Celiac disease is a condition that damages the lining of the small intestine and prohibits it from absorbing parts of foods. This damage is caused by eating gluten, commonly found in wheat, barley, rye, and sometimes oats. Symptoms may include diarrhea, short stature, discolored dental enamel, depression, premature degeneration of the nervous system, seizures, arthritis, nutritional deficiencies due to malabsorption, and abdominal distension. Long eyelashes, premature balding, and clubbing of the fingers are also commonly reported in this disease.

In celiac disease, there is an increase in the blood of antibodies to wheat. There is also a marked increase in antibodies called endomysial antibodies. The exact nature of the endomysial antigen has recently been identified as the tissue transglutaminase enzyme. Researchers in Norway believe that transglutaminase facilitates the physical linkage of the carboxamide group of an amino acid called glutamine in gluten to an epsilon-amino group of a lysine residue in transglutaminase in the intestinal tract. Because gluten has an abundance of the amino acid glutamine, it is especially vulnerable to this reaction with transglutaminase. This abnormally linked molecule is then perceived as a foreign antigen by the immune system and antibodies to transglutaminase begin to be produced, inhibiting the normal function of transglutaminase in repairing damaged intestinal mucosa. 

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