Gliadin Deamidated gliadin is produced by acid or enzymatic treatment of gluten. The enzyme tissue transglutaminase converts some of the abundant glutamines to glutamic acid. This is done because gliadins are soluble in alcohol and cannot be mixed with other foods (like milk) without changing the foods' qualities. Deamidated gliadin is soluble in water. The cellular immunity to deamidated α-/β-gliadin is much greater than α/β-gliadin and can result in symptomatic gluten-sensitive enteropathy. Celiac disease is a chronic, immune-mediated intestinal disorder, in which the body becomes intolerant to gliadin, which is a component of gluten. Individuals with celiac disease exhibit a lifelong
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