Many neurodegenerative conditions are characterized by the aggregation of altered proteins, such amyloid-β, α-synuclein, tau, and others. Once altered they can form solid deposits with a halo of surrounding biochemistry that is toxic and disruptive to the normal function of cells in the brain. Why do these protein aggregates only become significant in later life? There is some pace at which they are created, and some pace at which they are cleared by various mechanisms. For example, amyloid-β is an antimicrobial peptide, a component of the innate immune system. More will be created in the brains of people suffering persistent viral infections, which may explain the much-debated link between herpesviruses and risk of Alzheimer’s disease.
On the clearance side of the house, the immune cells of the brain are in part responsible for cleaning up protein aggregates. As the environment becomes more inflammatory, and other issues in aging impair immune function more generally, these cells falter in the task of removing aggregates. Of late, researchers have also directed their attention towards the physical clearance of aggregates from the brain via drainage of cerebrospinal fluid. The hypothesis on which Leucadia Therapeutics was
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