Cellular and Molecular Life Sciences

, Volume 67, Issue 21, pp 3589–3608 | Cite as

Understanding different functions of mammalian AP endonuclease (APE1) as a promising tool for cancer treatment

  • Gianluca Tell
  • Damiano Fantini
  • Franco Quadrifoglio
Multi-Author Review


The apurinic endonuclease 1/redox factor-1 (APE1) has a crucial function in DNA repair and in redox signaling in mammals, and recent studies identify it as an excellent target for sensitizing tumor cells to chemotherapy. APE1 is an essential enzyme in the base excision repair pathway of DNA lesions caused by oxidation and alkylation. As importantly, APE1 also functions as a redox agent maintaining transcription factors involved in cancer promotion and progression in an active reduced state. Very recently, a new unsuspected function of APE1 in RNA metabolism was discovered, opening new perspectives for this multifunctional protein. These observations underline the necessity to understand the molecular mechanisms responsible for fine-tuning its different biological functions. This survey intends to give an overview of the multifunctional roles of APE1 and their regulation in the context of considering this protein a promising tool for anticancer therapy.


Base excision repair Oxidative stress Redox signalling Nucleolus Cancer 







Activating Protein-1


Apurinic apyrimidinic endonuclease 1


Base excision repair


Casein kinase I and II


cAMP-responsible element binding protein


Early growth response protein-1


Flap endonuclease I


Glycogen synthase kinase 3


Granzyme A


Granzyme K


Hypoxia inducible factor-1α


Mitochondrial targeting sequence


Methylpurine DNA glycosylase


Human MutY glycosylase homolog


Nuclear factor-kappaB


Negative calcium responsive elements


Nuclear localization signal


Nucleophosmin 1


8-Oxoguanine DNA glycosylase


Poly(ADP-ribose) polymerase


Paired box-containing proteins


Proliferating cell nuclear antigen


Polyoma virus enhancer-binding protein-2


Protein kinase C


Polymerase β


Phosphatase and tensin homolog


Parathyroid hormone


Post-translational modification


Replication factor C


Reactive oxygen species




X-ray cross-species complementing 1



We thank Dr. Mark R. Kelley for helpful discussions. This work was supported by grants from: MIUR (FIRB RBRN07BMCT_008 and PRIN 2008CCPKRP_003) and from MAE (Joint Mobility Projects Program 2008–2010) to G.T.


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Copyright information

© Springer Basel AG 2010

Authors and Affiliations

  • Gianluca Tell
    • 1
  • Damiano Fantini
    • 1
  • Franco Quadrifoglio
    • 1
  1. 1.Department of Biomedical Sciences and TechnologiesUniversity of UdineUdineItaly

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