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. 2017 Nov 8;7:15101. doi: 10.1038/s41598-017-15415-4

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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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Characterization of HAI-2’s KDs in inhibiting matriptase activation and prostate cancer cell motility. (A) Schematic structures of wild-type HAI-2 and its variant mutants with domain deletions or active site mutations. (B) N2 cells were stably transfected with the plasmids encoding the wild type and mutants of HAI-2. Western blot revealed the levels of HAI-2 protein, total matriptase and activated matriptase using anti-c-Myc, M32 and M69 mAbs, respectively. β-actin was shown as control. (C/D) Examination of the effects of HAI-2 mutant proteins on N2 cell invasion (C) and migration (D) using transwell assays. N2 cells which stably expressed HAI-2 mutant proteins were seeded at a density of 3 × 10⁵ cells per upper chamber of Boyden chambers and incubated for 16 hours. Data were statistically calculated from three independent experiments and shown as mean ± SD. (*p < 0.5; **p < 0.01; ***p < 0.001, one-way ANOVA).