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
Bread mainly found in hulls in the form of insoluble bound ferulic acid, where it is relevant to wheat resistance to fungal diseases. Rye bread contains phenolic acids and ferulic acid dehydrodimers. Three natural phenolic glucosides, secoisolariciresinol diglucoside, p-coumaric acid glucoside and ferulic acid glucoside, can be found in commercial breads containing flaxseed. Glutenin and gliadin are functional proteins found in wheat bread that contribute to the structure of bread. Glutenin forms interconnected gluten networks within bread through interchain disulfide bonds. Gliadin binds weakly to the gluten network established by glutenin via intrachain disulfide bonds. Structurally, bread can be defined as