Neuro-cell biological studies of alpha-synuclein

在对阿尔茨海默病脑组织sds不溶性物质进行生化检测后，我们通过cDNA克隆鉴定了人α - synuclein。发现一些α -突触核蛋白基因错义突变是家族性帕金森病和家族性路易体痴呆患者的致病基因。然而，α -突触核蛋白的生理功能尚不清楚。在目前的研究中，我们发现α - synuclein定位于神经元线粒体的内膜，并且α - synuclein结合腺苷酸转运子。提示-突触核蛋白可能通过线粒体通透性过渡孔调节ATP的产生。利用体外细胞培养系统，我们发现α -突触核蛋白促进细胞增殖并影响早期神经突的生长。结果表明，这些作用是通过α -突触核蛋白组装微管蛋白形成的。

After the biochemical examination of SDS-insoluble materials of the brains with Alzheimer's disease, we identified human alpha-Synuclein by cDNA cloning. Some missense mutations of the gene for alpha-Synuclein were found as causal genes for the patients with familial Parkinson's disease and with familial dementia with Lewy bodies. However, physiological functions of alpha-Synuclein remain elusive. In the present studies, we have shown that alpha-Synuclein is localized in the inner membrane of neuronal mitochondria, and that alpha-Synuclein binds adenylate translocator. It suggests that alpha-Synuclein may regulate the production of ATP through mitochondrial permeability transition pore. Using in vitro cell culture systems, we showed that alpha-Synuclein promotes cell proliferation and affects early neurite outgrowth. It was shown that these effects are through microtubule formation via tubulin assembly by alpha-Synuclein.