In the Sept. 27 issue of Science, researchers identify a fragment of gluten called gliadin as the celiac culprit. They showed that this fragment is resistant to digestion and is responsible for the intestine-damaging inflammatory response experienced by celiac patients. They also report the use of a dietary enzyme made by a bacterium that can break down the fragment into harmless bits, suggesting future treatment through dietary supplements.
"These findings are the first step to giving people with celiac disease real hope for a normal life," said Chaitan Khosla, PhD, professor of chemistry, chemical engineering and, by courtesy, of biochemistry. Lu Shan, a graduate student in Khosla's lab, was lead author on the paper. The team included other Stanford researchers as well as a group from the University of Oslo in Norway.
The lining of the small intestine is normally carpetlike, covered with small protrusions called villi. Celiac disease, however, results in a smooth, pipelike intestine. The reduced surface area keeps the body from absorbing nutrients. Often diagnosed in childhood, the disease can lead to the distended stomach and stunted growth typical of starvation.
"The only effective therapy for most people is a lifelong gluten-free diet, and that's fairly restrictive," explained co-author Gary M. Gray, professor of medicine, emeritus. The diet is essential over the long term both to restore normal intestinal function and to reduce the risk of developing osteoporosis, lymphoma or cancer of the small intestine, he added.