2D polarization imaging as a low-cost fluorescence method to detect α-synuclein aggregation ex vivo in models of Parkinson’s disease
Camacho, Rafael ; Täuber, Daniela LU ; Hansen, Christian LU ; Shi, Juanzi LU ; Bousset, Luc ; Melki, Ronald ; Li, Jia-Yi LU and Scheblykin, Ivan LU
(2018)
In Communications Biology
1.
- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/8a23a80d-34b6-476d-950c-69f176de00b5
- author
- Camacho, Rafael
; Täuber, Daniela
LU
; Hansen, Christian
LU
; Shi, Juanzi
LU
; Bousset, Luc
; Melki, Ronald
; Li, Jia-Yi
LU
and Scheblykin, Ivan
LU
- organization
- publishing date
- 2018
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Communications Biology
- volume
- 1
- article number
- 157
- publisher
- Nature Publishing Group
- external identifiers
-
- scopus:85061033624
- ISSN
- 2399-3642
- DOI
- 10.1038/s42003-018-0156-x
- language
- English
- LU publication?
- yes
- id
- 8a23a80d-34b6-476d-950c-69f176de00b5
- date added to LUP
- 2018-10-09 10:54:07
- date last changed
- 2022-04-25 17:53:42
@article{8a23a80d-34b6-476d-950c-69f176de00b5,
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.}},
author = {{Camacho, Rafael and Täuber, Daniela and Hansen, Christian and Shi, Juanzi and Bousset, Luc and Melki, Ronald and Li, Jia-Yi and Scheblykin, Ivan}},
issn = {{2399-3642}},
language = {{eng}},
publisher = {{Nature Publishing Group}},
series = {{Communications Biology}},
title = {{2D polarization imaging as a low-cost fluorescence method to detect α-synuclein aggregation ex vivo in models of Parkinson’s disease}},
url = {{http://dx.doi.org/10.1038/s42003-018-0156-x}},
doi = {{10.1038/s42003-018-0156-x}},
volume = {{1}},
year = {{2018}},
}