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The secreted oligomeric form of alpha-synuclein affects mulpitple steps of membrane trafficking

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Authors
채예진
Advisor
장성호
Major
의과대학 의과학과
Issue Date
2013-08
Publisher
서울대학교 대학원
Keywords
alpha-synucleintransferrinParkinson's DiseaseTransferrin receptorEndocytosisMembrane trafficking
Description
학위논문 (석사)-- 서울대학교 대학원 : 의과학과, 2013. 8. 장성호.
Abstract
α-Synuclein (α-syn) can be secreted from neurons into the extracellular space, affecting the homeostasis of neighboring cells, but the pathophysiology of secreted α-syn remains largely unknown. We found that when exogenously applied to COS-7 cells, α-syn secreted from differentiated SH-SY5Y cells was taken up by dynamin-dependent endocytosis. Upon internalization, α-syn significantly increased the rate of transferrin receptor (TfR) internalization and recycling, and subsequently the surface levels of TfR. The effects are attributable to the oligomeric form, but not monomeric or fibrillar form, of extracellular α-syn. Together, multiple alterations in membrane trafficking by secreted oligomeric α-syn may contribute to the early stages of pathogenesis in Parkinsons disease.
Language
English
URI
https://hdl.handle.net/10371/132983
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College of Medicine/School of Medicine (의과대학/대학원)Dept. of Biomedical Sciences (대학원 의과학과)Theses (Master's Degree_의과학과)
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