Figure 3
Figure 3. LMP2A facilitates p27kip1 degradation in a proteasome-dependent manner. (A) Representative western blot analyses of p27kip1 expression after treatments with 25 μg/mL cycloheximide (CHX) with or without 40 μM MG-132 at indicated time points. The levels of p27kip1 were normalized to calnexin (a loading control), and the fold reductions of proteins were calculated using cells at 0 hour of each genotype as a control. (B) Combined data from 3 experiments represent the mean ± SD of the p27kip1 level. Differences in p27kip1 protein expression were analyzed by 2-way ANOVA. *P < .05, **P < .01, ***P < .001. (C) Representative western blot analyses of pretumor B-cell treatment with vehicle control (dimethyl sulfoxide [DMSO]) 40 μM, or 60 μM MG-132 for 2 hours. Gapdh and calnexin were used as loading controls. The left and right parts of the images shown are from the same membrane, and the middle, irrelevant, lanes were removed. Experiments were repeated at least 3 times.

LMP2A facilitates p27kip1degradation in a proteasome-dependent manner. (A) Representative western blot analyses of p27kip1 expression after treatments with 25 μg/mL cycloheximide (CHX) with or without 40 μM MG-132 at indicated time points. The levels of p27kip1 were normalized to calnexin (a loading control), and the fold reductions of proteins were calculated using cells at 0 hour of each genotype as a control. (B) Combined data from 3 experiments represent the mean ± SD of the p27kip1 level. Differences in p27kip1 protein expression were analyzed by 2-way ANOVA. *P < .05, **P < .01, ***P < .001. (C) Representative western blot analyses of pretumor B-cell treatment with vehicle control (dimethyl sulfoxide [DMSO]) 40 μM, or 60 μM MG-132 for 2 hours. Gapdh and calnexin were used as loading controls. The left and right parts of the images shown are from the same membrane, and the middle, irrelevant, lanes were removed. Experiments were repeated at least 3 times.

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