Acetylcholinesterase, a senile plaque component, affects the fibrillogenesis of amyloid-β-peptides

Alejandra Alvarez; Francisca Bronfman; Cristián A. Pérez; Matías Vicente; Jorge Garrido; Nibaldo C. Inestrosa

doi:10.1016/0304-3940(94)12127-C

Acetylcholinesterase, a senile plaque component, affects the fibrillogenesis of amyloid-β-peptides

Alejandra Alvarez, Francisca Bronfman, Cristián A. Pérez, Matías Vicente, Jorge Garrido, Nibaldo C. Inestrosa

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Resumen

Acetylcholinesterase (AChE) colocalizes with amyloid -β peptide (Aβ) deposits present in the brain of Alzheimer's patients. Recent studies showed that Aβ_1-40 can adopt two different conformational states in solution (an amyloidogenic conformer, Aβ ac, and a non-amyloidogenic conformer, Aβ nac) which have distinct abilities to form amyloid fibrils. We report here that AChE binds Aβ nac and accelerates amyloid formation by the same peptide. No such effect was observed with Aβ ac, the amyloidogenic conformer, suggesting that AChE acts as a 'pathological chaperone' inducing a conformational transition from Aβ nac into Aβ ac in vitro.

Idioma original	Inglés
Páginas (desde-hasta)	49-52
Número de páginas	4
Publicación	Neuroscience Letters
Volumen	201
N.º	1
DOI	https://doi.org/10.1016/0304-3940(94)12127-C
Estado	Publicada - 1 dic. 1995
Publicado de forma externa	Sí

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Neurociencias General

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title = "Acetylcholinesterase, a senile plaque component, affects the fibrillogenesis of amyloid-β-peptides",

abstract = "Acetylcholinesterase (AChE) colocalizes with amyloid -β peptide (Aβ) deposits present in the brain of Alzheimer's patients. Recent studies showed that Aβ1-40 can adopt two different conformational states in solution (an amyloidogenic conformer, Aβ ac, and a non-amyloidogenic conformer, Aβ nac) which have distinct abilities to form amyloid fibrils. We report here that AChE binds Aβ nac and accelerates amyloid formation by the same peptide. No such effect was observed with Aβ ac, the amyloidogenic conformer, suggesting that AChE acts as a 'pathological chaperone' inducing a conformational transition from Aβ nac into Aβ ac in vitro.",

keywords = "Acetylcholinesterase, Alzheimer's disease, Brain G, Fibrillogenesis, Synthetic amyloid-β peptides",

author = "Alejandra Alvarez and Francisca Bronfman and P{\'e}rez, {Cristi{\'a}n A.} and Mat{\'i}as Vicente and Jorge Garrido and Inestrosa, {Nibaldo C.}",

note = "Funding Information: This work was supported by FONDECYT grant no. 1940694 to N.C.I., a predoctoral fellowship from CONICYT to A.A. and F.B., and an M.Sc. fellowship from Catholic University to C.A.P.",

year = "1995",

month = dec,

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doi = "10.1016/0304-3940(94)12127-C",

language = "English",

volume = "201",

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journal = "Neuroscience Letters",

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TY - JOUR

T1 - Acetylcholinesterase, a senile plaque component, affects the fibrillogenesis of amyloid-β-peptides

AU - Alvarez, Alejandra

AU - Bronfman, Francisca

AU - Pérez, Cristián A.

AU - Vicente, Matías

AU - Garrido, Jorge

AU - Inestrosa, Nibaldo C.

N1 - Funding Information: This work was supported by FONDECYT grant no. 1940694 to N.C.I., a predoctoral fellowship from CONICYT to A.A. and F.B., and an M.Sc. fellowship from Catholic University to C.A.P.

PY - 1995/12/1

Y1 - 1995/12/1

N2 - Acetylcholinesterase (AChE) colocalizes with amyloid -β peptide (Aβ) deposits present in the brain of Alzheimer's patients. Recent studies showed that Aβ1-40 can adopt two different conformational states in solution (an amyloidogenic conformer, Aβ ac, and a non-amyloidogenic conformer, Aβ nac) which have distinct abilities to form amyloid fibrils. We report here that AChE binds Aβ nac and accelerates amyloid formation by the same peptide. No such effect was observed with Aβ ac, the amyloidogenic conformer, suggesting that AChE acts as a 'pathological chaperone' inducing a conformational transition from Aβ nac into Aβ ac in vitro.

AB - Acetylcholinesterase (AChE) colocalizes with amyloid -β peptide (Aβ) deposits present in the brain of Alzheimer's patients. Recent studies showed that Aβ1-40 can adopt two different conformational states in solution (an amyloidogenic conformer, Aβ ac, and a non-amyloidogenic conformer, Aβ nac) which have distinct abilities to form amyloid fibrils. We report here that AChE binds Aβ nac and accelerates amyloid formation by the same peptide. No such effect was observed with Aβ ac, the amyloidogenic conformer, suggesting that AChE acts as a 'pathological chaperone' inducing a conformational transition from Aβ nac into Aβ ac in vitro.

KW - Acetylcholinesterase

KW - Alzheimer's disease

KW - Brain G

KW - Fibrillogenesis

KW - Synthetic amyloid-β peptides

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U2 - 10.1016/0304-3940(94)12127-C

DO - 10.1016/0304-3940(94)12127-C

M3 - Article

C2 - 8830310

AN - SCOPUS:0028818362

SN - 0304-3940

VL - 201

SP - 49

EP - 52

JO - Neuroscience Letters

JF - Neuroscience Letters

IS - 1

ER -

Acetylcholinesterase, a senile plaque component, affects the fibrillogenesis of amyloid-β-peptides

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