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Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis

Y Zhou1, K H Kok, A C Chun

  • 1Institute of Molecular Biology, Division of Medical Physics, Department of Medicine, University of Hong Kong, Pokfulam, Hong Kong, China.

Biochemical and Biophysical Research Communications
|February 19, 2000
PubMed

Insights

Human and mouse peroxiredoxin V (Prx-V), a novel antioxidant enzyme, regulates intracellular redox signaling. Overexpression of Prx-V prevents p53-dependent reactive oxygen species generation and inhibits apoptosis.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Peroxiredoxins (Prx) are key antioxidant enzymes involved in cellular redox homeostasis.
  • The peroxiredoxin V (Prx-V) subfamily, including human and mouse orthologs, is newly identified.
  • Prx-V shares homology with yeast peroxisomal antioxidant enzyme PMP20 and has bacterial orthologs.

Purpose of the Study:

  • To identify and characterize human and mouse peroxiredoxin V (Prx-V).
  • To investigate the role of Prx-V in p53-mediated apoptosis and intracellular redox signaling.

Main Methods:

  • Sequence homology analysis for identification of Prx-V.
  • Biochemical characterization of Prx-V as a thioredoxin peroxidase.
  • Experimental manipulation of Prx-V expression to assess its impact on p53 function.

Main Results:

  • Human and mouse Prx-V were identified, representing a novel mammalian peroxiredoxin subfamily.
  • Prx-V functions biochemically as a thioredoxin peroxidase.
  • Overexpression of Prx-V inhibited p53-dependent reactive oxygen species generation and p53-induced apoptosis.

Conclusions:

  • Prx-V is a novel organellar thioredoxin peroxidase with orthologs in bacteria.
  • Prx-V plays a critical role in regulating intracellular redox signaling pathways.
  • Prx-V acts as a negative regulator of p53-mediated apoptosis.

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