Amyloid-β42/40 ratio drives tau pathology in 3D human neural cell culture models of Alzheimer's disease

Nat Commun. 2020 Mar 13;11(1):1377. doi: 10.1038/s41467-020-15120-3.

Abstract

The relationship between amyloid-β (Aβ) species and tau pathology in Alzheimer's disease (AD) is not fully understood. Here, we provide direct evidence that Aβ42/40 ratio, not total Aβ level, plays a critical role in inducing neurofibrillary tangles (NTFs) in human neurons. Using 3D-differentiated clonal human neural progenitor cells (hNPCs) expressing varying levels of amyloid β precursor protein (APP) and presenilin 1 (PS1) with AD mutations, we show that pathogenic tau accumulation and aggregation are tightly correlated with Aβ42/40 ratio. Roles of Aβ42/40 ratio on tau pathology are also confirmed with APP transmembrane domain (TMD) mutant hNPCs, which display differential Aβ42/40 ratios without mutant PS1. Moreover, naïve hNPCs co-cultured with APP TMD I45F (high Aβ42/40) cells, not with I47F cells (low Aβ42/40), develop robust tau pathology in a 3D non-cell autonomous cell culture system. These results emphasize the importance of reducing the Aβ42/40 ratio in AD therapy.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alzheimer Disease / diagnostic imaging
  • Alzheimer Disease / genetics
  • Alzheimer Disease / metabolism*
  • Alzheimer Disease / pathology*
  • Amyloid beta-Peptides / genetics
  • Amyloid beta-Peptides / metabolism*
  • Cell Culture Techniques / methods*
  • Cells, Cultured
  • Coculture Techniques
  • Humans
  • Mutation
  • Neural Stem Cells / metabolism
  • Neurons / metabolism*
  • Neurons / pathology*
  • Peptide Fragments / genetics
  • Peptide Fragments / metabolism*
  • Presenilin-1 / genetics
  • Presenilin-1 / metabolism

Substances

  • Amyloid beta-Peptides
  • Peptide Fragments
  • Presenilin-1
  • amyloid beta-protein (40-42)