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

Yuan Zhou, K. H. Kok, Abel C.S. Chun, Chi Ming Wong, Hing Wan Wu, Marie C.M. Lin, Peter C.W. Fung, Hsiang fu Kung, Dong Yan Jin

Research output: Journal article publicationJournal articleAcademic researchpeer-review

152 Citations (Scopus)


We have identified human and mouse peroxiredoxin V (Prx-V) by virtue of the sequence homologies to yeast peroxisomal antioxidant enzyme PMP20. Prx-V represents the fifth of the six currently known subfamilies of mammalian peroxiredoxins. It is a novel organellar enzyme that has orthologs in bacteria. Biochemically, Prx-V is a thioredoxin peroxidase. One important aspect of p53 function in mammalian cells involves induction of apoptosis likely mediated by redox. We show that overexpression of Prx-V prevented the p53-dependent generation of reactive oxygen species. Likewise, Prx-V inhibited p53-induced apoptosis. Thus, Prx-V is critically involved in intracellular redox signaling. (C) 2000 Academic Press.
Original languageEnglish
Pages (from-to)921-927
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number3
Publication statusPublished - 24 Feb 2000
Externally publishedYes


  • Apoptosis
  • p53
  • Peroxiredoxin
  • Reactive oxygen species (ROS)
  • Redox
  • Thioredoxin peroxidase

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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