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Fig. 1 | Molecular Brain

Fig. 1

From: Amyloid β oligomers elicit mitochondrial transport defects and fragmentation in a time-dependent and pathway-specific manner

Fig. 1

Selective inhibition of fast transport of mitochondria by Aβ oligomers. a Western blotting (WB, upper panel) and silver staining (SS, lower panel) showing the presence of Aβ monomers (1) and small Aβ oligomers, including dimmers (2), trimmers (3), and tetramers (4) in our Aβ oligomeric preparation (Aβ–O) from synthetic Aβ1-42. b Representative images showing hippocampal neurons with their late endosomes/lysosomes (endo/lysosomes; upper panels) and mitochondria (lower panels) labeled by LysoTracker and MitoTracker (left panels), as well as their movement tracings generated from 5 min time-lapse sequences before (middle panels) and after (right panels) 2 h exposure to 1 μM Aβ–O. Scale bar: 10 μm. c Quantitative analysis showing the dose- and exposure time-dependent Aβ–O effects on the fast transport of mitochondria and endo/lysosomes. Aβ42-1 was the negative control. All the data were normalized to the number of moving organelles in the 5-min time-lapse sequence before different treatments (see Methods). Each condition was repeated at least three times from different rounds of cultures and was averaged from 10 -20 cells. Error bars indicate the standard deviation (SD). *p < 0.05 and **p < 0.005 in comparison to the corresponding control (Student’s t-test). d Representative images (left) and kymographs (middle) showing the movement of mitochondria before and after Aβ oligomers 1 μM 2 h treatment. The kymographs are produced using the segmented lines labeled on the left images. Averaged transport speeds of mitochondria after different treatments are shown in the bar graph on the right. Data are from three dishes containing around total 60–150 moving mitochondria. Error bars indicate the standard error of the mean (SEM). **p < 0.005 when compared to the respective control period (Student’s t-test)

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