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. 2011 Aug 15;121(9):3689–3700. doi: 10.1172/JCI45709

Figure 2. Effect of CR-PA28αOE on UPS proteolytic function in the heart.

Figure 2

Mice were generated via cross-breeding between those harboring homozygous GFPdgn and hemizygous tTA and those carrying hemizygous PA28α responder Tg. (A and B) Western blot analyses of PA28α and GFPdgn protein levels (n = 4 mice/group). *P < 0.001 vs. all other groups. (C–F) Semiquantitative RT-PCR (C) and RNA dot blot analyses (D and E) of steady-state GFPdgn transcript levels, and assessment of GFPdgn mRNA polysomal distribution (F), in the ventricles of PA28α/tTA/GFPdgn triple-Tg (PA28αOE) and tTA/GFPdgn double-Tg control littermates. (C and D) GAPDH was analyzed for the loading control. (F) Polysomes were isolated from ventricular myocardium using sucrose gradients (see Methods). RNAs were extracted from the gradient fractions and used for RT-PCR to detect the distribution of GFPdgn mRNA. PA28α and GAPDH were probed as positive and negative controls, respectively.