Amyloid Deposits Not Always Toxic to Cells

How do protein aggregates damage cells? Scientists believe they are toxic themselves, or that they sequester other proteins that have an essential cellular function. In the November Science, researchers led by Frederic Rousseau and Joost Schymkowitz at VIB Switch Laboratory, Leuven, Belgium, add evidence for the latter. They designed a synthetic peptide consisting of an amyloidogenic fragment of vascular endothelial growth factor receptor 2 (VEGFR2). When added to endothelial cell cultures, which depend on VEGF signaling, the fragment triggered clumping of the receptor, and the cells died. When added to cells which express transgenic VEGFR2 but which do not normally make this receptor, the peptide seeded VEGFR2 aggregation, but the cells appeared normal. The findings suggest that at least in this case, toxicity occurs only through depriving cells of an essential protein.
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