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Fig. 7 | Acta Neuropathologica Communications

Fig. 7

From: Mechanisms underlying extensive Ser129-phosphorylation in α-synuclein aggregates

Fig. 7

Relation of Ser129-phosphorylation-mediated α-syn clearance between the proteasome and lysosome pathways. Wt-aS/SH #4 cells were fractionated into 1% Triton X-100 soluble and insoluble fractions by centrifugation at 100,000×g for 30 min. In 1% Triton X-100 soluble fractions, the extract (2.5 μg / lane) were loaded onto SDS-PAGE. In 1% Triton X-100 insoluble fractions, samples corresponding to 15 μg of soluble fractions were loaded. Samples were analyzed by western botting with EP1536Y, Syn-1, or AC-15 antibody. a Effect of proteasomal and lysosomal inhibitions on the metabolism of α-syn. Cells were incubated by either 100 nM epoxomicin, 100 μM chloroquine, or 100 nM epoxomicin plus 100 μM chloroquine for 24 h. Vehicle control cells were treated with the same concentration of DMSO. Upper and lower panels show the blots of 1% Triton X-100 insoluble fractions and 1% Triton X-100 soluble fractions, respectively. b Effect of Ser129-phosphorylation on the metabolism of α-syn in proteasomal and lysosomal inhibitions. Wt-aS/SH #4 cells and S129A-aS/SH #10 cells were incubated by either 100 nM epoxomicin, 100 μM chloroquine, or epoxomicin plus chloroquine for 24 h. Upper panels show the blots of 1% Triton X-100 insoluble fractions. Graph shows relative ratios of total α-syn to vehicle control cells. Data represent means ± SD and P values were estimated by one-way ANOVA with Bonferroni correction (*, P < 0.05; **, P < 0.01)

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