Abstract
Celiac disease is an autoimmune disease with genetically determined HLA class II binding DQ2 or DQ8 characterized by intestinal T cell responses to wheat gluten proteins in the diet. The unique α2-gliadin peptide fragment, gliadin-33mer, is considered to be the most important immunogenic sequence in gluten, this peptide is completely resistant to gastrointestinal peptidases and is completely specific for prolamins.
Gliadin 33-mer is a stimulator of CD4-T cells after deamidation by tissue transglutaminase. The only proven treatment for celiac disease is a lifelong gluten-free diet, and several new therapeutic approaches are currently being developed.
The enzymatic cleavage of gluten by glutenases with a focus on the cytotoxic gliadin 33-mer has been verified in a number of clinical studies. Detection of gluten immunogenic peptides, gliadin 33-mer, in faeces and urine is becoming a new non-invasive biomarker and offers a new simple and objective way to assess gluten intake and verify compliance with a gluten-free diet in patients with celiac disease.
In the diagnosis of celiac disease allows you to reliably verify non-responsive celiac disease.