Figure 1 | Translational Psychiatry

Figure 1

From: Early accumulation of intracellular fibrillar oligomers and late congophilic amyloid angiopathy in mice expressing the Osaka intra-Aβ APP mutation

Figure 1

Intra-amyloid β (Aβ) mutations decrease α-cleavage in vivo. Transgene expression and Aβ peptide precursor (APP) processing were compared in three mouse models of Alzhemier’s disease (AD). (a) Western blot analysis of cortical SDS extracts from 3-month-old E22ΔAβ mice in comparison with age-matched Tg2576 and arcAβ mice. Full-length APP and APP C-terminal fragments (C99 and C83) were detected with a C-terminal-specific APP antibody and values normalized to β-actin. Quantification reveals significant reductions in α-stub (C83) levels in both transgenic mouse lines bearing the intra-Aβ mutation. This results in an increased C99/C83 ratio in the E22ΔAβ and arcAβ mice as compared with the Tg2576 mice. *P<0.05 E22ΔAβ and arcAβ vs Tg2576 (Mann–Whitney U-test). n=4 per group. (b) MSD analysis of sAPPα and sAPPβ levels in cortical samples extracted with Tris buffer containing 2% SDS. In accordance with the results of the APP CTF analysis, sAPPβ levels were not significantly different among the three APP transgenic mouse lines, whereas sAPPα was reduced almost threefold in the E22ΔAβ and arcAβ mice as compared with the Tg2576 mice. *P=0.001 E22ΔAβ and arcAβ vs Tg2576 (Mann–Whitney U-test). n=6–8 per group.

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