The propagation of prion-like protein inclusions in neurodegenerative diseases

被引：353

作者：

Goedert, Michel ^{[1
]}

Clavaguera, Florence ^{[2
]}

Tolnay, Markus ^{[2
]}

机构：

[1] MRC, Mol Biol Lab, Cambridge CB2 0QH, England

[2] Univ Basel, Inst Pathol, CH-4031 Basel, Switzerland

来源：

TRENDS IN NEUROSCIENCES | 2010年 / 33卷 / 07期

基金：

瑞士国家科学基金会; 英国医学研究理事会;

关键词：

AMYOTROPHIC-LATERAL-SCLEROSIS; MULTIPLE SYSTEM ATROPHY; PROGRESSIVE SUPRANUCLEAR PALSY; GLIAL CYTOPLASMIC INCLUSIONS; FAMILIAL ALZHEIMERS-DISEASE; MUTANT SUPEROXIDE-DISMUTASE; TAU-TRANSGENIC MICE; ALPHA-SYNUCLEIN; PARKINSONS-DISEASE; LEWY BODIES;

D O I：

10.1016/j.tins.2010.04.003

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

The most common neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease, are characterized by the misfolding of a small number of proteins that assemble into ordered aggregates in affected brain cells. For many years, the events leading to aggregate formation were believed to be entirely cell-autonomous, with protein misfolding occurring independently in many cells. Recent research has now shown that cell non-autonomous mechanisms are also important for the pathogenesis of neurodegenerative diseases with intracellular filamentous inclusions. The intercellular transfer of inclusions made of tau, a-synuclein, huntingtin and superoxide dismutase 1 has been demonstrated, revealing the existence of mechanisms reminiscent of those by which prions spread through the nervous system.

引用

页码：317 / 325

页数：9

共 110 条

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