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Fig. 6 | Acta Neuropathologica Communications

Fig. 6

From: Pathogenic alpha-synuclein aggregates preferentially bind to mitochondria and affect cellular respiration

Fig. 6

Association of ps-αSyn with mitochondria in α-synucleinopathy patients’ brain tissues. a ps-αSyn in brains of controls (C) and of MSA (M), DLB (D), and PD (P) patients was detected by immunoblot analysis; GAPDH or β-actin was used as a loading control. b PNS prepared from brains of controls or MSA patients were subjected to iodixanol gradient separation. The ps-αSyn, total αSyn, and ATPIF1 were detected by immunoblotting. c The curve reflects the percentage of ps-αSyn or αSyn in each fraction, which is the average ± standard error of two control samples and two MSA patient samples that were separated by the gradient individually. d PNS prepared from brains of controls (C) and MSA (M) patients were separated into mitochondrial (mito) and cytosolic/microsomal (cyto+ms) fractions, which were verified by immunoblot detection of mitochondrial ATP5A and cytosolic GAPDH. The ps-αSyn and total αSyn in each fraction were detected by immunoblot analysis. f The cingulate cortex of brains from controls (C), DLB patients (D), and PD (P) patients were subjected to the analyses described in panel d. Bar graphs in e and g reflect the quantification of data in panels d and f, respectively, which are average ± standard error of the amount of ps-αSyn and total αSyn in each fraction

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