Supplementary Materials

Supplementary Materials for:

The amyloid-β oligomer Aβ*56 induces specific alterations in neuronal signaling that lead to tau phosphorylation and aggregation

Fatou Amar, Mathew A. Sherman, Travis Rush, Megan Larson, Gabriel Boyle, Liu Chang, Jürgen Götz, Alain Buisson, Sylvain E. Lesné*

*Corresponding author. Email: lesne002{at}umn.edu

This PDF file includes:

  • Fig. S1. Reverse coimmunoprecipitation of Aβ*56 with NMDAR subunits in Tg2576 and in human brain tissue.
  • Fig. S2. Age-dependent accumulation of Aβ oligomers in Tg2576 mice.
  • Fig. S3. Biochemical characterization of soluble Aβ species present in APP transgenic brain tissues.
  • Fig. S4. Molecular and morphological characterization of primary cortical neurons.
  • Fig. S5. The major pathways regulated by extrasynaptic NMDARs are not altered in 7-month-old Tg2576 mice.
  • Fig. S6. Relationship between CaMKIIα activity and Aβ*56 expression in brain tissue from young Tg2576 mice.
  • Fig. S7. The major pathways regulated by extrasynaptic NMDARs are not altered by endogenous Aβ oligomers in mouse cortical primary neurons after a 60-min exposure.
  • Fig. S8. Aβ*56-induced translocation of pCaMKIIα to postsynaptic sites in primary cortical neurons.
  • Fig. S9. CaMKIIα activation is not induced by low-n Aβ oligomers purified from APP transgenic mice.
  • Fig. S10. Epitope and dephosphorylation tau assays confirm the presence of hyperphosphorylated tau conformers.
  • Fig. S11. Aberrant phosphorylation of CaMKIIα and tau in young J20 mice expressing Aβ*56.
  • Fig. S12. Temporal expression profiles of CDK5 adaptor proteins and GSK3 in young wild-type and Tg2576 mice.
  • Fig. S13. Brain-derived Aβ dimers and trimers do not induce tau phosphorylation at Ser202.
  • Fig. S14. Dose-dependent uncoupling of PSD95 and NMDAR GluN1 subunit induced by tatNR2B9c in primary neurons.

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Citation: F. Amar, M. A. Sherman, T. Rush, M. Larson, G. Boyle, L. Chang, J. Götz, A. Buisson, S. E. Lesné, The amyloid-β oligomer Aβ*56 induces specific alterations in neuronal signaling that lead to tau phosphorylation and aggregation. Sci. Signal. 10, eaal2021 (2017).

© 2017 American Association for the Advancement of Science