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

doi:10.1006/bbrc.2000.2231

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 publication › Journal article › Academic research › peer-review

152 Citations (Scopus)

Abstract

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 language	English
Pages (from-to)	921-927
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	268
Issue number	3
DOIs	https://doi.org/10.1006/bbrc.2000.2231
Publication status	Published - 24 Feb 2000
Externally published	Yes

Keywords

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

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

More information

10.1006/bbrc.2000.2231

Cite this

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title = "Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis",

abstract = "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.",

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

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AU - Zhou, Yuan

AU - Kok, K. H.

AU - Chun, Abel C.S.

AU - Wong, Chi Ming

AU - Wu, Hing Wan

AU - Lin, Marie C.M.

AU - Fung, Peter C.W.

AU - Kung, Hsiang fu

AU - Jin, Dong Yan

PY - 2000/2/24

Y1 - 2000/2/24

N2 - 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.

AB - 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.

KW - Apoptosis

KW - p53

KW - Peroxiredoxin

KW - Reactive oxygen species (ROS)

KW - Redox

KW - Thioredoxin peroxidase

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U2 - 10.1006/bbrc.2000.2231

DO - 10.1006/bbrc.2000.2231

M3 - Journal article

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SN - 0006-291X

VL - 268

SP - 921

EP - 927

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 3

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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