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- W2074438246 abstract "β-amyloid protein (Aβ) formation was reconstituted in permeabilized neuroblastoma cells expressing human Alzheimer β-amyloid precursor protein (βAPP) harboring the Swedish double mutation associated with familial early-onset Alzheimer disease. Permeabilized cells were prepared following metabolic labeling and incubation at 20°C, a temperature that allows βAPP to accumulate in the trans-Golgi network (TGN) without concomitant Aβ formation. Subsequent incubation at 37°C led to the generation of Aβ. Aβ production in the TGN persisted even under conditions in which formation of nascent post-TGN vesicles was inhibited by addition of guanosine 5′- O -(3-thiotriphosphate), a nonhydrolyzable GTP analogue, or by omission of cytosol. These and other results indicate that vesicle budding and trafficking may not be required for proteolytic metabolism of βAPP to Aβ, a process that includes “γ-secretase” cleavage within the βAPP transmembrane domain." @default.
- W2074438246 created "2016-06-24" @default.
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- W2074438246 date "1997-04-15" @default.
- W2074438246 modified "2023-10-03" @default.
- W2074438246 title "Generation of Alzheimer β-amyloid protein in the trans-Golgi network in the apparent absence of vesicle formation" @default.
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- W2074438246 doi "https://doi.org/10.1073/pnas.94.8.3748" @default.
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