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Fig. 1 | Alzheimer's Research & Therapy

Fig. 1

From: The effects of different familial Alzheimer’s disease mutations on APP processing in vivo

Fig. 1

Effects of the APPswe, APParc and PSEN1 H163Y mutations on APP processing in vitro. a APPswe mutation is located in the extracellular domain of APP, at the BACE1 cleavage site, causing a 5–10-fold increase in the production of Aβ40 and Aβ42 [34]. Presenilin 1 is a subunit of the γ-secretase and most PSEN1 mutations modulate the γ-secretase cleavage site-preference in a disease-promoting manner by inhibiting cleavages at Gly37, Gly38 and Val39 in the Aβ sequence, without affecting the production of Aβ42 and Aβ40 significantly [35]. Finally, the arctic APP mutation, located within the Aβ sequence, leads to the production of Aβ with higher propensity for protofibril formation than wild-type Aβ [6]. b More detailed overview of the position of the APPswe and APParc mutations within APP. Letters, amino acids; numbers, position of the amino acids within the APP sequence. c Schematic illustration of the transmembrane protein presenilin 1, a subunit of γ-secretase. The PSEN1 H163Y mutation is located in the third transmembrane domain of the protein. APP amyloid precursor protein

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