High expression of ADAR mediated by OGT promotes chemoresistance in colorectal cancer through the A-to-I editing pathway

Mol Genet Genomics. 2024 Nov 11;299(1):106. doi: 10.1007/s00438-024-02197-4.

Abstract

Colorectal cancer (CRC) is a malignant tumor with poor prognosis and adverse therapeutic effect. The study aims to elucidate the contribution of OGT-mediated glycosylation of ADAR to chemoresistance in CRC through its role and regulatory mechanisms. Variations in OGT expression levels and their impact on CRC cell chemoresistance were investigated using gain-of-function and loss-of-function assays. Through a series of molecular biology experiments, we confirmed that ADAR is the downstream target of OGT regulation, emphasizing the role of OGT-mediated glycosylation in stabilizing ADAR. Furthermore, RNA immunoprecipitation (RIP) assays were conducted to examine the effects of ADAR-mediated A-to-I editing on the mRNA stability and translation of genes associated with DNA damage repair. Elevated OGT expression was found to enhance CRC's malignancy and resistance to chemotherapy. OGT's influence leads to the glycosylation of ADAR, thereby increasing its protein levels. ADAR, through its role in A-to-I editing, modulates the mRNA editing of genes implicated in DNA damage repair. This regulation enhances the expression of these genes, improves DNA repair capabilities, and ultimately, fosters chemoresistance in CRC cells. In conclusion, ADAR promotes PARP1 expression under the positive regulation of OGT-mediated O-glycosylation modification to enhance drug resistance in COAD cells. It provides the research basis for overcoming the drug resistance of CRC.

Keywords: ADAR; Chemoresistance; Colorectal cancer; OGT.

MeSH terms

  • Adenosine Deaminase* / genetics
  • Adenosine Deaminase* / metabolism
  • Cell Line, Tumor
  • Colorectal Neoplasms* / drug therapy
  • Colorectal Neoplasms* / genetics
  • Colorectal Neoplasms* / pathology
  • DNA Repair / genetics
  • Drug Resistance, Neoplasm* / genetics
  • Gene Expression Regulation, Neoplastic*
  • Glycosylation
  • Humans
  • N-Acetylglucosaminyltransferases* / genetics
  • N-Acetylglucosaminyltransferases* / metabolism
  • RNA Editing / genetics
  • RNA Stability / genetics
  • RNA-Binding Proteins* / genetics
  • RNA-Binding Proteins* / metabolism

Substances

  • RNA-Binding Proteins
  • Adenosine Deaminase
  • N-Acetylglucosaminyltransferases
  • ADAR protein, human
  • OGT protein, human