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

被引：61

作者：

Alvarez, A ^{[1
]}

Bronfman, F ^{[1
]}

Perez, CA ^{[1
]}

Vicente, M ^{[1
]}

Garrido, J ^{[1
]}

Inestrosa, NC ^{[1
]}

机构：

[1] PONTIFICIA UNIV CATOLICA CHILE,FAC CIENCIAS BIOL,DEPT BIOL CELULAR & MOLEC,SANTIAGO,CHILE

来源：

NEUROSCIENCE LETTERS | 1995年 / 201卷 / 01期

关键词：

acetylcholinesterase; brain G(4); synthetic amyloid-beta peptides; fibrillogenesis; Alzheimer's disease;

D O I：

10.1016/0304-3940(94)12127-C

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

Acetylcholinesterase (AChE) colocalizes with amyloid-beta peptide (A beta) deposits present in the brain of Alzheimer's patients. Recent studies showed that A beta(1-40) Can adopt two different conformational states in solution (an amyloidogenic conformer, A beta ac, and a non-amyloidogenic conformer, A beta nac) which have distinct abilities to form amyloid fibrils. We report here that AChE binds A beta nac and accelerates amyloid formation by the same peptide. No such effect was observed with A beta ac, the amyloidogenic conformer, suggesting that AChE acts as a 'pathological chaperone' inducing a conformational transition from A beta nac into A beta ac in vitro.

引用

页码：49 / 52

页数：4

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