Live Cell FRET Imaging Reveals Amyloid β-Peptide Oligomerization in Hippocampal Neurons |
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| Authors: | Yang Gao Stefan Wennmalm Bengt Winblad Sophia Schedin-Weiss Lars O. Tjernberg |
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| Affiliation: | 1.Department of Neurobiology, Care Sciences and Society, Division of Neurogeriatrics, Karolinska Institutet, 171 64 Solna, Sweden; (Y.G.); (B.W.); (S.S.-W.);2.SciLifeLab, Department of Applied Physics, Biophysics, Royal Institute of Technology, 171 65 Solna, Sweden;3.Theme Inflammation and Aging, Karolinska University Hospital, 141 86 Huddinge, Sweden |
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| Abstract: | Amyloid β-peptide (Aβ) oligomerization is believed to contribute to the neuronal dysfunction in Alzheimer disease (AD). Despite decades of research, many details of Aβ oligomerization in neurons still need to be revealed. Förster resonance energy transfer (FRET) is a simple but effective way to study molecular interactions. Here, we used a confocal microscope with a sensitive Airyscan detector for FRET detection. By live cell FRET imaging, we detected Aβ42 oligomerization in primary neurons. The neurons were incubated with fluorescently labeled Aβ42 in the cell culture medium for 24 h. Aβ42 were internalized and oligomerized in the lysosomes/late endosomes in a concentration-dependent manner. Both the cellular uptake and intracellular oligomerization of Aβ42 were significantly higher than for Aβ40. These findings provide a better understanding of Aβ42 oligomerization in neurons. |
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| Keywords: | amyloid β -peptide, oligomerization, aggregation, FRET |
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