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. 2017 Apr 26;7:1210. doi: 10.1038/s41598-017-01264-8

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© The Author(s) 2017

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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Influence of sHA3 on the TGF-β1-mediated TβR-I and Smad2 phosphorylation. Hs27 fibroblast cells were stimulated with 10 ng/ml TGF-β1 (0.4 nM) alone or pre-formed complexes of TGF-β1 and 100 µg/ml sHA3 (130 µM D.U.) for the indicated time points. Cells were lysed and applied to Western Blot analyses using specific anti-phospho-Smad2, anti-phospho-TβR-I and anti-GAPDH antibodies. Membranes were reblotted afterwards with anti-TβR-I antibody. For every time point a representative blot is shown (A). The time course of TGF-β1-mediated phosphorylation in the presence or absence of sHA3 is plotted for Smad2 phosphorylation (B) and TβR-I phosphorylation relative to unstimulated cells (C). Two-way ANOVA: ***p < 0.001 vs. TGF-β1 only.