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. 2018 May 8;8:7262. doi: 10.1038/s41598-018-25435-3

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© The Author(s) 2018

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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Full length perlecan and Domain IV-3 strongly dephosphorylate focal adhesion kinase (FAK) and alter several downstream signaling components. (A) C4-2 cells were cultured on several substrates (Set 1: Control BSA/digest buffer, set 2: Domain IV-3 alone, set 3: Domain IV-3 + MMP-7, set 4: perlecan + MMP-7, and set 5: perlecan alone) for 24 hours and probed for phosphorylated FAK (p-FAK), total FAK, p-AKT, FoxM1, p-p38, and GAPDH. Unpaired student t-tests between sets 2 and 3 were performed for densitometry quantified values of p-FAK/FAK, p-AKT/AKT, FoxM1/GAPDH, and p-p38/GAPDH. (B) A 12, 24 and 48-hour time course of C4-2 cells cultured on Domain IV-3 incubated either alone (−) or with MMP-7 (+) and probed for signaling components that were quantified by densitometry. An unpaired student’s t-test measured any significant difference between cells on Domain IV-3 or Domain IV-3 pre-cleaved with MMP-7 at each time point. p-values: * < 0.05, ** < 0.01, *** < 0.001. Expanded view of blots included in composite figure included in supplemental data file.