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. 2019 Oct 31;9:15771. doi: 10.1038/s41598-019-52364-6

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© The Author(s) 2019

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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The VEGFA–calpain-6 interaction is necessary for calpain-6-mediated VEGF protein secretion. (a) Schematic diagram of the Myc-tagged full-length calpain-6 and deletion mutants, showing the deletions and domains I, II, III, and T. (b) Calpain-6 domain III is necessary for calpain-6-mediated VEGF secretion. The indicated full-length and mutant calpain-6 constructs were transiently transfected into HEK293 cells, and then the VEGF protein secreted into the conditioned culture medium was assayed by ELISA. The results are expressed as the mean VEGF produced in the conditioned medium ± SD. P < 0.001 or P < 0.05 compared with the control vector.