Scientists have discovered a new protein that may come in handy to treat celiac disease effectively. Celiac disease is an auto-immune reaction faced by people who have gluten allergy or intolerance. In this condition, whenever a person who is gluten intolerant consumed anything with gluten, a protein found in wheat, barley and rye, he/she has allergic reactions.
The study conducted by researchers at the Stanford University was published in the Journal of Biological Chemistry. According to the researchers this new enzyme could prove to eb a path-breaking intervention in treatment of the disease.
The disorder is said to affects by some estimates nearly 1 in 100 people. The symptoms of the disease involves, belching, diarrhoea, fat in stool, indigestion, nausea, vomiting, or flatulence. While the gluten intolerance is triggered by a protein found in wheat and related plants, the digestive symptoms that patients suffer aren't for gluten alone. The study suggested that gluten activates overactive immune response when it's modified by the enzyme transglutaminase 2, or TG2, in the small intestine. The researchers have identified the enzyme that turns off TG2, potentially paving the way for new treatments for celiac disease.
Currently, best approach to treat celiac disease is to stick to a gluten-free diet. This study may make way to therapies to treat people with celiac disease. Our relatively poor understanding of TG2 could be the reason behind the lack of therapies, according to the researchers.
The study said, "TG2 is oxidatively inactivated by the protein disulfide isomerase ERp57, providing the first example of a defined and reversible protein-controlled redox switch and pointing to new strategies to inhibit undesirable TG2 activity in pathological states"/
The interaction of gluten and its impact on immune response has been well studied. However the mysteries surrounding TG2 protein and especially its behavior in people without celiac disease needs to be studied too.
Chaitan Khosla who was closely associated to the study right from the start has conducted many studies in the past that reflected upon the behavior of TG2. TG2 can be active or inactive, depending on the forming or breaking of a specific chemical bond, called a disulfide bond, between two amino acids in the enzyme. According to Khosla, even though there's a lot of TG2 protein in the small intestine, it's all inactive. Therefore despite its abundance, the question came down to what turns the protein on and then what turns it off.
The study was performed on cell cultures. It was found that there is an enzyme that re-forms this bond, inactivating TG2. This enzyme, ERp57, is mainly known for helping fold proteins inside the cell. When it turns off TG2, it does so outside of cells. How (Erp57) gets outside the cell, is one of the most peculiar aspect of ERp57 which needs to be studies in detail said the researchers. Understanding this on and off chemistry could be the key to celiac treatment .
A gluten-free diet could be a tedious diet to follow considering India's fixation with wheat. However it is not impossible. Here is a list of 7 gluten free grains you must know of.
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