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CROSS LINKING OF GLIADIN BY TISSUE TRANSGLUTAMINASE IS A CRITICAL PART OF THE PATHOGENESIS OF COELIAC DISASE
It is know that short peptides from α-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.
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Tissue transglutaminase expression in the wall of the oesophagus.
HOW JEJUNAL INFLAMMATION INDUCES ANOREXIA: ROLE OF CCK AND 5-HT
Many inflammatory illnesses are associated with anorexia but the mechanisms involved are uncertain. The authors had previously found increased cholecystokinin (CCK) levels in patients with giardiasis, an illness often associated with anorexia and nausea. They undertook a mechanistic study using Trichinella spiralis infected mice and found (see figure) that the number of CCK and …
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