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Anti-gliadin antibodies were one of the first serological markers for coeliac disease. Problematic with AGA is the typical sensitivity and specificity was about 85%. Gliadin peptides which are synthesized as the deamidated form have much higher sensitivity and specificity, creating 2 serological tests for CD that approach biopsy diagnostic in ...
Deamidated gliadin peptides are more inflammatory relative to natural peptides. Deamidated gliadin is also found in foods that have added gluten, such as wheat bread, food pastes. The major gluten proteins that are involved in coeliac disease are the α-gliadin isoforms. Alpha gliadin is composed of repeated motifs that, when digested, can be ...
Deamidation reactions have been conjectured to be one of the factors that limit the useful lifetime of proteins. [1]Deamidation proceeds much more quickly if the susceptible amino acid is followed by a small, flexible residue such as glycine whose low steric hindrance leaves the peptide group open for attack.
In disease, transglutaminase reacts with gliadin forming a linkage. [21] In forming this bond transglutaminase becomes linked to T-cell epitopes on gliadin. B-cells with surface IgM that react to transglutaminase can present it with bound gliadin peptides to T-cells which stimulate B-cell maturation and proliferation to plasma cells making IgA ...
Enteropathy-associated T-cell lymphoma (EATL), previously termed enteropathy-associated T-cell lymphoma, type I and at one time termed enteropathy-type T-cell lymphoma (ETTL), is a complication of coeliac disease in which a malignant T-cell lymphoma develops in areas of the small intestine affected by the disease's intense inflammation. [1]
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The immunodominant site for DQ2.5 is on α2-gliadin. The site is a protease resistant 33mer that has 6 overlapping DQ2.5 restricted epitopes. This creates very strong binding of T-cells for DQ2.5-33mer complexes. DQ2.5 binds gliadin, but the binding is sensitive to deamidation caused by tissue transglutaminase. In almost all case the highest ...
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