| First Author | Xie W | Year | 2012 |
| Journal | J Neurochem | Volume | 122 |
| Issue | 2 | Pages | 404-14 |
| PubMed ID | 22537068 | Mgi Jnum | J:186510 |
| Mgi Id | MGI:5432455 | Doi | 10.1111/j.1471-4159.2012.07769.x |
| Citation | Xie W, et al. (2012) Alpha-synuclein impairs normal dynamics of mitochondria in cell and animal models of Parkinson's disease. J Neurochem 122(2):404-14 |
| abstractText | Alpha-synuclein (alpha-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 alpha-syn can contribute to neurodegeneration in PD is not conclusive but it is agreed that mutations or excessive accumulation of alpha-syn can lead to the formation of alpha-syn oligomers or aggregates that interfere with normal cellular function and contribute to the degeneration of dopaminergic neurons. In this study, we found that alpha-syn can impair the normal dynamics of mitochondria and this effect is particular prominent in A53T alpha-syn mutant. In mice expressing A53T alpha-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 alpha-syn reduces the movement of mitochondria in both SH-SY5Y neuroblastoma and hippocampal neurons. Taken together, our study provides a new mechanism of how alpha-syn can contribute to PD through the impairment of normal dynamics of mitochondria. |
