basis of electrophoretic mobility and isoelectric focusing. Gliadin peptides cross the intestinal barrier by active transport. Metabolism Gliadins are known for their role, along with glutenin, in 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 celiac disease (also known as gluten-sensitive enteropathy) 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: Triticeae glutens Immunochemistry of gluten Deamidated 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 Celiac disease (or coeliac 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 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 problem with this disease is that it often goes unrecognized for many years, in which case it can cause serious damage to several organs, and most cases currently remain unrecognized, undiagnosed and untreated. This occurs as a result of CD4+T cell recognition of deaminated gliadin polypeptide chains within the intestinal epithelium. CD8+ T cells then enter the epithelium and express NK receptors specific for gliadin and transglutaminase causing intraepithelial T cells to kill enterocytes by mediating apoptosis. Celiac disease with "non-classic symptoms" is the most common clinical type and occurs in older children (over 2 years old), adolescents and adults. It is characterized by milder or even absent gastrointestinal symptoms and a wide spectrum of non-intestinal manifestations