Human recombinant NACP/α-synuclein is aggregated and fibrillated in vitro:: Relevance for Lewy body disease

被引：243

作者：

Hashimoto, M

Hsu, LJ

Sisk, A

Xia, Y

Takeda, A

Sundsmo, M

Masliah, E ^{[1
]}

机构：

[1] Univ Calif San Diego, Sch Med, Dept Neurosci, La Jolla, CA 92093 USA

[2] Univ Calif San Diego, Sch Med, Dept Pathol, La Jolla, CA 92093 USA

[3] Yokohama City Univ, Sch Med, Dept Psychiat, Kanazawa Ku, Yokohama, Kanagawa 236, Japan

来源：

BRAIN RESEARCH | 1998年 / 799卷 / 02期

关键词：

aggregation; fibrillation; Lewy body; NACP/alpha-synuclein; Parkinson's disease;

D O I：

10.1016/S0006-8993(98)00514-9

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

The precursor of non-amyloid beta protein component of Alzheimer's disease amyloid (NACP/alpha-synuclein) is aggregated and fibrillated under certain conditions, i.e., increasing time lag, high temperature and low pH. These in vitro aggregates form Thioflavine-S-positive filamentous structures, reminiscent of amyloid-like fibrils. Since some Lewy bodies in Parkinson's disease display Thioflavine-S reactivity, our results may suggest that amyloidogenic properties of NACP/alpha-synuclein may play a crucial role in pathogenesis of disorders with Lewy bodies such as Parkinson's disease. (C) 1998 Published by Elsevier Science B.V. All rights reserved.

引用

页码：301 / 306

页数：6