Journal
COMMUNICATIONS BIOLOGY
Volume 1, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s42003-018-0156-x
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Funding
- Research Foundation Flanders (FWO)
- KU Leuven Research Fund [IDO/13/008]
- German research foundation [DFG-TA 1049/1-1]
- China Scholarship Council (CSC) [201608110147]
- National Natural Science Foundation of China [81430025]
- EU-JPND [NEUTARGETs-ANR-14-JPCD-0002-02]
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A hallmark of Parkinson's disease is the formation of large protein-rich aggregates in neurons, where alpha-synuclein is the most abundant protein. A standard approach to visualize aggregation is to fluorescently label the proteins of interest. Then, highly fluorescent regions are assumed to contain aggregated proteins. However, fluorescence brightness alone cannot discriminate micrometer-sized regions with high expression of non-aggregated proteins from regions where the proteins are aggregated on the molecular scale. Here, we demonstrate that 2-dimensional polarization imaging can discriminate between preformed non-aggregated and aggregated forms of alpha-synuclein, and detect increased aggregation in brain tissues of transgenic mice. This imaging method assesses homo-FRET between labels by measuring fluorescence polarization in excitation and emission simultaneously, which translates into higher contrast than fluorescence anisotropy imaging. Exploring earlier aggregation states of alpha-synuclein using such technically simple imaging method could lead to crucial improvements in our understanding of alpha-synuclein-mediated pathology in Parkinson's Disease.
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