Human jejunal transglutaminase: demonstration of activity, enzyme kinetics and substrate specificity with special relation to gliadin and coeliac disease.

By use of a radiometric assay transglutaminase activity was demonstrated for the first time in human jejunal mucosa. The activity is similar to that in other tissues, with a pH optimum of 9.0, an absolute requirement for Ca2+ and an apparent Km for putrescine of 0.15 mmol/l. Assay of jejunal transglutaminase activity with a variety of dietary proteins as acceptors showed high activity with gliadin, comparable with that of the standard substrate, dimethylcasein. Deamidation of the gliadin markedly reduced its acceptor activity. Collagen, ovalbumin, elastin and zein exhibited very low acceptor activities. Increased transglutaminase activity was demonstrated in jejunal biopsies from four patients with untreated coeliac disease compared with 14 control subjects and eight patients with inflammatory bowel disease. Eight patients with coeliac disease in remission, with normal levels of brush border alpha-glucosidase, showed elevated transglutaminase activities compared with those of controls. It is postulated that intestinal transglutaminase activity may be important in gliadin binding to tissues and thus in the pathogenesis of coeliac disease.