Ever wondered how Parkinson’s disease spreads within the brain? A key culprit is the buildup and movement of abnormal alpha-synuclein (α-syn) protein clumps, called fibrils. New research has uncovered a fascinating piece of this puzzle, identifying a gene called FAM171A2 that plays a significant role in this process.

Here’s the breakdown:

• FAM171A2 and Parkinson’s Risk: This gene has been linked to an increased risk of Parkinson’s disease. It appears to act as a sort of “doorway” for α-syn fibrils to enter brain cells.
• How it Works: The FAM171A2 protein on the surface of brain cells interacts with the tail end of α-syn fibrils. This interaction is incredibly specific to the fibril form of α-syn, over a thousand times more so than other forms of the protein. This “sticky” interaction allows the fibrils to be absorbed into the neuron.
• Consequences of Increased FAM171A2: When there’s too much FAM171A2, more α-syn fibrils get inside neurons, which can accelerate the spread of the disease and increase its damaging effects.
• Potential Protective Effects: Excitingly, reducing FAM171A2 levels in neurons appears to protect them from the harmful effects of α-syn fibrils. This suggests that targeting FAM171A2 could be a promising therapeutic strategy.
• A Promising Drug Candidate: Researchers have identified a drug called bemcentinib that can block the interaction between FAM171A2 and α-syn fibrils. This blockage has been shown to be effective in laboratory settings, including cell cultures and even in mice.

This research offers a new understanding of how Parkinson’s disease progresses and highlights FAM171A2 as a potential target for future therapies. The possibility of using bemcentinib to interrupt the harmful interaction between FAM171A2 and α-syn fibrils opens up exciting new avenues for developing treatments to slow or even halt the progression of this debilitating disease.