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. 2019 Sep 13;9:13231. doi: 10.1038/s41598-019-49626-8

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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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Proteolytic activity of the two rs7020782 PAPP-A variants towards radiolabelled IGFBP-2, IGFBP-4, and IGFBP-5. Supernatants from HEK293T cells transfected with the two PAPP-A rs7020782 variants (serine: red, tyrosine: blue) were incubated with IGFBP-2 (lower panel), IGFBP-4 (upper panel), or IGFBP-5 (lower panel). Cleavage reactions were stopped at different time-points and subsequently, intact and cleaved IGFBPs were quantified (insert). IGFBP-4 cleavage in percent versus time (linear regression) as well as cleavage rates (mean ± SEM) for all three binding proteins are shown. Results showing IGFBP-4 proteolysis are derived from four independent proteinase assays and with supernatants from four independent transfections. Results showing IGFBP-2 and IGFBP-5 proteolysis are derived from three independents assays. A significantly lower IGFBP-4 cleavage rate was observed for the serine variant of the rs7020782 SNP compared to the tyrosine variant (p-value < 0.001). Reduced IGFBP-2 (p-value = 0.60) and IGFBP-5 (p-value = 0.78) cleavage rates that was not significant were observed for the serine variant compared to the tyrosine variant.