The self-seeding mechanism characteristic of the prion-protein has also been attributed to other neurodegenerative-disease-associated proteins including amyloid beta (Aβ), tau, and α-synuclein. An interesting facet of these prion-like proteins is their ability to horizontally "spread" and recruit their soluble counterparts in adjacent neurons. However, recent findings suggest a heterotoxic potential in these "seeds" whereby one neurodegeneration-associated protein can interact with another sequentially unrelated prion-like protein and influence its aggregation and drive cross-toxic outcomes and neurodegenerative co-morbidity. Yet, direct experimental evidence for amyloid cross-talk at the vertebrate level remains indirect, lacks resolution, or introduces confounding variables. Here, we discuss the need for a novel approach to resolve amyloid cross-toxicity at the neurohistochemical and organismal levels.
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http://dx.doi.org/10.1021/acschemneuro.9b00692 | DOI Listing |
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