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| The first 150 words of the full text of this article appear below. |
It is know that short peptides from 
-gliaden stimulate T cells in coeliac disease. The binding of these peptides to human leukocyte antigens (DQ2 and DQ8) is greatly enhanced when the peptides are deamidated by tissue transglutaminase. It has been hypothesised that the deamidation of a few specific gliadin peptides is responsible for the chronic inflammation of coeliac disease. However, this hypothesis has not been tested directly. Data are presented that tissue transglutaminase can deamidate a wide range of gliadin peptides. Furthermore, deamidation causes the binding and long term immobilisation of gliadin peptides to collagen, which contributes the chronicity of inflammation. This binding is also associated with increased titres of anticollagen antibodies, which may explain the high incidence of autoimmune disease in coeliac patients.
See p 478
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Many inflammatory illnesses are associated with anorexia but the mechanisms involved are uncertain. The
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