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Diagnostic criteria for coeliac disease and transient gluten intolerance.
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Diagnostic criteria for coeliac disease and transient gluten intolerance.
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Gluten and serum cholesterol.
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Diagnosing gluten intolerance.
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Gluten IgA antibodies and coeliac disease.
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Persistent decreased plasma cholecystokinin levels in celiac patients under gluten-free diet: respective roles of histological changes and nutrient hydrolysis.
Celiac disease is associated with impaired cholecystokinin (CCK) release. The mechanism by which CCK release is impaired is poorly understood and seems to be related to the mucosal atrophy or to decreased stimulation due to reduced intraduodenal nutrient hydrolysis. The aims of our study were to evaluate basal and postprandial CCK in celiac patients presenting with distinctive types of mucosal lesions (normal, infiltrative and atrophic), and to study the role of protein hydrolysis on CCK release. Plasma CCK was measured in 20 celiac patients (normal mucosa: n=6; infiltrative type: n=6; atrophic type=8) and 9 controls, before and after ingestion of a polymeric or a semi-elemental meal. Significant decreases in basal CCK plasma (B 0.6 [95% CI, 0.3-1.3] pmol/l; p<0.003) and postprandial CCK area under curve (AUC 34 [19-61] pmol/l x 120 min, p<0.0001) were observed in patients with an atrophic mucosa compared with treated patients (B 1.6 [1.0-2.4] pmol/l, AUC 267 [172-414] pmol/l x 120 min) or healthy volunteers (B 1.0 [0.7-1.4] pmol/l, AUC 186 [131-264] pmol/l x 120 min). A significant defective CCK release was also observed in patients with an infiltrative type: B 0.4 [0.2-0.7] pmol/l and AUC 56 [31-101] pmol/l x 120 min; p<0.0001. Administration of a semi-elemental diet did not correct the defective CCK release. In conclusion, the decreased CCK levels observed in celiac patients are not strictly related to the mucosal atrophy but rather to the lymphocytic infiltrate. Administration of a predigested meal did not correct the impaired CCK release. Some inhibitory mechanism could be involved in the CCK cell dysfunction observed in celiac patients presenting with lesser degrees of disease activity.
Quality of life of celiac patients living on a gluten-free diet.
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Dysmotility-like dyspeptic symptoms in coeliac patients: role of gluten and Helicobacter pylori infection.
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New insight into the solution structures of wheat gluten proteins from Raman optical activity.
Vibrational Raman optical activity (ROA) spectra of the wheat proteins alpha-gliadin (A-gliadin), omega-gliadin, and a 30 kDa peptide called T-A-1 from the high molecular weight glutenin subunit (HMW-GS) Dx5 were measured to obtain new information about their solution structures. The spectral data show that, under the conditions investigated, A-gliadin contains a considerable amount of hydrated alpha-helix, most of which probably lies within a relatively structured C-terminal domain. Smaller quantities of beta-structure and poly(l-proline) II (PPII) helix were also identified. Addition of methanol was found to increase the alpha-helix content at the expense of some of the beta and PPII structure. In comparison, omega-gliadin and the T-A-1 peptide were found to consist of large amounts of well-defined PPII structure with some turns but no alpha-helix. The results for the T-A-1 peptide are in agreement with a model in which HMW-GS are extended but not highly rigid. Application of a pattern recognition technique, based on principal component analysis (PCA), to the ROA spectra reinforces these conclusions.
Lectins in wheat gluten proteins.
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Comparison of the utilization of supplemented wheat gluten and other amino acid sources in the rat.
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Preparation and isolation of acid-catalyzed hydrolysates from wheat gluten.
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Preparation and properties of acid-solubilized gluten.
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Covalent attachment of lysine to wheat gluten for nutritional improvement.
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Growth response of mice and Tetrahymena pyriformis to lysinoalanine-supplemented wheat gluten.
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Physicochemical behaviors of sugars, lipids, and gluten in short dough and biscuit.
The structure of short dough and biscuit has been characterized at a macroscopic level (dimensions, bulk structure) and a microscopic level (starch damage, protein aggregates, microstructure) by physical and biochemical methods. The baking process of short dough induces a large decrease of the product bulk density from 1.26 to 0. 42 (+/-0.01) g.cm(-)(3) for final biscuit, leading to a cellular solid with a thin colored surface and a porous inner structure. Proteins appear aggregated in biscuit when compared to short dough, whereas starch granules remain almost intact in biscuits. The components which are involved in the cohesiveness of short dough and biscuit final structure have been identified. They suggest that short dough is a suspension of solid particles in a liquid phase being an emulsion of lipids in a concentrated sugar solution. The role of sugars in biscuit structure suggest that biscuit structure is a composite matrix of protein aggregates, lipids and sugars, embedding starch granules.