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. 2025 Aug 13;20:126. doi: 10.1186/s13020-025-01146-6

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© The Author(s) 2025

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 6 — Emodin directly targets GSK-3β to accelerate PD-L1 degradation. A, B GSK-3β protein expression compared with that of GAPDH in tumor tissues, H₂₂, Huh7, and LM3 cells after emodin treatment. C Exposure of H₂₂, Huh7, and LM3 cells with GSK-3β inhibition (GSK-3β^IB) to emodin. Western blot analysis was conducted to measure the expression levels of GSK-3β and PD-L1. D Overexpressing GSK-3β (GSK-3β^OE) enhanced the inhibitory effects of emodin on PD-L1 protein expression in H₂₂, Huh7, and LM3 cells. E Fluorescence images of LM3 cells that were stained with anti-GSK-3β (green), anti-PD-L1 (red), and DAPI (blue) (200 ×). The data are from three independent experiments (mean ± SD, *P < 0.05, **P < 0.01 vs. controls. ^#P < 0.05 vs. emodin group)