[S-25] Symposium 25
The Implication of Autophagy in Alzheimer's disease and Dementia

[S-25-4] Alteration of autophagy-related proteins in synucleinopathies

^○Yasuo Miki (Department of Neuropathology, Hirosaki University Graduate School of Medicine, Japan)

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.

[Professional Experience]
2018-2020 Research Associate, Queen Square Brain Bank for Neurological Disorders, UCL Queen Square Institute of Neurology, UK
2013-2018 Assistant Professor, Department of Neuropathology, Hirosaki University Graduate School of Medicine, Japan
2007-2013 MD, Department of Neurology, Aomori Prefectural Central Hospital, Japan
2005-2007 MD, Yodogawa Christian Hospital, Japan
[Education]
2011 PhD, Hirosaki University Graduate School of Medicine, Japan
2005 MD, Hirosaki University School of Medicine, Japan
[Honors and Awards]
2019 JSNP Award, the Japanese Society of Neuropathology
2017 Hirosaki University Outstanding Young Thesis Award, Hirosaki University
2015 JSNP Award, the Japanese Society of Neuropathology
[Research Interests]
Neuropathology of neurodegenerative diseases including synucleinopathies