Cytosine-based nucleoside analogs are selectively lethal to DNA mismatch repair-deficient tumour cells by enhancing levels of intracellular oxidative stress

Br J Cancer. 2013 Mar 5;108(4):983-92. doi: 10.1038/bjc.2013.3. Epub 2013 Jan 29.

Abstract

Background: DNA mismatch repair deficiency is present in a significant proportion of a number of solid tumours and is associated with distinct clinical behaviour.

Methods: To identify the therapeutic agents that might show selectivity for mismatch repair-deficient tumour cells, we screened a pair of isogenic MLH1-deficient and MLH1-proficient tumour cell lines with a library of clinically used drugs. To test the generality of hits in the screen, selective agents were retested in cells deficient in the MSH2 mismatch repair gene.

Results: We identified cytarabine and other related cytosine-based nucleoside analogues as being selectively toxic to MLH1 and MSH2-deficient tumour cells. The selective cytotoxicity we observed was likely caused by increased levels of cellular oxidative stress, as it could be abrogated by antioxidants.

Conclusion: We propose that cytarabine-based chemotherapy regimens may represent a tumour-selective treatment strategy for mismatch repair-deficient cancers.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing / genetics*
  • Antimetabolites, Antineoplastic / therapeutic use*
  • Cell Line, Tumor
  • Cytarabine / pharmacology*
  • DNA Mismatch Repair / drug effects*
  • DNA Repair-Deficiency Disorders / drug therapy*
  • Humans
  • MutL Protein Homolog 1
  • MutS Homolog 2 Protein / genetics*
  • Neoplasms / genetics*
  • Nuclear Proteins / genetics*
  • Nucleosides
  • Oxidative Stress / drug effects*
  • Oxidative Stress / genetics

Substances

  • Adaptor Proteins, Signal Transducing
  • Antimetabolites, Antineoplastic
  • MLH1 protein, human
  • Nuclear Proteins
  • Nucleosides
  • Cytarabine
  • MSH2 protein, human
  • MutL Protein Homolog 1
  • MutS Homolog 2 Protein