Gliadin the formation of gluten. They are slightly soluble in ethanol and contain only intramolecular disulfide links. They also cause some of the best examples of food-derived pathogenesis. People with gluten-sensitive enteropathy (the severe form of which is celiac disease) are sensitive to α, β, and γ gliadins. Those with WD urticaria and Baker's asthma are sensitive to ω-gliadins. Gliadin can also serve as a useful delivery method for sensitive enzymes (such as superoxide dismutase, which is fused with gliadin to form glisodin) – this helps protect them from stomach acids that cause breakdown. For useful description of the gliadins see:
Gluten immunochemistry revealed no mutation that would increase risk for MICA. HLA-DQ proteins present polypeptide regions of proteins of about 9 amino acids and larger in size (10 to 14 residues in involved in binding is common for gliadin) to T lymphocytes. Gliadin proteins can be adsorbed by APC. After digestion in the lysozomes of APCs, glaidin peptides can be recycled to the cell's surface bound to DQ, or they can be bound and presented directly from the cell surface. The major source of inflammatory gluten is dietary gluten. Optimal reactivity of gliadin occurs when the protein is partially digested by small