Accelerated repair and reduced mutagenicity of oxidative DNA damage in human bladder cells expressing the E. coli FPG protein

Monica Ropolo, Alessandro Geroldi, Paolo Degan, Virginia Andreotti, Simona Zupo, Alessandro Poggi, April Reed, Mark R. Kelley, Guido Frosina

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

Repair of some oxidized purines such as 8-oxo-7,8-dihydroguanine (8-oxoG) is inefficient in human cells in comparison to repair of other major endogenous lesions (e.g. uracil, abasic sites or oxidized pyrimidines). This is due to the poor catalytic properties of hOGG1, the major DNA glycosylase involved in 8-oxoG removal. The formamidopyrimidine DNA glycosylase (FPG) protein from E. coli is endowed with a potent 8-oxoG glycolytic activity coupled with a β,δ-AP lyase. In this study, we have expressed FPG fused to the enhanced green fluorescent protein (EGFP) in human bladder cells to accelerate the repair of oxidative DNA damage. Cells expressing the fusion protein EGFP-FPG repaired 8-oxoG and AP sites at accelerated rates, in particular via the single-nucleotide insertion base excision repair (BER) pathway and were resistant to mutagenicity of the oxidizing carcinogen potassium bromate. FPG may stably protect human cells from some harmful effects of oxidative DNA damage.

Original languageEnglish (US)
Pages (from-to)1628-1634
Number of pages7
JournalInternational Journal of Cancer
Volume118
Issue number7
DOIs
StatePublished - Apr 1 2006

Keywords

  • Antimutagenesis
  • DNA base excision repair
  • FPG protein
  • Overexpression
  • Oxidative DNA damage

ASJC Scopus subject areas

  • Cancer Research
  • Oncology

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