Dystrophic neurites infiltrate extracellular neurofibrillary tangles in Alzheimer disease

Jennifer Vande Weghe, Patrick Cras, Mitsuru Kawai, Sandra L. Siedlak, Massimo Tabaton, Barry Greenberg, George Perry

Research output: Contribution to journalArticlepeer-review


The neurotrophic activity of β-amyloid protein (β-AP) has been suggested to be responsible for the dystrophic neurites that surround β-AP deposits in senile plaques of Alzheimer disease. The recent finding that neurofibrillary tangles (NFT) that remain as remnants in the extracellular space (E-NFT) after the death of the neuron contain β-AP, suggested that dystrophic neurites might also be associated with E-NFT. In this study, we use a probe for E-NFT, basic fibroblast growth factor (bFGF)-binding to show that E-NFT do contain dystrophic neurites. Since these neurites contain the amyloid precursor protein whose cleavage can lead to β-AP, they may also play a role in further β-AP deposition in the E-NFT.

Original languageEnglish (US)
Pages (from-to)303-305
Number of pages3
JournalBrain research
Issue number1-2
StatePublished - Sep 27 1991
Externally publishedYes


  • Alzheimer disease
  • Amyloid
  • Amyloid precursor protein
  • Paired helical filament
  • Senile plaque
  • τ

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Clinical Neurology
  • Developmental Biology


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