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Title: | 2D polarization imaging as a low-cost fluorescence method to detect α-synuclein aggregation ex vivo in models of Parkinson’s disease |
Authors: | Camacho, Rafael; Täuber, Daniela; Hansen, Christian; Shi, Juanzi; Bousset, Luc; Melki, Ronald; Li, Jia-Yi; Scheblykin, Ivan G. |
Publishers Version: | https://doi.org/10.1038/s42003-018-0156-x |
Issue Date: | 2018 |
Published in: | Communications Biology 1 (2018) |
Publisher: | Berlin : Nature Publishing |
Abstract: | A hallmark of Parkinson’s disease is the formation of large protein-rich aggregates in neurons, where α-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 α-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 α-synuclein using such technically simple imaging method could lead to crucial improvements in our understanding of α-synuclein-mediated pathology in Parkinson’s Disease. |
Keywords: | Parkinson’s disease; protein-rich aggregates; α-synuclein |
DDC: | 570 |
License: | CC BY 4.0 Unported |
Link to License: | https://creativecommons.org/licenses/by/4.0/ |
Appears in Collections: | Ingenieurwissenschaften |
This item is licensed under a Creative Commons License