作者
Thomas Antony, Wolfgang Hoyer, Dmitry Cherny, Gudrun Heim, Thomas M Jovin, Vinod Subramaniam
发表日期
2003/1/31
期刊
Journal of Biological Chemistry
卷号
278
期号
5
页码范围
3235-3240
出版商
Elsevier
简介
The cellular polyamines putrescine, spermidine, and spermine accelerate the aggregation and fibrillization of α-synuclein, the major protein component of Lewy bodies associated with Parkinson's disease. Circular dichroism and fluorometric thioflavin T kinetic studies showed a transition of α-synuclein from unaggregated to highly aggregated states, characterized by lag and transition phases. In the presence of polyamines, both the lag and transition times were significantly shorter. All three polyamines accelerated the aggregation and fibrillization of α-synuclein to a degree that increased with the total charge, length, and concentration of the polyamine. Electron and scanning force microscopy of the reaction products after the lag phase revealed the presence of aggregated particles (protofibrils) and small fibrils. At the end of the transition phase, α-synuclein formed long fibrils in all cases, although some …
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T Antony, W Hoyer, D Cherny, G Heim, TM Jovin… - Journal of Biological Chemistry, 2003