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. 2020 Jul 31;10:12912. doi: 10.1038/s41598-020-69396-y

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© The Author(s) 2020

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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Activity of HF3 upon PDGFR and PDGF. (A) HF3 cleaves PDGFR (alpha and beta forms) and PDGF in vitro. PDGFR-α (recombinant mouse PDGFR-α-Fc chimera), PDGFR-β (recombinant mouse PDGFR-β-Fc chimera) and PDGF were incubated with HF3, as described in “Materials and methods”, and submitted SDS-PAGE. White rectangles indicate proteins bands identified by mass spectrometry. Letters A and B indicate the subunits of the disulfidelinked PDGF heterodimer. Arrows indicate cleavage products generated by HF3. Proteins were stained with silver. (B) Degradation of PDGFR-α and PDGFR-β in the mouse skin injected with HF3, as shown by Western blot analysis. Protein samples (30 μg) from control skin (C) or skin injected with HF3 (H), and PDGFR-α (recombinant mouse PDGFR-α-Fc chimera) and PDGFR-β (recombinant mouse PDGFR-β-Fc chimera) (10 ng) were immunostained with anti-PDGFR-α and anti-PDGFR-β antibodies. Full-length images of Western blots and SDS-PAGE profiles of mouse proteins from control and hemorrhagic skins in comparison with PDGFRα and PDGFRβ are shown in Supplementary Figure S3.