Prion-like mechanisms in neurodegenerative diseases

被引：589

作者：

Frost, Bess ^{[2
]}

Diamond, Marc I. ^{[1
]}

机构：

[1] Washington Univ, Sch Med, Dept Neurol, St Louis, MO 63110 USA

[2] Harvard Univ, Sch Med, Dept Pathol, Boston, MA 02115 USA

来源：

NATURE REVIEWS NEUROSCIENCE | 2010年 / 11卷 / 03期

关键词：

PARKINSONS-DISEASE; ALZHEIMERS-DISEASE; MOUSE MODEL; PROTEIN; BETA; TAU; INFECTION; PATHOLOGY; SPREAD; CONFORMATIONS;

D O I：

10.1038/nrn2786

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

Many non-infectious neurodegenerative diseases are associated with the accumulation of fibrillar proteins. These diseases all exhibit features that are reminiscent of those of prionopathies, including phenotypic diversity and the propagation of pathology. Furthermore, emerging studies of amyloid-beta, alpha-synuclein and tau - proteins implicated in common neurodegenerative diseases - suggest that they share key biophysical and biochemical characteristics with prions. Propagation of protein misfolding in these diseases may therefore occur through mechanisms similar to those that underlie prion pathogenesis. If this hypothesis is verified in vivo, it will suggest new therapeutic strategies to block propagation of protein misfolding throughout the brain.

引用

页码：155 / 159

页数：5

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