aDivision of Neuropathology, Institute of Pathology, Case Western Reserve University, Cleveland, OH 44106 U.S.A.
bInstitute of Neurology, University of GenoaItaly
cUpjohn Company, Kalamazoo, MI U.S.A.
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.