Fluvastatin enhances the sensitivity of clear cell renal cell carcinoma to sunitinib by inhibiting PHF8

Wang Ziqian; Xie Xiaodu; Wang Ze; Tang Peng; Zhang Junying; Xu Jing; Zheng Chongliang; Xiao Haiyang; Jin Junhao; Wang Luofu; Jiang Jun; Lan Weihua; Liu Qiuli

doi:10.16016/j.2097-0927.202606076

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Fluvastatin enhances the sensitivity of clear cell renal cell carcinoma to sunitinib by inhibiting PHF8

Basic Medicine | 更新时间：2026-10-19

- Fluvastatin enhances the sensitivity of clear cell renal cell carcinoma to sunitinib by inhibiting PHF8
- Journal of Army Medical University Vol. 48, Issue 19, Pages: 2719-2732(2026)
- 作者机构：
  
  1.陆军军医大学（第三军医大学）大坪医院泌尿外科，重庆
  2.联勤保障部队第988医院泌尿外科，河南郑州
  3.重庆医药高等专科学校，重庆
  4.浙江大学医学院附属第二医院泌尿外科，浙江杭州
- 作者简介：
  
  Lan Weihua，E-mail： doclan@yeah.net
  Liu Qiuli，E-mail： liuqiuli900827@163.com
- 基金信息：
  
  the General Program of National Natural Science Foundation of China(82473441);the Project of High-Level Young and Middle-Aged Medical Talents of Chongqing(YXGD202519)
- DOI：10.16016/j.2097-0927.202606076
  CLC： R345;R737.11;R979.19
- Received：18 June 2026，
  
  Revised：2026-08-28，
  
  Accepted：31 August 2026，
  
  Published：15 October 2026
- 稿件说明：
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王子乾，解晓都，汪泽，等.氟伐他汀通过抑制PHF8增强肾透明细胞癌对舒尼替尼敏感性［J］.陆军军医大学学报，2026，48（19）：2719-2732.DOI：10.16016/j.2097-0927.202606076.

Wang Z Q，Xie X D，Wang Z，et al.Fluvastatin enhances the sensitivity of clear cell renal cell carcinoma to sunitinib by inhibiting PHF8［J］.J Army Med Univ，2026，48（19）：2719-2732.DOI：10.16016/j.2097-0927.202606076.
王子乾，解晓都，汪泽，等.氟伐他汀通过抑制PHF8增强肾透明细胞癌对舒尼替尼敏感性［J］.陆军军医大学学报，2026，48（19）：2719-2732.DOI：10.16016/j.2097-0927.202606076. DOI：

Wang Z Q，Xie X D，Wang Z，et al.Fluvastatin enhances the sensitivity of clear cell renal cell carcinoma to sunitinib by inhibiting PHF8［J］.J Army Med Univ，2026，48（19）：2719-2732.DOI：10.16016/j.2097-0927.202606076. DOI：

摘要

目的

舒尼替尼耐药是影响肾透明细胞癌（clear cell renal cell carcinoma，ccRCC）靶向治疗疗效的重要因素，其分子机制及有效干预策略尚未完全明确。本研究旨在探讨组蛋白去甲基化酶PHF8在ccRCC舒尼替尼耐药中的作用，并评价氟伐他汀靶向PHF8、增强耐药ccRCC对舒尼替尼敏感性的效果。

方法

构建舒尼替尼耐药细胞株（786-O-R）及患者来源异种移植瘤（patient-derived xenograft， PDX）耐药模型，采用Western blotting、免疫组织化学染色检测模型中PHF8的表达水平。构建PHF8稳定过表达的786-O和A498细胞株及细胞源性异种移植瘤（cell line-derived xenograft， CDX）模型，通过体外增殖测定、体内肿瘤体积、Ki-67及CD31免疫组织化学染色，探究PHF8对舒尼替尼治疗反应性的影响。转录组测序及Western blotting、免疫组织化学染色分析PHF8调控舒尼替尼耐药的具体分子机制。分析陆军军医大学大坪医院泌尿外科46例接受舒尼替尼治疗的ccRCC患者肿瘤病理标本，评估PHF8表达与病理分级及无进展生存期（progression-free survival， PFS）的相关性。基于FDA批准的小分子药物库进行虚拟筛选，并结合RT-qPCR、放线菌酮追踪、MG132和氯喹补救、细胞热迁移实验（cellular thermal shift assay，CETSA）、表面等离子共振（surface plasmon resonance，SPR）及分子对接，分析氟伐他汀调控PHF8蛋白稳定性的作用。采用CCK-8及体内实验评价氟伐他汀联合舒尼替尼对耐药细胞的增敏作用。

结果

构建舒尼替尼耐药细胞及PDX模型。与敏感对照组相比，PHF8蛋白在786-O-R细胞及耐药PDX模型（Su-P8）中表达均显著上调，提示PHF8可能参与ccRCC舒尼替尼耐药。进一步功能实验显示，

PHF8

过表达显著降低786-O（IC

：5.406

15.920 μmol/L）和A498（IC

：5.186

16.300 μmol/L）细胞对舒尼替尼的敏感性；敲除

PHF8

后，耐药细胞对舒尼替尼的敏感性明显恢复（IC

：13.470

6.355 μmol/L）。体内实验进一步证实，舒尼替尼治疗后，

PHF8

过表达组的肿瘤体积（

0.000 1）、肿瘤质量（

=0.001 3）、Ki-67表达（

0.000 1）及CD31表达（

0.000 1）均显著高于对照组，表明PHF8可促进ccRCC对舒尼替尼的治疗抵抗。临床样本分析显示，PHF8高表达与ccRCC患者较高的病理分级显著相关（

=0.000 3），并与较短的靶向治疗PFS相关（

=0.04）。基于PHF8蛋白结构的虚拟筛选获得潜在小分子抑制剂氟伐他汀可抑制

PHF8蛋白表达并升高H3K9me1/2水平，同时显著缩短PHF8蛋白半衰期（

=0.000 7），且该作用可被蛋白酶体抑制剂MG132明显逆转，提示氟伐他汀促进PHF8蛋白酶体降解。CETSA显示，氟伐他汀可提高PHF8蛋白的热稳定性；SPR进一步证实氟伐他汀可直接与PHF8结合（K

=23.8 μmol/L），分子对接揭示了二者潜在的分子结合模式。氟伐他汀与舒尼替尼联合处理使786-O-R细胞的舒尼替尼IC

显著下降（IC

：17.460

4.601 μmol/L），细胞抑制作用显著强于舒尼替尼单药组（

0.000 1）；而敲除

PHF8

后，联合用药与单药处理之间差异无统计学意义，表明氟伐他汀对舒尼替尼的增敏作用具有PHF8依赖性。体内实验进一步显示，联合氟伐他汀可显著提高耐药PDX模型对舒尼替尼的治疗敏感性。

结论

PHF8是促进ccRCC舒尼替尼耐药的重要因子，其高表达与较高病理分级及较差预后相关。氟伐他汀可通过靶向PHF8并促进其蛋白降解，提高耐药ccRCC细胞对舒尼替尼的敏感性。

Abstract

Objective

Sunitinib resistance is an important factor affecting the efficacy of targeted therapy for clear cell renal cell carcinoma (ccRCC)

and its underlying molecular mechanisms and effective intervention strategies have not been fully elucidated. This study aims to investigate the role of histone demethylase PHF8 in sunitinib resistance and to evaluate the effect of fluvastatin in targeting PHF8 and enhancing the sensitivity to sunitinib in ccRCC.

Methods

A sunitinib-resistant ccRCC cell line (786-O-R) and a patient-derived xenograft (PDX) resistant model were established. The expression of PHF8 in these resistant models was validated with Western blotting and immunohistochemical staining. Then 786-O and A498 cell lines with stable

PHF8

overexpression and their corresponding cell line-derived xenograft (CDX) models were constructed. The regulatory effect of PHF8 on sunitinib responsiveness was evaluated through

in vitro

cell proliferation assay

in vivo

tumor volume monitoring

and immunohistochemical detection of Ki-67 and CD31 expression. Transcriptome sequencing

Western blotting

and immunohistochemical staining were performed to elucidate the molecular mechanisms by which PHF8 mediates sunitinib resistance. Tumor specimens from 46 ccRCC patient

s who received sunitinib treatment in Department of Urology of Daping Hospital were analyzed to evaluate the correlations of PHF8 expression with pathological grade and progression-free survival (PFS). An FDA-approved small-molecule drug library was used for virtual screening. RT-qPCR

cycloheximide chase assay

MG132/chloroquine rescue experiments

cellular thermal shift assay (CETSA)

surface plasmon resonance (SPR)

and molecular docking were conducted to verify the regulatory effect of fluvastatin on PHF8 protein stability. CCK-8 assay and

in vivo

animal experiments were performed to evaluate the synergistic sensitizing effect of fluvastatin combined with sunitinib on sunitinib-resistant ccRCC cells.

Results

Stable sunitinib-resistant cell lines and PDX models were successfully constructed. Compared with sunitinib-sensitive control counterparts

the protein expression of PHF8 was markedly upregulated in 786-O-R cells and resistant PDX tumors (Su-P8)

indicating that PHF8 may be involved in sunitinib resistance in ccRCC. Further functional experiments demonstrated that

PHF8

overexpression significantly reduced the sensitivity of 786-O (IC

: 5.406

15.920 μmol/L) and A498 cells (5.186

16.300 μmol/L) to sunitinib. Conversely

PHF8

knockout substantially restored the sensitivity of resistant cells to sunitinib (IC

: 13.470

6.355 μmol/L). Consistent with

in vitro

findings

in vivo

experiments showed that after sunitinib treatment

the

PHF8

-overexpression group exhibited significantly larger tumor volume (

0.000 1)

higher tumor weight (

=0.001 3)

and elevated Ki-67 and CD31 expression levels (both

0.000 1) compared with the control group

confirming that PHF8 drives sunitinib resistance in ccRCC. Clinical sample analysis revealed that high PH

F8 expression was significantly correlated with advanced pathological grade (

=0.000 3) and shorter PFS after targeted therapy (

=0.04). Virtual screening targeting PHF8 identified fluvastatin as a potential candidate inhibitor. Fluvastatin downregulated PHF8 expression

increased H3K9me1/2 level

and significantly shortened the half-life of PHF8 (

=0.000 7)

this effect could be significantly reversed by the proteasome inhibitor MG132

indicating that fluvastatin facilitates proteasome-dependent degradation of PHF8. CETSA results verified that fluvastatin enhanced the thermal stability of PHF8

and SPR analysis further confirmed the direct binding between fluvastatin and PHF8 (K

=23.8 μmol/L)

with molecular docking predicting their potential binding pattern. Combination treatment with fluvastatin and sunitinib reduced the IC

value of sunitinib in 786-O-R cells (from 17.460 to 4.601 μmol/L) and exerted a significantly stronger inhibitory effect on cell viability than sunitinib monotherapy (

0.000 1). Notably

no significant difference was observed between combination therapy and sunitinib monotherapy after

PHF8

knockout

demonstrating that the sunitinib-sensitizing effect of fluvastatin is PHF8-dependent. Moreover

in vivo

PDX model experiments further validated that fluvastatin supplementation effectively restored the sensitivity of resistant PDX models to sunitinib.

Conclusion

PHF8 is a critical driver of sunitinib resistance in ccRCC

and its high expression is correlated with advanced pathological grade and poorer prognosis in ccRCC patients receiving sunitinib treatment. Fluvastatin enhance the sensitivity of sunitinib-resistant ccRCC cells to sunitinib by directly targeting PHF8 and promoting its proteasomal degradation.

关键词

Keywords

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Bone marrow mesenchymal stem cell-derived exosomes promote proliferation, invasion and migration of renal cancer cells by regulating cholestanol metabolism

Clinicopathological analysis of fumarate hydratase-deficient renal cell carcinoma and literature review

Differential diagnosis of common subtypes of renal cell carcinoma based on corrected CT value and relative enhancement rate in multi-slice spiral CT

Lentivirus-mediated LATS1 overexpression suppresses proliferation, improves apoptosis and down-regulates downstream oncogene YAP in human renal cell carcinoma 786-0 cells

Related Author

Xiaoming LI

Guangjie DUAN

Ping CAI

Guojiao ZUO

Qiao XIE

Dongzi NIE

Hexi WANG

Xueyang LIU

Related Institution

Department of Radiology, Frist Affiliated Hospital, Army Medical University (Third Military Medical University)

Department of Pathology, Frist Affiliated Hospital, Army Medical University (Third Military Medical University)

Department of Urology, the First Affiliated Hospital of Chongqing Medical University

Institute of Pathology, First Affiliated Hospital, Army Medical University (Third Military Medical University)

Department of Radiology, Second Affiliated Hospital, Army Medical University (Third Military Medical University)

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