Abstract
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 language | English (US) |
---|---|
Pages (from-to) | 303-305 |
Number of pages | 3 |
Journal | Brain research |
Volume | 560 |
Issue number | 1-2 |
DOIs | |
State | Published - Sep 27 1991 |
Externally published | Yes |
Keywords
- Alzheimer disease
- Amyloid
- Amyloid precursor protein
- Paired helical filament
- Senile plaque
- τ
ASJC Scopus subject areas
- Neuroscience(all)
- Molecular Biology
- Clinical Neurology
- Developmental Biology