HKUST Library Institutional Repository Banner

HKUST Institutional Repository >
Division of Life Science >
LIFS Doctoral Theses  >

Please use this identifier to cite or link to this item: http://hdl.handle.net/1783.1/7594
Title: Alpha-synuclein impairs normal dynamics of mitochondria in cell and animal models of Parkinson's disease
Authors: Xie, Weilin
Issue Date: 2011
Abstract: Parkinson’s disease (PD) is a progressive movement disorder marked by a selective dopaminergic neuronal loss in the brain stem and the presence of protein aggregates designated as Lewy bodies (LBs). The cause of most PD cases is not known but a small percentage of patients are known to inherit the disease from the family. Alpha-synuclein (α-syn) is a synaptic protein that mutations have been linked to Parkinson’s disease (PD), a common neurodegenerative disorder that is caused by the degeneration of the dopaminergic neurons in the substantia nigra (SNc). How α-syn can contribute to neurodegeneration in PD is not conclusive but it is agreed that mutations or excessive accumulation of α-syn can lead to the formation of α-syn oligomers or aggregates that interfere with normal cellular function and contribute to the degeneration of dopaminergic neurons. In this study, we found that α-syn can impair the normal dynamics of mitochondria and this effect is particular prominent in A53T α-syn mutant. In the cellular model of PD, we found that α-syn reduces the movement of mitochondria in both SH-SHY5Y neuroblastoma and in hippocampal neurons. In mice expressing A53T α-syn, age-dependent changes in both mitochondrial morphology and proteins that regulate mitochondrial fission and fusion were observed. Taken together, our study provides a new mechanism of how α-syn can contribute to PD through the impairment of normal dynamics of mitochondria.
Description: Thesis (Ph.D.)--Hong Kong University of Science and Technology, 2011
xii, 119 p. : ill. (some col.) ; 30 cm
HKUST Call Number: Thesis LIFS 2011 Xie
URI: http://hdl.handle.net/1783.1/7594
Appears in Collections:LIFS Doctoral Theses

Files in This Item:

File Description SizeFormat
th_redirect.html0KbHTMLView/Open

All items in this Repository are protected by copyright, with all rights reserved.