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. 2018 Apr 20;8:6331. doi: 10.1038/s41598-018-24576-9

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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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KLK12 exerts proteolytic activity against fibronectin isoforms. (A) Proteolysis of matrix proteins by KLK12, analyzed with SDS-PAGE and Coomassie blue staining (E:S molar ratio: 1:5, 4 h at 37 °C). (B) Characterization of FN proteolysis by KLK12, analyzed as in A. Left panel: Dose-dependent proteolysis of FN by KLK12 with an E:S molar ratio ranging from 1:5 to 1:1000; 4 h at 37 °C. Right panel: Time-dependent proteolysis of FN by KLK12, from 1 min to 5 h at 37 °C (E:S molar ratio: 1:50). (C) In control experiments, KLK12 was incubated with either E64 (100 µM), PMSF (0.5 mM) or EDTA (0.5 mM) and with FN. (D) Dose-dependent proteolysis of cellular FN isoforms (cFN and FN-EDB) by KLK12. E:S molar ratio: from 1:5 to 1:50; 4 h at 37 °C. The band corresponding to recombinant human KLK12 is indicated by an arrowhead when visible, and bands corresponding to proteolytic products are indicated by arrows.