Prion-like spread of protein aggregates in neurodegeneration

被引：144

作者：

Polymenidou, Magdalini ^{[1
,2
]}

Cleveland, Don W. ^{[1
,2
]}

机构：

[1] Univ Calif San Diego, Ludwig Inst Canc Res, La Jolla, CA 92093 USA

[2] Univ Calif San Diego, Dept Cellular & Mol Med, La Jolla, CA 92093 USA

来源：

JOURNAL OF EXPERIMENTAL MEDICINE | 2012年 / 209卷 / 05期

关键词：

ALPHA-SYNUCLEIN; PARKINSONS-DISEASE; ALZHEIMERS-DISEASE; SCRAPIE; MICE; PATHOLOGY; MUTATION; BRAIN; ALS; TRANSMISSION;

D O I：

10.1084/jem.20120741

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

Protein misfolding is common to most neurodegenerative diseases, including Alzheimer's and Parkinson's diseases. Recent work using animal models with intracellular alpha-synuclein and tau inclusions adds decisively to a growing body of evidence that misfolded protein aggregates can induce a self-perpetuating process that leads to amplification and spreading of pathological protein assemblies. When coupled with the progressive nature of neurodegeneration, recognition of such cell-to-cell aggregate spread suggests a unifying mechanism underlying the pathogenesis of these disorders.

引用

页码：889 / 893

页数：5

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