Gliadin intolerance of wheat, barley and rye – all of which contain prolamins. Gliadin proteins have the ability to provoke an autoimmune enteropathy caused by an abnormal immune response in genetically susceptible individuals. Specific amino acid sequences within the gliadin proteins are responsible for this activity. The main problems with this disease is that it often goes unrecognized for many years, in which it can cause serious damage to several organs, and most cases currently remain unrecognized, undiagnosed and untreated. Mainly intestinal villi destruction mediated by Interferon Gamma and CD 4(+). Celiac disease with "non-classic symptoms" is the most common clinical
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