• Top page
  • Timetable
  • Per session
  • Per presentation
  • How to
  • Meeting Planner



日本-韓国神経科学学会合同シンポジウム:Molecular Mechanisms underlying Parkinson Disease
Joint Symposium of the Japan Neuroscience Society and the Korean Society of Brain and Neuroscience:Molecular Mechanisms underlying Parkinson Disease

開催日 2014/9/12
時間 9:00 - 11:00
会場 Room C(502)
Chairperson(s) 望月 秀樹 / Hideki Mochizuki (大阪大学医学系研究科神経内科学 / Department of Neurology, Osaka University Graduate School of Medicine, Japan)
Young Jun Oh (Department of Systems Biology, Yonsei University College of Life Science and Biotechnology, Korea)

Structure and function of α-synuclein

  • S2-C-1-5
  • 望月 秀樹 / Hideki Mochizuki: 
  • 1:大阪大学医学系研究科神経内科学 / Department of Neurology, Osaka University Graduate School of Medicine, Japan 

The presence of α-synuclein (αSyn) -rich aggregates (Lewy bodies) in neurons of the substantia nigra is the defining histopathological hallmark of Parkinson's disease (PD). It has so far been reported that αSyn was an unfolded monomer without a specific structure. Recently, several studies suggested that αSyn produced in Escherichia coli or isolated from mammalian cells exists predominantly as a tetramer. I will present our data of αSyn proteins and brain analysis by small-angle X-ray (SAXS) at Spring-8 in Japan and neutron (SANS) scattering at The Institute Laue-Langevin (ILL) in France.
I also focus on the function of αsyn. Recent report showed that more than 90% of αSyn aggregates are present in the form of very small deposits in presynaptic terminals of the affected neurons in DLB. However, the mechanisms responsible for the presynaptic accumulation of abnormal αSyn remain unclear. I will review the recent findings on the involvement of presynaptic dysfunction in the initiation of neuronal dysfunctional changes including our data.

Copyright © Neuroscience2014. All Right Reserved.