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
Prolamin disease in genetically predisposed individuals. Prolamin Prolamins are a group of plant storage proteins having a high proline content and found on plant materials mainly like in the seeds of cereal grains: wheat (gliadin), barley (hordein), rye (secalin), corn (zein), sorghum (kafirin) and as a minor protein, avenin in oats. They are characterised by a high glutamine and proline content and are generally soluble only in strong alcohol [70-80%] solutions, light acids, and alkaline solution. They do not coagulate in heat. They hydrolyse into prolin and ammonia. Some prolamins, notably gliadin, and similar proteins found in the tribe Triticeae (see