Celiac Disease and Grindstone Breads
Celiac Disease (CD) is an inflammatory illness that leads to destruction of the microscopic fingerlike projections of the small intestine called villi. The disease is triggered by ingestion of the gluten proteins contained in Wheat, Spelt, Barley, and Rye, and symptoms range from minor complaints to severe nutrient malabsorption Wheat, Spelt, Rye, and Barley are related cereals of the family Triticeae and are toxic to patients with CD. Oats can be classified as a cousin of Triticeae and thus a more distant family member. Their storage proteins are collectively called gluten proteins by celiac patients and their physicians, although, strictly speaking, gluten is derived only from the endosperm of wheat grain. Prolamins, which comprise the alcohol soluble fraction of the storage proteins of cereals, are termed gliadin in wheat and avenin in oats. They have been named according to their content of the amino acids proline and glutamine, which is much higher in gliadin than in avenin.
The proportion of prolamins in cereals may reflect their degree of toxicity to celiacs. In wheat, rye, and barley, prolamins constitute 40 to 50 percent, 30 to 50 percent, and 35 to 45 percent respectively of total proteins, but in oats, they constitute only 10 to 15 percent. Sixty grams of oats is estimated to contain 1.2 g of avenin. The injurious constituent of wheat for patients with celiac disease is located in gliadin. As mentioned before, recent studies at Stanford University have identified a sequence of 33 amino acids in gliadin as being responsible for the exceptional toxic potency against the small intestinal mucosa that characterizes CD. This same sequence was found in other grain prolamins like hordeins (from barley), and secalins (from rye), all of which are toxic cereals in the Celiac diet. Proteins in nontoxic food grains, such as avenins (in oats), rice, and maize, do not contain a homologous sequences to the 33 amino acids sequence found in gliadin.
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