Stanford University Researchers Find A Chemical "

Details reported by the Journal of Biological Chemistry.

Celiac disease, or celiac disease, is a common hereditary disease that affects about 1% of the world's population.

The paradox is that most patients live without a diagnosis, continuing to attribute symptoms to other diseases..

Symptoms of celiac disease - diarrhea, malabsorption of nutrients, anemia - are caused by damage to the small intestine from gluten intake. Patients are intolerant to wheat, rye and other cereals, as well as drugs containing gluten.

There are currently no effective drugs for celiac disease.

Once diagnosed, patients are advised to take a life-long gluten-free diet..

However, new research is moving us closer to curing celiac disease..

Role of TG2 in disease development.

It is known that one of the links in the pathogenesis of celiac disease is the enzyme transglutaminase 2 (TG2), which regulates the synthesis of connective tissue proteins. Anti-TG2 antibodies are considered a diagnostic feature of the disease.

Project leader Michael Yi has suggested that the reason for the " Stanford scientists decided to study this enzyme more thoroughly..

Specifically, they wanted to understand how TG2 behaves in healthy people..

“This enzyme turns on and off in the presence of certain chemical bonds. Although there may be a lot of TG2 in a healthy gut, it is inactive. When we figured it out, the question became different: what turns the enzyme on and off? "

ERp57 - Celiac Disease Medication?

In a 2012 study, Stanford biochemists led by Professor Khosla discovered how to activate TG2. Now they've learned to do the opposite..

Transglutaminase 2 is activated by the destruction of a disulfide chemical bond in intestinal proteins. A new study shows that restoring this bond again " Another enzyme, ERp57, claimed the role of a chemical " It usually helps proteins "

But cell culture experiments conducted by Prof. Hosla and the team did confirm the possibility of TG2 'shutdown', but only outside the cell..

“The question is, how does ERp57 work in healthy people?. Nobody understands how (Erp57) goes outside the cell. The general consensus is that it is released to the outside in small amounts.. Its purpose is to interact with proteins from the outside, ”the authors explain..

Previous experiments in mice demonstrate that lack of TG2 does not cause time in mice. Blocking this enzyme in humans should not cause adverse reactions..

Now we have to find drugs that can control the new " Scientists are already actively looking for candidates among approved drugs for other diseases.

medbe. ru.