Discussion

Through current research, the pathology of Celiac disease has been laid out as a biochemical and immunological mechanism.   The protein gluten is broken down by digestive enzymes such as trypsin or pepsin, and is sent to the intestinal tract for further processing.  However, once its fragments enter the tract they are not easily digested nor are they easily removed from the system, possibly because of insolubility.  The epitopes build up a concentration, which leads to the activation of the tissue transglutaminase.   The transglutaminase reacts strongly with the identified 33-mer peptide of an a-gliadin, to generate a regiospecific deamidated product.  Until the current research conducted at Stanford this step of the mechanism was uncertain.  After the deamidation, the product protein then reacts with HLA DQ2 to form a complex that changes the conformation of the antigen (gliadin).  This change in conformation initiates the inflammatory response that destroys the intestinal tract in Celiac patients.    The understanding of  this mechanism by which Celiac disease manifests has lead to new ideas regarding therapeutic treatments.  One potential treatment is an oral vaccine using immunogenic peptide epitopes that are resistant to pepsin, trypsin, and chymotrypsin.   The potential for understanding even more about the mechanism behind this disease exists and researchers continue to build on the advances already made.   Moreover, with the potential to understand more comes the potential for more therapeutic techniques and possibly even a cure for Celiac disease.