Dr Hilal Lashuel’s group reports a ground-breaking discovery
In a study appeared in the Proceedings of the National Academy of Sciences (PNAS), Dr Hilal Lashuel, who is SASTA Secretary, reports a ground-breaking discovery that opens doors for the development of new drug therapies for Parkinson’s Disease. The team “exonerated a process thought to play a role in causing Parkinson’s disease; rather than triggering toxic aggregates in neurons, it turns out that it actually slows down the disease, pharmas have now new tracks to explore”.
Press Release
Clues left at the scene of the crime don’t always point to the guilty party, as EPFL researchers investigating Parkinson’s disease have discovered. It is generally accepted that the disease is aggravated when a specific protein is transformed by an enzyme. The EPFL neuroscientists were able to show that, on the contrary, this transformation tends to protect against the progression of the disease. This surprising conclusion could radically change therapeutic approaches that are currently being developed by pharmaceutical companies. The research is to appear in an article in the Proceedings of the National Academy of Sciences (PNAS).
Parkinson’s disease is characterized by the accumulation of a protein known as alpha-synuclein in the brain. If too much of it is produced or if it’s not eliminated properly, it then aggregates into small clumps inside the neurons, eventually killing them. Several years ago scientists discovered that these aggregated proteins in the brain had undergone a transformation known as “phosphorylation” — a process in which an enzyme adds an extra chemical element to a protein, thus modifying its properties.
The investigators’ conclusion that the enzyme’s activity could be responsible for the disease seems eminently reasonable. If phosphorylation and protein aggregation go hand in hand, then it makes sense that one should cause the other. This is the assumption that researchers and pharmaceutical companies made as they tried to reduce the phosphorylation by deactivating an enzyme involved in the process. But they have been following a false lead, as the EPFL team was able to show.
The scientists even discovered that the phosphorylation of the protein has positive effects. On the one hand, it considerably reduces the toxic aggregation of the protein, and on the other, it helps the cell eliminate the protein. “The two phenomena are undoubtedly related, and together could play a role in the reduction of alpha-synuclein toxicity, but we don’t yet understand the impact of both processes at each stage of the disease,” explains neurobiologist Abid Oueslati, first author on the study. Continue
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