Scientists have found a way to treat celiac disease
Last reviewed: 23.04.2024
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Employees of the University of Stanford 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 violation of the functionality of the small intestine. The disease is associated with a lack of enzymatic substances necessary for the breakdown of gluten.
Celiac disease is diagnosed in 1% of the inhabitants of our planet - however, statistics take into account only cases with an exactly established diagnosis. According to doctors, the vast majority of cases of celiac disease are mistaken for other diseases. Therefore, patients with this pathology, in fact, much more.
The main signs of the disease is diarrhea with impaired absorption of essential substances from food, as well as anemia that occurs as a result of intestinal damage. Symptoms occur when ingested with gluten, which is found in many cereals and other foods high in gluten. Celiac disease is considered an incurable disease, and the main treatment measures are the lifelong observance of certain dietary rules.
But research conducted by scientists gave many patients hope: celiac disease is cured.
It has long been found that part of the pathogenetic mechanism of the disease is the enzyme substance TG2 (transglutaminase2), which normalizes the production of connective tissue proteins. In celiac disease, one of the markers of pathology is the presence of antibodies to this substance.
The author of the development, Michael Yee, suspected that the disease was practically not treatable due to a lack of understanding of the functional processes associated with TG2. Scientists have begun to study this enzyme substance more thoroughly.
"In the human body, the enzyme is able to both turn on and off under the influence of individual chemical bonds. In the intestine of a healthy person, this enzyme is also present, but in an inactive state. The moment we found this, we asked ourselves: what factor can TG2 turn on and off? ", The researchers say.
The first experiment, conducted in 2012 by the doctor-biochemist Khosla, made it possible to learn how to "include" this enzyme. In the subsequent experiment, scientists managed to do the opposite.
TG2 is "turned on" during the disruption of the disulfide bond in intestinal proteins. The new experiment allowed to prove: the renewal of the broken bond again deactivates the activity of the enzyme. In the role of the "deactivator", another enzymatic substance - Erp57 - has emerged, which helps proteins to 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 of "neutralizing" in their body TG2. In this case, no side effects were observed. Now scientists only have to pick up a substance that could control a new "switch".
Full information about the research is published on the website of the scientific journal jbc.org
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