Gluten immunochemistry motif", which is found in wheat and other "Triticeae" genera.(see also: ). Alpha-2 secalin, the glutinous protein in rye, is composed of two amino-terminal overlapping T-cell sites at positions (8-19) and (13-23). Although T-cell responses to many prolamins can be found in coeliac disease, one particular gliadin, α2-gliadin appears to be the focus of T-cells. These responses were dependent on prior treatment with tissue transglutaminase. Α2-gliadin differs from the other α-gliadins, specifically because it contains an insert of 14 amino acids. This particular insertion creates 6 T-cell sites where, in the most similar gliadins, there are 2 or less sites.
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