Gluten immunochemistry to react with gamma gliadin to a degree comparable to DQ2.5. T-cell responses to the high molecular weight glutenin may be more important with DQ8 mediated than DQ2.5 mediated celiac disease. Antibody recognition of gluten is complex. Direct binding to gluten such as anti-gliadin antibodies has an ambiguous pathogenesis in coeliac disease. The crosslinking of gliadin with tissue transglutaminase leads to the production of anti-transglutaminase antibodies, but this is mediated through T-cell recognition of gliadin. The allergic recognition of gliadin by mast cells, eosinophiles in the presence of IgE has notable direct consequences, such as exercise-induced anaphylaxis. Anti-gliadin antibodies, like
Gliadin main types of gliadin (α, γ, and ω), to which the body is intolerant in coeliac (or celiac) disease. Diagnosis of this disease has recently been improving. Gliadin can cross the intestinal epithelium. Breast milk of healthy human mothers who eat gluten-containing foods presents high levels of non-degraded gliadin. The α, γ, and ω gliadin types are separated and distinguished based on their amino acid sequences. Gliadins are prolamins and are separated on the basis of electrophoretic mobility and isoelectric focusing. Gliadin peptides cross the intestinal barrier by active transport.. Gliadins are known for their role, along with glutenin, in