[S-25] シンポジウム25
オートファジーからせまるアルツハイマー病・認知症疾患

[S-25-3] 神経変性における顆粒空胞変性

^○牧岡 幸樹¹, 山崎 恒夫², 高玉 真光³, 岡本 幸市³, 池田 佳生¹ (1.群馬大学病院 脳神経内科, 2.群馬大学大学院保健学研究科, 3.老年病研究所附属病院)

The deposition of abnormally misfolded proteins, amyloid β protein (Aβ), and tau protein is pathogenic mechanisms of Alzheimer’s disease (AD). Aβ forms senile plaques, and tau aggregates forms neurofibrillary tangles. Misfolded α-synuclein is observed in dementia with lewy bodies (DLB), and aggregated α-synuclein forms Lewy bodies. Autophagy is the main conserved pathway for the degeneration of aggregated proteins, Aβ, tau, and dysfunctional organelles in the cell. α-synuclein is also degraded in autophagy. Many animal model studies have demonstrated that autophagy normally functions as the protective factor against AD, and DLB. So, the upregulation of autophagy can be favorable in AD, or DLB treatment. The cellular and molecular machineries of autophagy, their function in the pathogenesis of AD and DLB, and current drug discovery strategies will be discussed.

1994- 2000 Shimane Medical University (Izumo/Japan)
2000 Resident of Neurology; Gunma University Hospital
2006-2009 Gunma University Graduate School of Medicine (Maebashi / Japan)
2011-2016 Research Associate; Gunma University Hospital
2016-2019 Research Fellow; Brigham and Women’s Hospital
2019- Research Associate; Gunma University Hospital