Celiac Disease Essay

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Celiac Disease
Dascha C. Weir, MD
Ciaran Kelly, MD

Celiac disease (CD) is an immune-mediated enteropathy secondary to permanent sensitivity to wheat gluten and related proteins in rye and barley. It results in characteristic histologic changes consisting of inflammation, crypt hyperplasia, and villous atrophy of the small intestine in genetically susceptible individuals. Significant variability in the clinical presentation of
CD in the pediatric population complicates recognition of the disease in many patients. Treatment for CD consists of a lifelong strict gluten-free diet (GFD). Adherence to this diet is associated with resolution of most related signs and symptoms and a decreased risk of related complications. With an
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Clearly, enteric exposure to specific proteins in wheat, rye, and barley are essential to disease activation in a genetically susceptible person.
Wheat, rye, and barley have common ancestry and are all derived from the Triticeae tribe of the grass family. Broadly termed “gluten,” the specific

proline- and glutamine-rich proteins that activate disease are gliadins in wheat, secalins in rye, and hordeins in barley. Gluten, the second major protein fraction of wheat gluten, is likely involved to a lesser degree. Multiple toxic antigenic epitopes have been described (Figure 1).
These peptides activate immune cells causing a chain of events that result in tissue damage. The mechanisms for this activation are incompletely understood and are likely a combination of adaptive and innate immunity. Partially because of their high proline content, these large cereal peptides are resistant to digestion by intestinal proteases and pass through the epithelium and into the lamina propria in an intact state. The mechanisms of this passage through the intestinal barrier are not well understood. Tissue transglutaminase deamidates these peptides in the lamina propria causing them to become negatively charged as the glutamine residues are converted to glutamic acid. Deamidated peptides bind with far greater affinity to specific positively charged residues on the peptide-binding groove of HLA-DQ2 or
HLA-DQ8

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