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Gliadin 33-mer in coeliac disease pathogenesis, therapy and monitoring
Authors: P. Kocna
Authors‘ workplace: Ústav lékařské biochemie a laboratorní diagnostiky, 1. Lékařské fakulty Karlovy University a Všeobecné fakultní nemocnice, Praha
Published in: Klin. Biochem. Metab., 29, 2021, No. 2, p. 64-70
doi: https://doi.org/10.61568/kbm.2021.010Overview
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.
Keywords:
monitoring – Pathogenesis – Celiac disease – therapy – gluten-free diet – gliadine – gli-33mer – glutenase
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Clinical biochemistry Nuclear medicine Nutritive therapist
Article was published inClinical Biochemistry and Metabolism
2021 Issue 2-
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