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신경세포 연접소낭의 수송에 미치는 α-synuclein 역할 규명
Reports NRF is supported by Research Projects( 신경세포 연접소낭의 수송에 미치는 α-synuclein 역할 규명 | 2005 Year 신청요강 다운로드 PDF다운로드 | 이학주(세종대학교) ) data is submitted to the NRF Project Results
Researcher who has been awarded a research grant by Humanities and Social Studies Support Program of NRF has to submit an end product within 6 months(* depend on the form of business)
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  • Researchers have entered the information directly to the NRF of Korea research support system
Project Number C00026
Year(selected) 2005 Year
the present condition of Project 종료
State of proposition 재단승인
Completion Date 2007년 01월 09일
Year type 결과보고
Year(final report) 2007년
Research result report
  • Abstract
  • a-Synuclein (a-syn) constitutes the major fibrillar component of Lewy bodies and Lewy neurites, and has been implicated in the pathogenesis of Parkinson’s disease (PD). Although a-syn is highly conserved, its normal function in the central nervous system remains unclear. a-syn has been known as a naively unstructured proteins, but it may acquire some secondary structures upon interaction with their partner(s).
    In an effort to define functions from analysis of interacting partners, a phage display library, constructed using human brain cDNA library, has been employed to identify a-syn-interacting protein(s). Some phages that selectively bind to a-syn contained the prenylated Rab acceptor protein 1 (PRA1), vesicle t-SNARE interacting protein homologous 1B (VTI1B), and spectrin beta non-erythrocyte 1 (SPTBN1) cDNA fragments. Not only three candidate proteins were co-precipitated with a-syn in vitro, but also the overexpressed proteins in N2a mouse neuronal cells was co-immunoprecipitated with a-syn. PRA1, VTI1B, and SPTBN1 were also co-localized with a-syn. Co-transfection of a-syn with PRA1, VTI1B, and SPTBN1, showed effects on PRA1 movement to axon terminals, Subcellular distribution of vesicles, and neurite extension.
    Our results suggest that a-syn, cooperated with PRA1, VTI1B, and SPTN1, may participate in vesicle trafficking, vesicle fusion with target membrane, and synaptic plasticity in neuronal cells, respectively.
  • Research result and Utilization method
  • a-Syn은 퇴행성 뇌질환인 파킨슨병의 원인 단백질로 보고되어졌지만, 현재 생물학적 기능과 질병의 원인에 대한 규명이 명확히 이루어지지 않았다. 본 연구에서는 a-syn과 상호작용하는 단백질을 탐색하여, a-syn의 기능을 규명하였다. a-Syn은 세포 내 물질 수송에 관여하는 소낭체의 이동을 조절하며, 세포의 분화 과정 동안 세포의 형태를 결정해줌을 밝혔다. 결론적으로 a-syn은 PRA1, VTI1B, SPTBN1과의 상호작용을 통하여 소낭체의 이동 및 융합, 시냅스의 가소성을 조절함을 규명하였다. 본 연구는 a-syn의 기능을 유추하였고, 이는 파킨슨병 원인과 치료에 대한 배경 지식을 제공할 수 있을 것으로 기대한다.
  • Index terms
  • a-Syn, alpha-synuclein; PRA1, prenylated Rab acceptor 1; VTI1B, vesicle t-SNARE interacting protein homologous 1B; SPTBN1, spectrin, beta, non-erythrocyte 1; PD, Parkinson’s disease.
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