Deamidation of gliadin peptides in lamina propria: implications for celiac disease
| Autor: | Hans Sjöström, Dorit Anthonsen, Hanne Skovbjerg, E. Knudsen |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Glutens
Physiology Tissue transglutaminase medicine.drug_class Duodenum Ovalbumin Swine Biopsy Immunofluorescence Monoclonal antibody digestive system Epitope Coeliac disease Antibodies Gliadin medicine Animals Humans Deamidation Lamina propria Mucous Membrane Transglutaminases biology medicine.diagnostic_test Gastroenterology food and beverages nutritional and metabolic diseases Serum Albumin Bovine medicine.disease digestive system diseases Rats Celiac Disease Disease Models Animal medicine.anatomical_structure Biochemistry Deamination biology.protein Peptides |
| Zdroj: | Digestive diseases and sciences. 53(11) |
| ISSN: | 0163-2116 |
| Popis: | Activation of small intestinal gluten-reactive CD4(+) T-cells is a critical event in celiac disease. Deamidation of specific glutamine residues by tissue transglutaminase enhances the binding of T-cell activating gliadin epitopes to DQ2, increasing T-cell recognition. Our purpose was to investigate whether deamidated gliadin epitopes can be generated in the small intestinal mucosa by tissue transglutaminase and to characterize the location of the process. Intestinal explants from pig intestine and frozen biopsy slices from human and rat intestine were incubated with alpha-gliadin peptides containing the immunodominant motif. Monoclonal antibodies specifically recognizing the non-deamidated and/or the deamidated epitope were used for immunofluorescence studies. We conclude that endogenous tissue transglutaminase can mediate extracellular deamidation of gliadin peptides in the lamina propria. Gliadin peptides with more than one recognition site can be simultaneously cross-linked and deamidated extracellularly in the lamina propria, and might be of importance for the antibody response seen in untreated celiac disease patients. |
| Databáze: | OpenAIRE |
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