Alzheimer’s protease curates neuron surfaces
The brains of people with Alzheimer’s disease contain many protein aggregates outside of cells, known as plaques. These are mainly made of the peptide amyloid-beta, which is released from the plasma membrane when the protease BACE1 cleaves its membrane-anchored precursor protein. Because amyloid-beta cannot be produced without BACE1, numerous BACE1 inhibitors have been tested or are in clinical trials as Alzheimer’s therapy.
In a recent article in Molecular & Cellular Proteomics, Julia Herber and colleagues at the German Center for Neurodegenerative Diseases described how they used a targeted surface glycoproteomics method to observe the effects of BACE1 inhibition. By labeling glycosylated membrane proteins, the researchers showed that BACE1 inhibition increases the abundance of unprocessed amyloid precursor protein but also increases other BACE1 substrates and even nonsubstrate proteins. This suggests that the inhibitor may exert unanticipated side effects by remodeling neuronal surface proteomes.
Linking cancer’s sweet tooth and distaste for fiber
Cancer cells are strange. For energy, they rely on aerobic glycolysis, a relatively inefficient way of getting energy out of glucose, instead of shuttling glycolysis products into the mitochondria to finish breaking them down. Besides this widespread preference of most cancers, known
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