Inhibition of the RBMS1/PRNP axis improves ferroptosis resistance-mediated oxaliplatin chemoresistance in colorectal cancer

Mol Carcinog. 2024 Feb;63(2):224-237. doi: 10.1002/mc.23647. Epub 2023 Oct 20.

Abstract

The majority of patients with advanced colorectal cancer have chemoresistance to oxaliplatin, and studies on oxaliplatin resistance are limited. Our research showed that RNA-binding motif single-stranded interacting protein 1 (RBMS1) caused ferroptosis resistance in tumor cells, leading to oxaliplatin resistance. We employed bioinformatics to evaluate publically accessible data sets and discovered that RBMS1 was significantly upregulated in oxaliplatin-resistant colorectal cancer cells, in tandem with ferroptosis suppression. In vivo and in vitro studies revealed that inhibiting RBMS1 expression caused ferroptosis in colorectal cancer cells, restoring tumor cell sensitivity to oxaliplatin. Mechanistically, this is due to RBMS1 inducing prion protein translation, resulting in ferroptosis resistance in tumor cells. Validation of clinical specimens revealed that RBMS1 is similarly linked to tumor development and a poor prognosis. Overall, RBMS1 is a potential therapeutic target with clinical translational potential, particularly for oxaliplatin chemoresistance in colorectal cancer.

Keywords: RNA-binding motif single-stranded interacting protein 1; colorectal cancer; ferroptosis; oxaliplatin resistance.

MeSH terms

  • Cell Line, Tumor
  • Colorectal Neoplasms* / drug therapy
  • Colorectal Neoplasms* / genetics
  • Colorectal Neoplasms* / metabolism
  • DNA-Binding Proteins / metabolism
  • Drug Resistance, Neoplasm
  • Ferroptosis*
  • Humans
  • Oxaliplatin / pharmacology
  • Prion Proteins / metabolism
  • RNA-Binding Proteins

Substances

  • Oxaliplatin
  • RBMS1 protein, human
  • DNA-Binding Proteins
  • RNA-Binding Proteins
  • PRNP protein, human
  • Prion Proteins