WEDNESDAY, Sept. 19 (HealthDay News) -- The gluten in wheat flour can be detoxified by transamidation with a food-grade enzyme and an appropriate amine donor that blocks T cell-mediated gliadin activity, suggesting that such interventions may help prevent cereal toxicity in patients with celiac disease, according to the results of a study published in the September issue of Gastroenterology.
Mauro Rossi, Ph.D., of the Institute of Food Sciences in Avellino, Italy, and colleagues treated wheat flour with microbial transglutaminase and lysine methyl ester and then extracted, digested, and deamidated the gliadin. Using biopsy specimens from 12 adult patients, they generated gliadin-specific intestinal T-cell lines and challenged them in vitro with different antigen preparations.
The researchers found that tissue transglutaminase-mediated transamidation with lysine or lysine methyl ester of p56-68 or gliadin in alkaline conditions inhibited the interferon γ expression in gliadin-specific intestinal T-cell lines.
"Considering the problems associated with a life-long gluten-free diet, the availability of 'non-toxic' bread and other cereal products would already mean an enormous improvement of life quality for celiac disease patients," state the authors of an accompanying editorial. "Nonetheless, the social problems at public events (dinner parties, receptions or invitations) would remain. Therefore, apart from the availability of cereal products that have been modified pre-ingestion, a drug that can neutralize unaltered gluten upon ingestion remains an important goal of future translational research in celiac disease."
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