Department of Pathology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115, USA.
Nat Rev Neurosci. 2010 Mar;11(3):155-9. doi: 10.1038/nrn2786. Epub 2009 Dec 23.
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.
许多非传染性神经退行性疾病与纤维状蛋白质的积累有关。这些疾病都表现出与朊病毒病相似的特征，包括表型多样性和病理学的传播。此外，对淀粉样β、α-突触核蛋白和 tau——这些与常见神经退行性疾病有关的蛋白质——的新兴研究表明，它们与朊病毒具有关键的物理化学特性。因此，这些疾病中蛋白质错误折叠的传播可能通过类似于朊病毒发病机制的机制发生。如果这一假设在体内得到验证，它将为阻断蛋白质错误折叠在整个大脑中的传播提供新的治疗策略。
