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

doi:10.1016/0006-8993(91)91247-X

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 journal › Article › peer-review

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	https://doi.org/10.1016/0006-8993(91)91247-X
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

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10.1016/0006-8993(91)91247-X

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title = "Dystrophic neurites infiltrate extracellular neurofibrillary tangles in Alzheimer disease",

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.",

keywords = "Alzheimer disease, Amyloid, Amyloid precursor protein, Paired helical filament, Senile plaque, τ",

author = "Weghe, {Jennifer Vande} and Patrick Cras and Mitsuru Kawai and Siedlak, {Sandra L.} and Massimo Tabaton and Barry Greenberg and George Perry",

note = "Funding Information: Supported by NIH Grants AG07552, AG09287 and K04-000415 to G.P., Fogarty International Fellowships to P.C. and M.K. and the Alzheimer Association of Northwestern Pennsylvania to J.V.W.",

year = "1991",

month = sep,

day = "27",

doi = "10.1016/0006-8993(91)91247-X",

language = "English (US)",

volume = "560",

pages = "303--305",

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T1 - Dystrophic neurites infiltrate extracellular neurofibrillary tangles in Alzheimer disease

AU - Weghe, Jennifer Vande

AU - Cras, Patrick

AU - Kawai, Mitsuru

AU - Siedlak, Sandra L.

AU - Tabaton, Massimo

AU - Greenberg, Barry

AU - Perry, George

N1 - Funding Information: Supported by NIH Grants AG07552, AG09287 and K04-000415 to G.P., Fogarty International Fellowships to P.C. and M.K. and the Alzheimer Association of Northwestern Pennsylvania to J.V.W.

PY - 1991/9/27

Y1 - 1991/9/27

N2 - 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.

AB - 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.

KW - Alzheimer disease

KW - Amyloid

KW - Amyloid precursor protein

KW - Paired helical filament

KW - Senile plaque

KW - τ

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Dystrophic neurites infiltrate extracellular neurofibrillary tangles in Alzheimer disease

Abstract

Keywords

ASJC Scopus subject areas

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