Charcot-Marie-Tooth disease (CMT) is a changing neurological disorder involving more than 90 genes. An anomaly in just one of these is enough for the disease to manifest itself. Yet, despite the amount of abnormalities involved, the symptoms are always the same.

This makes understanding the biological mechanisms involved even more difficult. However, a study led by Professor Xiang-Lei Yang may have shed a new light on the whole. The study in question analyzes what is in common between the different genetic mutations. In particular, it focuses on enzymes known as aminoacyl-tRNA-synthetase. From what has emerged, they are the largest family of proteins related to CMT.

According to the researchers, enzymes would spread throughout the body, attacking amino acids and preventing them from producing new proteins. A blow to the body, which would block the production of blood, hormones, bones. To test the theory in question, the scientists took samples from a group of patients. In this way they could observe the action of enzymes in their natural environment. Later, they added healthy enzymes to mutated ones. After doing so, they have recovered their functionality.

However, this does not fully explain the involvement of the mutated enzymes in the disease. The researchers then shifted the focus to the form of enzymes, rather than their functionality. Mutated enzymes have a different shape than healthy ones.

They are much wider, with so much exposed surface. This could expose them to unwanted interactions with neighboring proteins, causing the symptoms of the disease. Now all that remains is to examine the different forms of enzymes and deepen the research.

Source: scripps.edu