Structure of β-amyloid fibrils and its relevance to their neurotoxicity:: Implications for the pathogenesis of Alzheimer's disease

被引：80

作者：

Irie, K ^{[1
]}

Murakami, K

Masuda, Y

Morimoto, A

Ohigashi, H

Ohashi, R

Takegoshi, K

Nagao, M

Shimizu, T

Shirasawa, T

机构：

[1] Kyoto Univ, Div Food Sci & Biotechnol, Grad Sch Agr, Sakyo Ku, Kyoto 6068502, Japan

[2] Kyoto Univ, Dept Chem, Grad Sch Sci, Sakyo Ku, Kyoto 6068502, Japan

[3] Kyoto Univ, Div Integrated Life Sci, Grad Sch Biostudies, Sakyo Ku, Kyoto 6068502, Japan

[4] Tokyo Metropolitan Inst Gerontol, Dept Mol Gerontol, Itabashi Ku, Tokyo 1730015, Japan

来源：

JOURNAL OF BIOSCIENCE AND BIOENGINEERING | 2005年 / 99卷 / 05期

关键词：

Alzheimer's disease; A beta 40; A beta 42; amyloid; cerebral amyloid angiopathy; familial Alzheimer's disease; neurotoxicity; oxidative stress; solid-state nuclear magnetic resonance;

D O I：

10.1263/jbb.99.437

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Alzheimer's disease and cerebral amyloid angiopathy are characterized by the deposition of P-amyloid fibrils consisting of 40- and 42-mer peptides (A beta 40 and A beta 42). Since the aggregation (fibrilization) of these peptides is closely related to the pathogenesis of these diseases, numerous structural analyses of A beta 40 and A beta 42 fibrils have been carried out. A beta 42 plays a more important role in the pathogenesis of these diseases since its aggregative ability and neurotoxicity are considerably greater than those of A beta 40. This review summarizes mainly our own recent findings from the structural analysis of A beta 42 fibrils and discusses its relevance to their neurotoxicity in vitro.

引用

页码：437 / 447

页数：11

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