Corrigendum to: Pioglitazone Attenuates Drug-Eluting Stent-Induced Proinflammatory State in Patients by Blocking Ubiquitination of PPAR (PPAR Research (2016) 2016 (7407153) DOI: 10.1155/2016/7407153)

In the article titled 'Pioglitazone Attenuates Drug-Eluting Stent-Induced Proinfammatory State in Patients by Blocking Ubiquitination of PPAR' [1], there are additional methods that should be added to the article which are mainly about the methods for PPAR gamma binding and ubiquitination. Te additional methods are shown below: 2.8. Immunoblotting. Protein levels of p65, p50, PPAR-γ, and Gapdh of MNC were detected by western blotting with Santa Cruz antibodies against the p65 subunit (sc- 372), p50 subunit (sc-114), PPAR-γ (sc-7273), and Gapdh (SC-48166) as described previously [24, 25]. Mononuclear cells were lysed in RIPA bufer (Cybrdi, Gaithersburg, MD, USA) that contained protease inhibitor (Roche Diagnostics, Indianapolis, IN, USA). Equal amounts of protein were loaded onto 4'12% Bis-Tris precast gels for electrophoresis and were electrotransferred onto a PVDF membrane (Roche Diagnostics). Afer blocking for 1 h at room temperature, membranes were sequentially incubated with primary Abs at 4°C overnight and secondary Abs at room temperature for 1 h. Te protein signal was detected by chemiluminescence and all values were corrected by loading with Gapdh. 2.9. Immunoprecipitation. Immunoprecipitation assays were performed as described previously [25, 26]. Cell extracts were prepared by using modifed RIPA bufer (Cell Signaling Technology). Cell lysates (300 μg) were incubated with 1 ?g of PPAR Ab (sc-7273) at 4°C overnight and precipitated with protein G agarose beads (Santa Cruz) at 4°C for 2 h. Immunoprecipitated proteins were separated by SDS-PAGE and transferred onto a PVDF membrane. Membranes were then sequentially incubated with primary ubiquitination Ab (SC-8017) and secondary Abs. Bands were visualized by using an ECL system. In addition, the below part should be added to the Discussion section afer the third paragraph: 'Te peroxisome proliferator-activated receptor-? (PPAR-γ) is a member of the nuclear receptor superfamily of ligand-dependent transcription factors which regulate adipocyte diferentiation, glucose homeostasis, and macrophage activation [27]. PPAR-γ ubiquitination and degradation have been found in adipocyte, and proteasome inhibitors inhibited the downregulation of PPAR-γ [28]. Proinfammation cytokine was also found to induce PPAR-γ degradation [29]. Herein, we found a novel mechanism such that PIO enhances PPAR-γ binding activity though inhibiting its ubiquitination and degradation, which may be important for TZDs clinical use.