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Alpha-synuclein impairs normal dynamics of mitochondria in cell and animal models of Parkinson's disease.
J Neurochem. 2012 Jul; 122(2):404-14.JN

Abstract

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 pars compacta (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 mice expressing A53T α-syn, age-dependent changes in both mitochondrial morphology and proteins that regulate mitochondrial fission and fusion were observed. In the cellular model of PD, we found that α-syn reduces the movement of mitochondria in both SH-SY5Y neuroblastoma and hippocampal neurons. Taken together, our study provides a new mechanism of how α-syn can contribute to PD through the impairment of normal dynamics of mitochondria.

Authors+Show Affiliations

Division of Life Science, State Key Laboratory of Molecular Neuroscience, The Hong Kong University of Science and Technology, Hong Kong, China.No affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

22537068

Citation

Xie, Weilin, and Kenny K K. Chung. "Alpha-synuclein Impairs Normal Dynamics of Mitochondria in Cell and Animal Models of Parkinson's Disease." Journal of Neurochemistry, vol. 122, no. 2, 2012, pp. 404-14.
Xie W, Chung KK. Alpha-synuclein impairs normal dynamics of mitochondria in cell and animal models of Parkinson's disease. J Neurochem. 2012;122(2):404-14.
Xie, W., & Chung, K. K. (2012). Alpha-synuclein impairs normal dynamics of mitochondria in cell and animal models of Parkinson's disease. Journal of Neurochemistry, 122(2), 404-14. https://doi.org/10.1111/j.1471-4159.2012.07769.x
Xie W, Chung KK. Alpha-synuclein Impairs Normal Dynamics of Mitochondria in Cell and Animal Models of Parkinson's Disease. J Neurochem. 2012;122(2):404-14. PubMed PMID: 22537068.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Alpha-synuclein impairs normal dynamics of mitochondria in cell and animal models of Parkinson's disease. AU - Xie,Weilin, AU - Chung,Kenny K K, Y1 - 2012/05/23/ PY - 2012/4/28/entrez PY - 2012/4/28/pubmed PY - 2013/8/15/medline SP - 404 EP - 14 JF - Journal of neurochemistry JO - J Neurochem VL - 122 IS - 2 N2 - 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 pars compacta (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 mice expressing A53T α-syn, age-dependent changes in both mitochondrial morphology and proteins that regulate mitochondrial fission and fusion were observed. In the cellular model of PD, we found that α-syn reduces the movement of mitochondria in both SH-SY5Y neuroblastoma and hippocampal neurons. Taken together, our study provides a new mechanism of how α-syn can contribute to PD through the impairment of normal dynamics of mitochondria. SN - 1471-4159 UR - https://www.unboundmedicine.com/medline/citation/22537068/Alpha_synuclein_impairs_normal_dynamics_of_mitochondria_in_cell_and_animal_models_of_Parkinson's_disease_ L2 - https://doi.org/10.1111/j.1471-4159.2012.07769.x DB - PRIME DP - Unbound Medicine ER -