Repair of Oxidative DNA Damage and Cancer: Recent Progress in DNA Base Excision Repair

These results suggest that apyrimidinic endonuclease 1 does not cross the nuclear membrane in its monoubiquitinated form

Timothy L. Scott; Suganya Rangaswamy; Christina A. Wicker; Tadahide Izumi


Scholarcy highlights

  • Shogyo Mujo: nothing can stay unchanged, a layman’s term equal to the second law of thermodynamics
  • This review discuses reactive oxygen species generation from mitochondria first, as the cellular response to oxidative stress and DNA damage is closely linked to carcinogenesis
  • While the relatively broad substrate specificity of NEIL2 makes it difficult to assess a particular kind of oxidative base damage to link to cancer risk, it is independently reported that 5-OHU is highly mutagenic and it is possible that cells carrying NEIL2 with the particular Single nucleotide polymorphisms accumulate 5-OHU, which increases cancer risk
  • In an early study in T-cells, it was reported that apyrimidinic endonuclease 1 was in the endoplasmic reticulum as a component of the SET complex, and during apoptosis APE1 is translocated into nuclei with N-terminal 35 amino acid truncation, the site different from the one during mitochondrial translocalization
  • It should be noted that mitochondrial APE1, which is processed through a similar truncation did not show an increase in exonuclease activity, and APE1 must be associated with some other factors to facilitate exonuclease reaction
  • While ubiquitin-APE1 fusion protein was found exclusively in the cytoplasm, APE1 ubiquitinated de novo was detected in the nuclei and in a chromatin bound complex. These results suggest that APE1 does not cross the nuclear membrane in its monoubiquitinated form
  • Recent studies described above are beginning to link the DNA repair and the other activities of apyrimidinic endonuclease 1 toward understanding of APE1’s influence on cancer malignancies

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