PrP<sup>Sc</sup> in N2a-FK cells is potently increased by a lysosomal but not by a proteasomal inhibitor. Daisuke Ishibashi Takujiro Homma Takehiro Nakagaki Takayuki Fuse Kazunori Sano Hanae Takatsuki Ryuichiro Atarashi Noriyuki Nishida 10.1371/journal.pone.0137958.g001 https://plos.figshare.com/articles/figure/_PrP_Sc_in_N2a_FK_cells_is_potently_increased_by_a_lysosomal_but_not_by_a_proteasomal_inhibitor_/1541291 <p>(A) N2aFK cells were treated for 48 h with 0.01 to 1 μM MG132 and 0.1 to 10 nM epoxomicin (Epo) as proteasome inhibitors and 0.1 to 10 mM NH<sub>4</sub>Cl as a lysosomal inhibitor. PK-treated and-untreated N2a-FK cells were loaded at concentrations of 100 and 30 μg protein per lane onto a 15% polyacrylamide gel and subjected to SDS-PAGE. The proteins were detected by western blotting using anti-PrP and -β-actin antibodies. (B) For densitometric analysis, PrP<sup>Sc</sup> band intensities are expressed as a percentage of those of the negative controls. The results in the graph are the mean ± SD of at least three independent experiments. *p < 0.05 and **p < 0.01 (one-way ANOVA followed by Tukey's test).</p> 2015-09-14 02:50:21 macroautophagy inducer rapamycin fk cells stably Prion Strains Chandler strain 22 L Infected Neuronal Cells Prion diseases Host cells neurodegenerative disorders signal transduction pathways PrPSc degradation Abnormally Folded Prion Protein Degradation 3 MA prion protein prion strain Fukuoka accumulation