期刊
NEUROCHEMICAL RESEARCH
卷 40, 期 7, 页码 1341-1349出版社
SPRINGER/PLENUM PUBLISHERS
DOI: 10.1007/s11064-015-1597-y
关键词
Dopamine; Norepinephrine; Parkinson's disease; Alpha-synuclein; Oligomers
资金
- NSF [CHE-1229562]
- Elon Chemistry Department, Elon College, Elon University
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1229562] Funding Source: National Science Foundation
Aggregation of the protein alpha-synuclein has been identified in the pathogenesis of Parkinson's disease and is initiated by the folding of the protein monomer into an amyloid form of insoluble fibrils. The neurotransmitters dopamine and norepinephrine have been shown to both inhibit the formation of these fibrils and disaggregate existing fibrils, yielding the more toxic oligomeric form of alpha-synuclein. This study characterizes the stable oligomers formed through the aggregation and disaggregation processes in the presence of these catecholamines, and suggests differences in oligomer formation depending on the extent of oxidation of the neurotransmitter at the time of oligomerization. Unique oligomers are also stabilized, likely formed from the aggregation of monomeric alpha-synuclein and a proteolytic fragment of alpha-synuclein; however, proteolytic fragments do not form as readily in the presence of these neurotransmitters. These findings suggest novel pathways for the formation of alpha-synuclein oligomers in the presence of neurotransmitters, particularly oxidized forms.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据