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. 2020 May 13;22:113. doi: 10.1186/s13075-020-02207-x

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© The Author(s) 2020

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 3 — Impact of recombinant human proteoglycan-4 (rhPRG4) treatment on TGF-β induced stress fiber formation, vinculin expression, and formation of focal adhesions (FAs) in murine fibroblasts (NIH3T3) and its relationship to cell migration. Stress fiber formation was probed using an anti-alpha smooth muscle actin (α-SMA) antibody (green) and a blinded investigator evaluated % stress fiber-positive fibroblasts. Vinculin (a marker of FAs) expression was probed using an anti-vinculin antibody (green) and cells were counterstained using rhodamine-labeled phalloidin (cytoskeleton label; red). NIH3T3 Fibroblast migration was performed using a scratch assay and the wound closure percentage was determined. *p < 0.001; **p < 0.01; ***p < 0.05; n.s., non-significant. Scale in a and f = 20 μm; a Representative images showing TGF-β induced stress fiber formation and vinculin staining (white arrows) in NIH3T3 fibroblasts. b rhPRG4 reduced stress fiber formation in NIH3T3 fibroblasts. c rhPRG4 reduced mean NIH3T3 fibroblast spread area. d rhPRG4 reduced the number of FAs in NIH3T3 fibroblasts. e rhPRG4 reduced the mean size of FAs in NIH3T3 fibroblasts. f Representative images showing NIH3T3 migration in response to TGF-β ± rhPRG4. g rhPRG4 reduced NIH3T3 migration