Corrigendum to "Pioglitazone Attenuates Drug-Eluting Stent-Induced Proinflammatory State in Patients by Blocking Ubiquitination of PPAR".

[This corrects the article DOI: 10.1155/2016/7407153.].

In the article titled “Pioglitazone Attenuates Drug-Eluting Stent-Induced Proinflammatory 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. The 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 buffer (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). After 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. The 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 modified RIPA buffer (Cell Signaling Technology). Cell lysates (300 μg) were incubated with 1 μg 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 after the third paragraph:

“The peroxisome proliferator-activated receptor-γ (PPAR-γ) is a member of the nuclear receptor superfamily of ligand-dependent transcription factors which regulate adipocyte differentiation, 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]. Proinflammation 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.”

Moreover, the references below should be included in the References list:

[24] T. Chen, X. Jin, B. H. Crawford et al., “Cardioprotection from oxidative stress in the newborn heart by activation of PPARg is mediated by catalase,” Free Radical Biology & Medicine, vol. 53, no. 2, pp. 208–215, 2012.

[25] C. Xie, T. Yagai, Y. Luo et al., “Activation of intestinal hypoxia-inducible factor 2α during obesity contributes to hepatic steatosis,” Nature Medicine, vol. 23, no. 11, pp. 1298–1308, 2017.

[26] Q. Zhao, D. Zhou, H. You et al., “IFN-γ aggravates neointimal hyperplasia by inducing endoplasmic reticulum stress and apoptosis in macrophages by promoting ubiquitin-dependent liver X receptor-α degradation,” The FASEB Journal, vol. 31, no. 12, pp. 5321-5331, 2017.

[27] L. Fajas, D. Auboeuf, E. Raspé et al., “The organization, promoter analysis, and expression of the human PPARgamma gene,” The Journal of Biological Chemistry, vol. 272, no. 30, pp.18779–89, 1997.

[28] S. Hauser, G. Adelmant, P. Sarraf, H. M. Wright, E. Mueller, B. M. Spiegelman, “Degradation of the peroxisome proliferator-activated receptor gamma is linked to ligand-dependent activation,” The Journal of Biological Chemistry, vol. 275, no. 24, pp. 18527–18533, 2000.

[29] K. J. Waite, Z. E. Floyd, P. Arbour-Reily, J. M. Stephens, “Interferon-gamma-induced regulation of peroxisome proliferator-activated receptor gamma and STATs in adipocytes,” The Journal of Biological Chemistry, vol. 276, no. 10, pp. 7062–7068, 2001.