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. 2019 Oct 25;5:141. doi: 10.1038/s41420-019-0221-3

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 5 — a mRNA expression of Cx43 and panx1 in the presence (+) and absence (−) of Smad3 siRNA (100 nM) incubation and subsequent TGF-β1 (5 ng/ml) treatment by qPCR. The results shown are based on three independent experiments (n = 3). *p < 0.05. b mRNA expression of Cx43 and panx1 in the presence (+) and absence (−) of SIS3 (5 μM) incubation and subsequent TGF-β1 (5 ng/ml) treatment by qPCR. The results shown are based on three independent experiments (n = 3). *p < 0.05. c Representative Western blots showing protein expressions of Cx43 and panx1 in the presence (+) and absence (−) of Smad3 siRNA incubation and subsequent TGF-β1 treatment. The results shown are based on three independent experiments (n = 3). d Quantitative analysis of proteins in c The results were normalized to β‐actin as western blot loading control. Data are presented as the mean ± s.d.; n = 3, *p < 0.05 by t-test. e Representative Western blots showing protein expressions of Cx43 and panx1 in the presence (+) and absence (−) of SIS3 incubation and subsequent TGF-β1 treatment. The results shown are based on three independent experiments (n = 3). f Quantitative analysis of proteins in e. The results were normalized to β-actin as western blot loading control. Data are presented as the mean ± s.d.; n = 3, *p < 0.05 by t-test. g Representative IF staining by CLSM showing enhanced translocation of Smad3 into nuclei in osteocytes (MLO-Y4 cell line) after treatment of TGF-β1 (5 ng/ml) for 6 h. The results shown are based on three independent experiments (n = 3). h Bioinformatics showing the predicted binding sites of nuclear translocated-Smad3 on the promoter of Cx43 gene (Gja1, GenBank name) and Panx1 gene. i ChIP assay was performed in osteocytes (MLO-Y4 cell line) in the presence or absence of TGF-β1 to confirm the binding sites of Smad3 at the promoter region of Gja1 and Panx1 genes. Histogram indicated the relative levels of PCR products at the five binding sites on the proximal promoter of Gja1 and panx1 induced by TGF-β1. The assay was repeated at three times (n = 3). All data are shown as the mean ± s.d.; *p < 0.05 by t-test