Dystrophic neurites infiltrate extracellular neurofibrillary tangles in Alzheimer disease.
The neurotrophic activity of beta-amyloid protein (beta-AP) has been suggested to be responsible for the dystrophic neurites that surround beta-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 beta-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 beta-AP, they may also play a role in further beta-AP deposition in the E-NFT.
Vande Weghe
J
J
Division of Neuropathology, Institute of Pathology, Case Western Reserve University, Cleveland, OH 44106.
Cras
P
P
Kawai
M
M
Siedlak
S L
SL
Tabaton
M
M
Greenberg
B
B
Perry
G
G
D000368:Aged; D000544:Alzheimer Disease / Q000473:pathology*; D016229:Amyloid beta-Peptides / Q000378:metabolism; D005110:Extracellular Space; D006801:Humans; D016501:Neurites / Q000378:metabolism / Q000648:ultrastructure*; D016874:Neurofibrillary Tangles / Q000473:pathology*; D016875:tau Proteins / Q000378:metabolism
D016229:Amyloid beta-Peptides; D016875:tau Proteins