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Scientists have found a cure for celiac disease
Last reviewed: 02.07.2025
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Stanford University researchers have found a way to “turn off” celiac disease, a chronic autoimmune disease that affects the digestive system.
Celiac disease is a genetically determined pathology that occurs with a disruption of the functionality of the small intestine. The disease is associated with a lack of enzymes necessary for the breakdown of gluten.
Celiac disease is diagnosed in 1% of the population of our planet, but statistics only take into account cases with a precisely established diagnosis. According to doctors, the vast majority of cases of celiac disease are mistaken for other diseases. Therefore, there are, in fact, many more patients with this pathology.
The main symptoms of the disease are diarrhea with impaired absorption of essential substances from food, as well as anemia, which occurs due to intestinal damage. Symptoms appear when gluten is consumed with food, which is found in many cereals and other products with a high gluten content. Celiac disease is considered an incurable disease, and the main treatment measures consist of lifelong adherence to certain dietary rules.
But research conducted by scientists has given many patients hope: celiac disease is curable.
It has long been discovered that the enzyme substance TG2 (transglutaminase2), which normalizes the production of connective tissue proteins, becomes part of the pathogenetic mechanism of the disease. In celiac disease, one of the markers of the pathology is the presence of antibodies to this substance.
The author of the development, Michael Yee, suspected that the disease was practically untreatable due to insufficient understanding of the functional processes associated with TG2. Scientists began a more thorough study of this enzymatic substance.
"In the human body, the enzyme is capable of both switching on and off under the influence of individual chemical bonds. In the intestines of a healthy person, this enzyme is also present, but in an inactive state. At the moment when we discovered this, we asked ourselves: what factor can switch TG2 on and off?", the researchers say.
The first experiment, conducted in 2012 by biochemist Dr. Khosla, revealed how to “switch on” this enzyme. In a subsequent experiment, scientists were able to do the opposite.
TG2 is "switched on" when a disulfide bond in intestinal proteins is broken. A new experiment has shown that restoring the broken bond deactivates the enzyme's activity again. The "deactivator" was another enzyme substance, Erp57, which helps proteins become functional within the cellular structure.
The second question that scientists faced was: how does the "deactivator" behave in the body of a healthy person? The first experiments with rodents demonstrated a positive effect from "neutralizing" TG2 in their body. No side effects were observed. Now scientists only need to find a substance that could control the new "switch".
Full details of the study are published on the website of the scientific journal jbc.org
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