09-26" @default.
• W4213065850 title "This month in gastroenterology" @default.
• W4213065850 doi "https://doi.org/10.1016/s0016-5085(03)01070-9" @default.
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