The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Gliadin is a good substrate of several transglutaminases: possible implication in the pathogenesis of coeliac disease.

BACKGROUND: Deamidation of distinct glutamines in HLA-DQ2 restricted gliadin epitopes, considered critical in the pathogenesis of coeliac disease (CD), can be mediated by tissue transglutaminase (tTG). To elucidate the possible role of other transglutaminases in CD we investigated whether different mammalian, microbial and vegetable transglutaminases can use gliadin as substrate. METHODS: Studies in which small amounts of transglutaminase have been measured have led to our modifying a microtitre plate assay. We used proteolytically digested gliadin as solid phase substrate and Europium-labelled streptavidine to quantify the biotinylated product covalently linked by the enzyme to the plate. RESULTS: The modified assay is ultrasensitive and quantitative, measuring guinea pig liver transglutaminase concentrations between 0.5 and 50 ng/well. The specific activities of the enzymes (counts/min/mg) against gliadin and N,N-dimethylcasein, respectively, are: tTG 9800/4900, Factor XIII 97330/55620, epidermal transglutaminase 47650/50770, streptoverticillium transglutaminase 4290/2200, phytophora cactorum transglutaminase 6910/4110. For the first time, we have detected transglutaminase activity in bean sprouts, spinach leaves and green peas, which are commonly used Vegetables. CONCLUSION: Gliadin is a good substrate for endogenous, microbial and plant transglutaminases. An interesting altemative is that gliadins are deamidated by microbial or food transglutaminases in the intestinal lumen. The assay described provides an ultrasensitive method for measuring small amounts of transglutaminase and is considered a helpful tool in further studies of the possible role of transglutaminases in the pathogenesis of CD.[1]


  1. Gliadin is a good substrate of several transglutaminases: possible implication in the pathogenesis of coeliac disease. Skovbjerg, H., Norén, O., Anthonsen, D., Moller, J., Sjöström, H. Scand. J. Gastroenterol. (2002) [Pubmed]
WikiGenes - Universities