Targeting SIRT7 with Oroxylin A Unlocks a Dual Program of Cellular Senescence and NK Cell-Mediated Clearance to Combat Liver Fibrosis
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Targeting SIRT7 with Oroxylin A Unlocks a Dual Program of Cellular Senescence and NK Cell-Mediated Clearance to Combat Liver Fibrosis


Liver fibrosis, a progressive scarring of the liver tissue, represents a major global health burden with limited treatment options. It is primarily driven by the activation of hepatic stellate cells (HSCs), which proliferate and secrete excess extracellular matrix proteins. Effective strategies to inactivate or eliminate these activated HSCs are crucial for reversing fibrosis. However, current therapies often lack precision and efficiency.

Recently, the team of Shao Jiangjuan/Zheng Shizhong/Cheng Haibo from Nanjing University of Chinese Medicine revealed a dual regulatory mechanism: inhibition of SIRT7 by Oroxylin A (OA) reprograms the fate of HSCs through PRMT5 succinylation-driven senescence and ecto-calreticulin (ecto-CRT)-dependent NK cell immune clearance. The study achieved a significant reduction in fibrosis markers in experimental models and highlighted the critical role of inhibiting the SIRT7 protein.

“Targeting SIRT7 unlocks a dual cytotoxic and immunogenic program against activated HSCs,” said lead author Jiangjuan Shao. “Natural compounds like OA offer multi-targeted therapeutic potential. Our findings reveal an efficient strategy for reprogramming HSCs fate and provide a promising candidate for anti-fibrotic therapy.”

Professor Shao is from the Jiangsu Key Laboratory for Pharmacology and Safety Research of Chinese Materia Media at Nanjing University of Chinese Medicine.

Dual Mechanism for HSCs Fate Reprogramming
OA, a bioactive compound derived from the traditional Chinese herb Scutellaria baicalensis, was identified to directly bind and inhibit SIRT7, a protein highly expressed in activated HSCs. This interaction initiates a dual anti-fibrotic program: First, OA-induced SIRT7 inhibition promotes succinylation and proteasomal degradation of PRMT5, activating the cGAS-STING pathway and triggering irreversible HSCs senescence. Second, SIRT7 blockade—independent of its desuccinylase activity—leads to externalization of calreticulin (ecto-CRT) on HSCs. This “eat-me” signal facilitates recognition and elimination by NK cells via the NKp46 receptor.

Selective and Recyclable Anti-Fibrotic Effects

The researchers found that OA exhibits high selectivity for activated HSCs with good biocompatibility. The compound also demonstrated reusability and stability in its anti-fibrotic effects. In vivo experiments showed remarkable regression of liver fibrosis, supporting its therapeutic potential. The selectivity stems from specific SIRT7 targeting and subsequent immune-dependent clearance, minimizing off-target effects.

“Combatting fibrosis requires integrated manipulation of both cellular aging and immune recognition,” Professor Shao said. “The complex crosstalk between HSCs and the immune microenvironment underscores the need for smart targeting strategies. Our approach provides a synergistic and sustainable solution for fibrosis treatment.

The complete study is accessible via DOI:10.34133/research.0808
Title: Dual Roles of SIRT7 Inhibition by Oroxylin A Reprogram HSCs Fate: PRMT5 Succinylation-Driven Senescence and Ecto-Calreticulin-Dependent NK Cell Immune Clearance in Liver Fibrosis
Authors: JUNRUI WANG, HAOYUAN TIAN, YUANYUAN GAO, XINRAN QIU, ZHENGYANG BAO, DANLI ZHAO, FENG ZHANG, ZILI ZHANG, FEIXIA WANG, SHIZHONG ZHENG, HAIBO CHENG, AND JIANGJUAN SHAO
Journal: RESEARCH,7 Aug 2025,Vol 8,Article ID: 0808
DOI: 10.34133/research.0808
Fichiers joints
  • Fig. 1. OA activates cGAS-STING pathway by restraining PRMT5 in LX2 cells. LX2 cells were treated with the suggested concentration of OA or PRMT5 plasmid for 24 h. (A) Bioinformatics analysis based on the GSE137720 dataset. Visualize genes’ average expression and the percentage of cells expressing in different cell types (dot plot). (B) Primary mouse hepatic stellate cells were stimulated with a combination of 5 ng/ml TGFβ and 10 ng/ml PDGF-BB for 48 h and cultured for a further 7 days for full activation. Different concentrations of OA were added to intervene for 24 h. The protein expression level of PRMT5 was measured by WB. (C and D) WB and RT-PCR were employed to analyze the expression of the cGAS-STING pathway. (E and I) The levels of cGAS were detected by immunofluorescence. Scale bars are 1,000 μm. The levels of p16 and p21 were detected by immunofluorescence. Scale bars are 100 μm. (F) The IFN-β levels were gauged by the ELISA kit. (G) RT-PCR was applied to measure the mRNA level of IL-1β. (H) WB was used to measure the protein level of IL-6. (J) The percentage of senescent cells was determined with the SA-β-Gal Kit. Scale bars are 200 μm. The data of the graph are displayed as mean ± SD (n = 3). Levels of statistical significance are indicated as **P < 0.01, ***P < 0.001 vs. the OA group. ##P < 0.01, ###P < 0.001 vs. the control group.
  • Fig. 2. OA inhibits PRMT5-mediated dimethylation of cGAS in LX2 cells. (A) Protein levels of cGAS-STING were measured by WB. (B) The IFN-β level was gauged by the ELISA kit. (C) WB was utilized to measure the protein levels of IL-6 and IL-1β. (D) IP analysis showed the interaction between cGAS and PRMT5. (E) The methylation level of HA-tagged cGAS was gauged by IP analysis. (F) GPS-MSP was used to predict symmetrical di-methylation sites of cGAS. (G) The methylation level of HA-tagged cGAS was shown by IP analysis. (H) The cGAMP level was detected by the ELISA kit. Levels of statistical significance are indicated as ns, not significant vs. OA group. ##P < 0.01 vs. control group.
  • Fig. 3. OA promotes PRMT5 protein degrading by inhibiting SIRT7 from desuccinylating PRMT5 in LX cells. (A) Succinylation level was tested by WB. (B) Succinylation level of PRMT5 was tested by IP analysis treated with OA or DMSO. The succinylation level of PRMT5 was shown by IP analysis. (C) Bioinformatics analysis based on the GSE137720 dataset. Visualize genes’ average expression and the percentage of cells expressing in different cell types (dot plot). (D) Primary mouse hepatic stellate cells were stimulated with a combination of 5 ng/ml TGFβ and 10 ng/ml PDGF-BB for 48 h and cultured for a further 7 days for full activation. Different concentrations of OA were added to intervene for 24 h. The protein expression level of SIRT7 was measured by WB. (E) SIRT7 mRNA expression was gauged by RT-PCR. (F) Protein level of PRMT5 was measured by WB. (G) Protein levels of the cGAS-STING pathway were measured by WB. (H) IP analysis of the interaction between HA-SIRFT7 and Flag-PRMT5. (I) The succinylation level of PRMT5 or PRMT5 mutants was shown by IP analysis. (J) The methylation levels of HA-tagged cGAS were gauged by IP analysis. Levels of statistical significance are indicated as **P < 0.01, ***P < 0.001 vs. OA group. ###P < 0.001; ns, not significant vs. control group.
  • Fig. 4. The OA–SIRT7 complex shows positive stability. (A) OA–SIRT7 complexes at various time breaks respectively are captured in panels (a) to (e). Panel (f) is the representative structure generated by cluster analysis of 200 snapshots. (B) RMSD fluctuation of OA–SIRT7 complexes. (C) Radius of gyration fluctuation of OA–SIRT7 complexes. (D) Hydrogen bond simulation. The time scale is represented by the horizontal axis, while the quantity of hydrous bonds is indicated by the vertical axis. Different data regarding density, pressure, energy, and other variables during the simulation process. (E) A compilation of data about energy, pressure, density, and further simulation-related changes. (F) After incubating LX2 cells with or without OA (40 μM) for 2 h, the cells were removed and exposed to the CETSA test.
  • Fig. 5. Gln299 and Asp305 are essential in OA-mediated SIRT7 degradation. (A) The expression of SIRT7 protein was gauged by WB. (B) The expression of SIRT7 protein was detected by WB. (C) Molecular docking analysis of the potential binding between OA and SIRT7. (D) Comparison of exogenous SIRT7-WT/SIRT7-R73A/SIRT7-Q299A/ SIRT7-D305A expressions in LX2 cells treated with OA (0, 20, 30, and 40 μM) for 24 h. Levels of statistical significance are indicated as ***P < 0.001; ns, not significant vs. the OA group.
  • Fig. 6. Increasing SIRT7 expression in vivo will diminish the antifibrosis effect of OA. (A) The liver fibrosis stage was assessed by Metavir criteria. For histopathological study, human liver samples (F0/1, 3; F2, 3; F3, 4; F4, 5) were stained with H&E Masson and IHC for SIRT7. Representative images were shown. Scale bar: 50 μm. n = 3 per group. (B) The livers were taken out from the animals after they were killed and photographed so that the shape of the liver could be seen. (C and D) Items of liver fiber (HA and LN) in serum and indexes of liver injury (ALT and ALP) were detected. (E) Determine the ratio of liver to body weight. n = 6 per group. (F) The expression of α-SMA protein in liver tissues was detected by WB. **P < 0.01; ***P < 0.001, compared with the control group; #P < 0.05, ##P < 0.01, ###P < 0.001, compared with the CCl4 group; &&P < 0.01, &&&P < 0.001, compared with the CCl4 +OA+vector group).
  • Fig. 7. SIRT7 blockade by OA promotes CRT externalization, thus increasing NK cell recognizing and killing HSCs. (A) Bioinformatics analysis based on the GSE84044 dataset. Gene set enrichment analysis (GSEA) was used to further reveal the expression of differential genes in the progression of hepatic fibrosis. (B) Bioinformatics analysis based on the GSE136103 dataset. Statistical enrichment of differentially expressed genes in KEGG pathways. (C) The cytotoxicity was calculated when the target-to-effector cell ratio is 1:2. (D) Volcano map of significant differentially expressed genes. (E) WB analyzed the expression of ERS-associated proteins in HSCs. The data are shown as mean ± SD (n = 3). (F) The level of ecto-CRT was detected by immunofluorescence and quantified with ImageJ software. Representative photographs were shown. Scale bars are 20 μm. (G) The level of ecto-CRT was detected by immunofluorescence. (H) The cytotoxicity was calculated when the target-to-effector cell ratio is 1:2. The data are shown as mean ± SD (n = 3). **P < 0.01, ***P < 0.001 vs. the OA group. ##P < 0.01, ###P < 0.001 vs. the control group.
  • Fig. 8. SIRT7 blockade by OA promotes CRT exposure in HSCs, independent of the desuccinylase activity of SIRT7. (A) Immunofluorescence screening was employed to detect the protein expression and colocalization of α-SMA and p16. The scale bar is 50 μm. (B) Utilizing immunofluorescence screening, the expression of Nkp46 and α-SMA proteins was identified. Antibodies against NKp46 were utilized in immunofluorescence staining of liver slices in order to precisely label NK cells. The HSCs were selectively stained with an antibody against α-SMA. The scale bar is 100 μm. (C) The level of ecto-CRT was detected by immunofluorescence and quantified with ImageJ software. Representative photographs were shown. Scale bars are 100 μm. (D) The level of ecto-CRT was detected by immunofluorescence and quantified with ImageJ software. Representative photographs were shown. Scale bars are 100 μm. (E) WB analyzed the expression of ERS-associated proteins in HSCs. (F) The cytotoxicity was calculated when the target-to-effector cell ratio is 1:2. The data are shown as mean ± SD (n = 3). ns, not significant, $P < 0.05, $$P < 0.01 vs. the control group; *P < 0.05, **P < 0.01, compared with the OA group; ###P < 0.001, compared with the CCl4+vector group; &&&P < 0.001, compared with the CCl4+OA+vector group).
  • Fig. 9. Mechanism diagram of the dual role of SIRT7 in OA inducing HSC senescence and promoting NK cell killing.
Regions: Asia, China
Keywords: Health, Medical, People in health research

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