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Fig. 3 | Acta Neuropathologica Communications

Fig. 3

From: Intracellular amyloid β oligomers impair organelle transport and induce dendritic spine loss in primary neurons

Fig. 3

Effects of extracellular Aβ on spines. Synthetic wild-type (WT) or Osaka-mutant (OSK) Aβ42 peptides were added into culture media of GFP-expressing neurons at various concentrations. a Before adding the peptides, Aβ oligomer formation in the peptide solutions were examined by Western blot with 6E10 antibody. Aβ WT peptide showed mainly monomers and faintly dimers, whereas Aβ OSK peptide exhibited abundant monomers as well as dimers and trimers and faintly tetramers and 12-mers. b, c After a 2-day culture in the presence of Aβ peptides, spine densities and types were measured. Aβ WT peptide (b) increased total and mushroom-type spines at physiological, low concentrations from 100 pM to 400 pM. In contrast, Aβ OSK peptide (c) did not affect spine morphology at those concentrations. However, both Aβ WT and Aβ OSK peptides significantly decreased total and mushroom-type spines at higher concentrations: at 25 nM of Aβ WT peptide and over 1 nM of Aβ OSK peptide

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