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. 2019 Dec 12;9:19009. doi: 10.1038/s41598-019-55391-5

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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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Platelet inhibition (by PGI₂ or CTAD) induces shifts of protein spots to a more acidic pI. Significantly changed protein species, belonging to (A) VASP, (B) LASP1, (C) ZYX and (D) SKAP2 are depicted along their pI ranges. Values of each protein spots are given as relative fold changes between treated gel-filtered platelets (PGI₂ ●, CTAD ○) and untreated control (dashed line y = 1) with their means and 95% confidence interval (n = 6 in each subgroup). Statistical significance was set at p < 0.05 and was determined by post-hoc testing between subgroups (PGI₂, CTAD) and untreated controls. PGI₂- and CTAD-dependent protein profiles of VASP were also validated by flow cytometry (Supplementary Fig. 11). PGI₂ - prostacyclin, CTAD - citrate, theophylline, adenosine, dipyridamole, pI - isoelectric point.