Abstract

Celiac Sprue is a genetic disorder of the autoimmune system that is widely prevalent among individuals of European decent.  Nearly 1 in 300 Americans alone are affected.  Celiac causes an inflammatory response throughout the gastrointestinal tract that manifests with the following symptoms: fatigue, diarrhea, weight loss due to malabsorption of nutrients and vitamins, anemia and neurological anomalies.  The past ten years has seen the most rapid accumulation of knowledge regarding the pathogenesis and biochemical pathways of this disease, with much of the research focusing on the dietary protein gluten.    Most of the  current research links gluten through its epitopes, their interactions with T 1 helper cells, and the histocompatibility leukocyte antigens (DQ2) to the symptoms of the disease.  The primary mechanism by which these components interact has been elucidated, which yields several new strategies for combating the disease, aside from the traditional modes of avoidance of gluten containing foods.   The most recent research has focused on the degraded portion of gluten called gliadin, and more importantly the primary amino acid glutamine that comprises more than half of the molecular weight of the protein.  Below is a 3-D replication of the structure of glutamine.  The red parts of the molecule represent oxygen, the blue represent nitrogen, the black represent carbon, while the white represent hydrogen.  On the primary or first carbon atom there is a double bond between it and the oxygen.