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- W2005452561 abstract "In some pedigrees of familial Alzheimer's disease (FAD), three mutations of β amyloid precursor protein (APP) have been found at the Val717residue (to Ile, Phe, or Gly) and these mutations increase the secretion of Aβ42(43). To study the specificity of the effects of these mutations on APP processing, we transiently expressed APP genes with mutations of Val717to Lys, Ser, Glu, or Cys in COS cells. The three familial AD-linked mutations increased the levels or ratios of Aβ42(43), whereas the secretion of Aβ40 was decreased. Other mutations irrelevant to FAD except Val717to Lys had little effect on the ratio of Aβ42(43). Substitution to Lys decreased the secretion of Aβ42(43); substitution to Glu or Gly decreased the amount of intracellular C-terminal fragment produced by α-secretase, whereas it was increased by mutations to Phe, Cys, or Lys. However, the levels of secretion of soluble APP were constant, but a substitution to Glu reduced it. These results suggest a specific role of the Val717residue in APP processing and, especially, in γ-cleavage." @default.
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- W2005452561 date "1996-10-01" @default.
- W2005452561 modified "2023-10-17" @default.
- W2005452561 title "Familial Alzheimer's Disease-Linked Mutations at Val717of Amyloid Precursor Protein Are Specific for the Increased Secretion of Aβ42(43)" @default.
- W2005452561 doi "https://doi.org/10.1006/bbrc.1996.1577" @default.
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