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ID: 17253.0, MPI für biophysikalische Chemie / Molekulare Biologie (Dr. Thomas M. Jovin)
Cellular polyamines promote the aggregation of α-synuclein
Authors:Antony, T.; Hoyer, W.; Cherny, D. I.; Heim, G.; Jovin, T. M.; Subramaniam, V.
Date of Publication (YYYY-MM-DD):2003-01-31
Title of Journal:Journal of Biological Chemistry
Issue / Number:5
Start Page:3235
End Page:3240
Review Status:Peer-review
Audience:Not Specified
Abstract / Description: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.
Free Keywords:Atomic force microscopy; Beta-amyloid peptide; Parkinsons disease; Alzheimers-disease; Lewy bodies; Neurodegenerative disorders; Subcellular-localization; Ornithine decarboxylase; Fibril formation; Human brain
Comment of the Author/Creator:Date: 2003, JAN 31
Last Change of the Resource (YYYY-MM-DD):2004-07-27
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für biophysikalische Chemie/Abt. Thomas Jovin / 060
External Affiliations:Max Planck Inst Biophys Chem, Dept Mol Biol, Fasserg 11, D-; 37077 Gottingen, Germany; Max Planck Inst Biophys Chem, Dept Mol Biol, D-37077 Gottingen, Germany; Russian Acad Sci, Inst Mol Genet, Moscow 123182, Russia
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