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. 2023 Jul 20;14(7):452. doi: 10.1038/s41419-023-05976-w

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© The Author(s) 2023

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. 5 — A RNA pull-down and mass spectrometry assays were used to identify the proteins interacting with circSLC4A7. B The interaction between circSLC4A7 and HSP90 was determined by RIP assay. C Colocalization of circSLC4A7 and HSP90 detected by FISH and IF. Nuclei were stained with DAPI. D Expression of HSP90 was measured in AGS-shcircSLC4A7/AGS-Vector cells and MGC803circSLC4A7/MGC803-Vector cells by Western blot assay. E Relative expression level of circSLC4A7 was measured in AGS, BGC823, MGC803, and SGC7901 cells transfected with siNC or siHSP90 by qRT-PCR. F Expression of HSP90 was measured in GES1 and 4 gastric cancer cell lines (the MGC803, AGS, BGC823, and SGC7901 cell lines). **P < 0.01 based on the Student t test. All results are from three independent experiments. Data are represented as mean ± SD. At least one representative image was captured.