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. 2018 Nov 2;8:16247. doi: 10.1038/s41598-018-34548-8

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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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Activation of Syk is required for PMA-induced Thy-1 up-regulation. (A) PMA (20 ng/mL) time-dependently increased Syk phosphorylation in HUVECs. n = 3. Pre-treatment of HUVECs with Syk inhibitors, Bay 61-3606 (1 μM) or piceatannol (10 μM), abolished the PMA-induced Syk activation (B), Thy-1 up-regulation (C) and migration inhibition (D). In (B), values shown in parentheses represent the quantified results adjusted with G3PDH and expressed as ratio over control. In (C and D), n = 3. (E) Pre-treatment of HUVECs with Röttlerin (5 μM) abolished the PMA-induced increases in the levels of p-Syk protein. n = 3. The gels have been run in the same experimental conditions and the cropped blots were shown. The entire gel pictures of 3A (p-Syk), 3B (p-Syk), 3C (Thy-1), and 3E (p-Syk) were shown in the Supplemental Fig. S3. *p < 0.05. Con, control; RÖ, Röttlerin.