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. 2021 Jul 22;12:4452. doi: 10.1038/s41467-021-24736-y

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© The Author(s) 2021

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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Fig. 2 — a Cys66 is identified as the SNO-site of GNAI2 according to the liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis. b HUVECs were ectopically expressed with GNAI2-WT and GNAI2-C66A, followed by exposure to HG and oxLDL for 24 h. GNAI2-C66A abolishes S-nitrosylation of GNAI2 induced by HG and oxLDL as determined by a biotin-switch assay. n = 3 distinct samples for each group. c HAECs were transfected with pcDNA, GNAI2-WT, and GNAI2-C66A, followed by stimulated with HG and oxLDL for 24 h. GNAI2-C66A inhibits the mRNA expressions of adhesion molecules (ICAM1, VCAM1, SELE, and SELP) and chemokines (CXCL4, CXCL8, CCL2, and CCL5) induced by HG and oxLDL as determined by qPCR. n = 3 distinct samples for each group. d GNAI2-C66A prevents the attachment of THP-1 cells to HAECs in HG and oxLDL condition. Scale bar = 100 μm. n = 3 distinct samples for each group. Data are represented as the Mean ± SEM. One-way ANOVA followed by Tukey’s test for post-hoc comparisons was used. Source data are provided as a Source Data file.