Scholarlink

Background <p>Gomisin B was reported to alleviate neuroblastoma (NB) progression, and the promotion of ferroptosis also inhibited NB. This study aimed to investigate the mechanism by which Gomisin B regulates ESR1 to affect ferroptosis in NB.</p> Methods <p>SH-SY5Y and IMR-32 cells were induced to ferroptosis by RSL3 and treated with Gomisin B. Co-IP was utilized to probe the relationship between USP7 and SREBF1. The interaction between ESR1 and USP7 was tested by dual luciferase reporter and ChIP. In addition, cell viability was assessed via CCK-8. Commercial kits were implemented to determine the MDA, GSH, Fe<sup>2+</sup>, and LPO levels. C-11 BODIPY 581/591 fluorescent probe was employed to examine lipid ROS level. BALB/c nude mice were used to construct NB animal models for in vivo studies.</p> Results <p>Gomisin B promoted ferroptosis in NB cells and overexpression of ESR1 reversed this phenomenon. Additionally, ESR1 transcriptionally activated USP7 by interacting with the USP7 promoter to inhibit NB cell ferroptosis. USP7 facilitated SREBF1 deubiquitination by binding to SREBF1, thereby enhancing its protein stability. Gomisin B regulated the ESR1/USP7/SREBF1 axis to promote ferroptosis in NB cells. Finally, it was verified at the animal level that Gomisin B promoted ferroptosis and inhibited tumor growth in NB tumor-bearing nude mice.</p> Conclusion <p>Gomisin B inhibited the transcriptional activation of USP7 by downregulating ESR1, thereby suppressing the deubiquitination of SREBF1. This enhanced NB ferroptosis to alleviate NB progression.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Gomisin B promotes RSL3-induced ferroptosis in neuroblastoma by inhibiting the ESR1/USP7/SREBF1 axis

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年3月9日

查看全文
  • Mengyao Dong,
  • Ting Gao,
  • Yongtao Xu,
  • Qinghao Li,
  • Zhaolong Ma,
  • Bin Zhao,
  • Ming Ming

摘要

Background

Gomisin B was reported to alleviate neuroblastoma (NB) progression, and the promotion of ferroptosis also inhibited NB. This study aimed to investigate the mechanism by which Gomisin B regulates ESR1 to affect ferroptosis in NB.

Methods

SH-SY5Y and IMR-32 cells were induced to ferroptosis by RSL3 and treated with Gomisin B. Co-IP was utilized to probe the relationship between USP7 and SREBF1. The interaction between ESR1 and USP7 was tested by dual luciferase reporter and ChIP. In addition, cell viability was assessed via CCK-8. Commercial kits were implemented to determine the MDA, GSH, Fe2+, and LPO levels. C-11 BODIPY 581/591 fluorescent probe was employed to examine lipid ROS level. BALB/c nude mice were used to construct NB animal models for in vivo studies.

Results

Gomisin B promoted ferroptosis in NB cells and overexpression of ESR1 reversed this phenomenon. Additionally, ESR1 transcriptionally activated USP7 by interacting with the USP7 promoter to inhibit NB cell ferroptosis. USP7 facilitated SREBF1 deubiquitination by binding to SREBF1, thereby enhancing its protein stability. Gomisin B regulated the ESR1/USP7/SREBF1 axis to promote ferroptosis in NB cells. Finally, it was verified at the animal level that Gomisin B promoted ferroptosis and inhibited tumor growth in NB tumor-bearing nude mice.

Conclusion

Gomisin B inhibited the transcriptional activation of USP7 by downregulating ESR1, thereby suppressing the deubiquitination of SREBF1. This enhanced NB ferroptosis to alleviate NB progression.