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. 2018 Jul 24;8:11380. doi: 10.1038/s41598-018-29406-6

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© The Author(s) 2018

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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Radioligand binding assays and functional assays showed that SAA and SAC can bind and antagonize both P2Y₁ and P2Y₁₂ receptors, while SAB can bind and antagonize only the P2Y₁₂ receptor. (a) Displacement curves of SAA, SAB and SAC against [³H]2MeSADP binding to the P2Y₁₂ receptor. (b) Functional antagonism by SAA of 2MeSADP-induced inhibition of foskolin-stimulated cAMP accumulation in U2OS cells expressing the P2Y₁₂ receptor. (c) Schild plots of the antagonism of SAA, SAB and SAC at the P2Y₁₂ receptors. (d) Displacement curves of SAA, SAB and SAC against [³H]2MeSADP binding to the P2Y₁ receptor. (e) 2MeSADPinduced IP-1 accumulation in U2OS cells expressing the P2Y₁ receptor (compared to MRS2500). (f) Schild plots of antagonism by SAA and SAC at the P2Y₁ receptor. Results are expressed as mean ± SEM. The K_i values from binding experiments and K_B values from Schild analyses of functional antagonism by SAA, SAB and SAC are listed in the text and are from at least three independent experiments. MRS, MRS2500; SAR, SAR216471.