− この都医学研セミナーは終了しました。 −
Pasteur Institute, Paris, France （Head of Department）
|会場||東京都医学総合研究所 2階 BC会議室|
|世話人||野中 隆（認知症・高次脳機能研究分野 認知症プロジェクト）|
Neurodegenerative diseases (NDs) like Prion disease, Alzheimer’s (AD), Parkinson’s (PD) and Huntington’s (HD) disease are part of a larger group of protein misfolding disorders characterized by the progressive accumulation and spreading of different protein aggregates. Like Prions, misfolded forms of ASYN, tau, Abeta and Htt proteins associated with AD, PD and HD can be transmitted experimentally in cellular and in animal models where act as ‘seeds’ to recruit the endogenous protein into aggregates. However, the mechanism of intercellular transfer is still debated. We have recently described a novel mechanism of PrPSc transmission through Tunneling Nanotubes (TNTs)1. TNTs are actin-based protrusions connecting cells in culture and represents a novel mechanism of cell-to-cell communication. Furthermore mutant polyQ Htt aggregates appear to highjack TNTs2 as well as fibrillar and oligomeric ASYN assemblies3 and Tau fibrils4. We propose that TNTs contribute to the progression of the pathology of NDs by spreading in the brain of misfolded protein assemblies5. We also demonstrated that in vitro and in ex vivo culture models astrocytes have a role in degrading asyn fibrils rather then in transfer6.