1. Volume 125, Issue 3, Pages 696-707 (September 2003)
Alterations of the intestinal transport and processing of gliadin peptides in celiac disease 
Tamara Matysiak-Budnik, Celine Candalh, Christophe Dugave, Abdelkader Namane, Christophe Cellier, Nadine Cerf-Bensussan, Martine Heyman 
Gastroenterology 
Volume 125, Issue 3, Pages (September 2003)
DOI: /S (03)

2. Figure 3
(A) RP-HPLC chromatographic pattern of the native 3H peptide 31–49 before any experiment. (B) Typical elution profile of 3H peptide 31–49 after a 3-hour incubation in the mucosal compartment of duodenal biopsy specimens from controls. (C) Typical elution pattern of 3H metabolites found in the serosal compartment after transport across duodenal biopsy specimens from controls (the same profile was also found in most of the patients with TCD).
Gastroenterology  , DOI: ( /S (03) )

3. Figure 5
(A) RP-HPLC chromatographic pattern of the native 3H peptide 57–68 before any experiment. (B) The elution profile after a 3-hour incubation in the mucosal compartment of duodenal biopsy specimens from controls. (C) Typical elution profile of 3H peptide 57–68 metabolites in the serosal compartment after duodenal transport in controls.
Gastroenterology  , DOI: ( /S (03) )

4. Figure 8
(A) RP-HPLC chromatographic analysis of the native 3H 33-mer. The same profile was observed after 3 hours of incubation in the mucosal compartment (brush-border membrane) of controls, patients with ACD, or patients with TCD, indicating the absence of degradation. (B–D) Typical elution pattern of 3H 33-mer metabolites observed in the serosal compartment bathing a duodenal biopsy specimen after intestinal transport (3 hours) in controls, patients with ACD, and patients with TCD, respectively. The 33-mer peptide was almost totally degraded in controls and patients with TCD but only partially digested in patients with ACD.
Gastroenterology  , DOI: ( /S (03) )

5. Figure 1
(A) Evolution of the electrical resistance of control, ACD, and TCD duodenal biopsy specimens incubated in Ussing chambers in the presence of the gliadin peptides for 3 hours. (B) Initial electrical resistance immediately after mounting the biopsy specimens in the chambers. ∗P < 0.001, significantly different from controls; #P < , significantly different from TCD.
Gastroenterology  , DOI: ( /S (03) )

6. Figure 2
(A) 3H-equivalent peptide 31–49 fluxes (μg · 3 h−1 · cm2) across control, ACD, and TCD duodenal biopsy specimens mounted in Ussing chambers. ∗P < 0.01, significantly different from controls; #P < 0.002, significantly different from TCD. (B) 3H-equivalent peptide 57–68 fluxes (μg · 3 h−1 · cm2) across duodenal biopsy specimens. (C) 3H-equivalent 33-mer fluxes (μg · 3 h−1 · cm2).
Gastroenterology  , DOI: ( /S (03) )

7. Figure 4
(A) Typical RP-HPLC elution profile of the 3H peptide 31–49 after a 3-hour incubation with the mucosal side of a duodenal biopsy specimen from a patient with ACD. (B and C) Typical elution patterns of 3H metabolites found after transport of the 3H peptide 31–49 across duodenal biopsy specimens from patients with ACD. One half of the patients had the type I elution profile, and the remainder had the type II profile.
Gastroenterology  , DOI: ( /S (03) )

8. Figure 6
(A) Typical RP-HPLC chromatographic analysis of the 3H peptide 57–68 after 3 hours of contact with the mucosal side of a duodenal biopsy specimen from a patient with ACD (the same profiles were found in patients with TCD). (B) Typical elution pattern of 3H metabolites observed after duodenal transport of the 3H peptide 57–68 in patients with ACD.
Gastroenterology  , DOI: ( /S (03) )

9. Figure 7
Comparison of 3H peptide 31–49 and 3H peptide 57–68 metabolites found in the serosal compartment after transport across 2 adjacent duodenal biopsy specimens from the same patient with ACD with subtotal villus atrophy. These 2 biopsy specimens had an electrical resistance of 16.9 and 11.6 ohms · cm2 for peptides 31–49 and 57–68, respectively.
Gastroenterology  , DOI: ( /S (03) )