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- W4244781907 abstract "Amyloid-β peptide, derived from the amyloid precursor protein, plays a crucial role in the pathogenesis of Alzheimer's disease. Processing of amyloid precursor protein by β-secretase generates C99, which is further cleaved by γ-secretase, yielding two major species of β-amyloid, β-amyloid40 and β-amyloid42, differing in length of the amino acid chain. β-amyloid is normally secreted; however are produced, remaining inside the cells. In the present study, we investigated the intracellular metabolism of AAP using a truncated γ-secretase-specific β-amyloid precursor, C99. We have selected two point mutations close to the β-amyloid42/40 ratio of β-amyloid secreted, and examined their effects on the formation of β-amyloidi. Analysis of SH-SY5Y cells stably expressing these constructs led to the unexpected result, that the β-amyloid42/40 ratios of β-amyloidI and β-amyloid secreted were differently influenced by the introduced point mutations." @default.
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- W4244781907 date "2001-03-28" @default.
- W4244781907 modified "2023-09-27" @default.
- W4244781907 title "Intracellular and Secreted Aβ <sub>42/40</sub> Ratios Are Differently Influenced by APP Mutations" @default.
- W4244781907 doi "https://doi.org/10.1002/0470846453.ch43" @default.
- W4244781907 hasPublicationYear "2001" @default.
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