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  Cellular polyamines promote the aggregation of α-synuclein

Antony, T., Hoyer, W., Cherny, D. I., Heim, G., Jovin, T. M., & Subramaniam, V. (2003). Cellular polyamines promote the aggregation of α-synuclein. Journal of Biological Chemistry, 278(5), 3235-3240. Retrieved from http://www.jbc.org/content/278/5/3235.full.pdf+html.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F18D-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-DFF6-7
Genre: Journal Article

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 Creators:
Antony, T.1, Author              
Hoyer, W.1, Author              
Cherny, D. I.1, Author              
Heim, G.2, Author              
Jovin, T. M.1, Author              
Subramaniam, V.1, Author              
Affiliations:
1Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society, ou_578628              
2Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society, ou_578615              

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Free keywords: Atomic force microscopy; Beta-amyloid peptide; Parkinsons disease; Alzheimers-disease; Lewy bodies; Neurodegenerative disorders; Subcellular-localization; Ornithine decarboxylase; Fibril formation; Human brain
 Abstract: 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 morphological variations were apparent. In the presence of polyamines, fibrils formed large networks leading ultimately to condensed aggregates. In the absence of polyamines, fibrils were mostly isolated. We conclude that the polyamines at physiological concentrations can modulate the propensity of α-synuclein to form fibrils and may hence play a role in the formation of cytosolic alpha- synuclein aggregates.

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Language(s): eng - English
 Dates: 2004-07-272003-01-31
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 278 (5) Sequence Number: - Start / End Page: 3235 - 3240 Identifier: -