## Abstract Parkinson's disease is neuropathologically characterized by the presence of Lewy bodies, whose major component is α‐synuclein. We had previously generated transgenic mice that expressed human α‐synuclein carrying an Ala53Thr point mutation (hα‐syn140m) under the control of the rat tyros
The behavior of α-synuclein in neurons
✍ Scribed by Doris L. Fortin; Venu M. Nemani; Ken Nakamura; Robert H. Edwards
- Publisher
- John Wiley and Sons
- Year
- 2010
- Tongue
- English
- Weight
- 132 KB
- Volume
- 25
- Category
- Article
- ISSN
- 0885-3185
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
Despite considerable evidence linking α‐synuclein with membranes in vitro, it has proven difficult to demonstrate membrane association of the protein in vivo. α‐Synuclein localizes to the nerve terminal, but biochemical experiments have not revealed a tight association with membranes. To address the dynamics of the protein in live cells, we have used photobleaching and found that α‐synuclein exhibits high mobility, although distinctly less than an entirely soluble protein. Further, neural activity controls the distribution of α‐synuclein, causing its dispersion from the synapse. In addition to the presumed role of α‐synuclein dynamics in synaptic function, changes in its physiological behavior may underlie the pathological changes associated with Parkinson's disease. © 2010 Movement Disorder Society
📜 SIMILAR VOLUMES
The letter by Papapetropoulos and colleagues presents an additional study correlating ␣-synuclein expression levels and sporadic PD. Previously we and others published studies of mRNA levels of SNCA in PD brains that have been performed using different methods. Some are in agreement with our results