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Fig. 5 | Acta Neuropathologica Communications

Fig. 5

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

Fig. 5

Association of ps-αSyn with mitochondria in primary neuron and transgenic mouse models. a ps-αSyn and CCAAT-enhancer-binding protein homologous protein (CHOP) accumulations in primary neurons treated with the proteasomal inhibitor epoxomicin (Epo) were determined by immunoblot analyses. b The homogenates prepared from Epo-treated (+) or untreated (−) neurons were separated into mitochondrial fraction (mito) and cytosolic/microsomal fraction (cyto+ms) by differential centrifugation. The mitochondrial enrichment of proteasomal-inhibition-induced ps-αSyn, mitochondrial ATPIF1, and the cytosolic marker GAPDH were detected by immunoblot analyses. c An A53T transgenic mouse was sacrificed at terminal stage of neurodegeneration (T, 305 d of age); Littermates of A53T transgenic mice intramuscularly injected with PBS (C) or αSyn PFF (F) were sacrificed when the PFF-injected mouse developed terminal neurodegeneration at 67 d after injection (135 d of age). Spinal cord homogenates prepared from these mice were separated into mitochondrial (mito) and cytosolic/microsomal (cyto+ms) fractions by differential centrifugation. ps-αSyn, total αSyn, mitochondrial ATP synthase (ATP5A), and cytosolic GAPDH were detected by immunoblot analyses. d Mitochondria isolated from the spinal cords of transgenic mice that received PBS (control) or αSyn PFF (+PFF) injections were subjected to iodixanol gradient separation, and the presence of ps-αSyn and ATPIF1 was detected by immunoblot analyses

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