Mitochondrial and cytosolic expression of human peroxiredoxin 5 in Saccharomyces cerevisiae protect yeast cells from oxidative stress induced by paraquat

被引:33
作者
Nguyên-nhu, NT [1 ]
Knoops, B [1 ]
机构
[1] Catholic Univ Louvain, Cell Biol Lab, ISV, Dept Biol, B-1348 Louvain, Belgium
关键词
peroxiredoxin; paraquat; yeast; mitochondria; cytosol; oxidative stress;
D O I
10.1016/S0014-5793(03)00493-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Human peroxiredoxin 5 is a recently discovered mitochondrial, peroxisomal and cytosolic thioredoxin peroxidase able to reduce hydrogen peroxide and alkyl hydroperoxides. To gain insight into peroxiredoxin 5 antioxidant role in cell protection, we investigated the resistance of yeast cells expressing human peroxiredoxin 5 in mitochondria or in the cytosol against oxidative stress induced by paraquat. The herbicide paraquat is a redox active drug known to generate superoxide anions in mitochondria and the cytosol of yeast and mammalian cells leading to the formation of several reactive oxygen species. Here, we report that mitochondrial and cytosolic human peroxiredoxin 5 protect yeast cells from cytotoxicity and lipid peroxidation induced by paraquat. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:148 / 152
页数:5
相关论文
共 34 条
[1]   From Cytoprotection to Tumor Suppression: The Multifactorial Role of Peroxiredoxins [J].
Butterfield, Lisa H. ;
Merino, Alejandro ;
Golub, Sidney H. ;
Shau, Hungyi .
ANTIOXIDANTS & REDOX SIGNALING, 1999, 1 (04) :385-402
[2]   Requirement for the two AhpF cystine disulfide centers in catalysis of peroxide reduction by alkyl hydroperoxide reductase [J].
Calzi, ML ;
Poole, LB .
BIOCHEMISTRY, 1997, 36 (43) :13357-13364
[3]  
CHAE HZ, 1994, J BIOL CHEM, V269, P27670
[4]   Triggering and modulation of apoptosis by oxidative stress [J].
Chandra, J ;
Samali, A ;
Orrenius, S .
FREE RADICAL BIOLOGY AND MEDICINE, 2000, 29 (3-4) :323-333
[5]   1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities [J].
Chen, JW ;
Dodia, C ;
Feinstein, SI ;
Jain, MK ;
Fisher, AB .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (37) :28421-28427
[6]   ON THE EFFECTS OF PARAQUAT ON ISOLATED-MITOCHONDRIA - EVIDENCE THAT PARAQUAT CAUSES OPENING OF THE CYCLOSPORINE A-SENSITIVE PERMEABILITY TRANSITION PORE SYNERGISTICALLY WITH NITRIC-OXIDE [J].
COSTANTINI, P ;
PETRONILLI, V ;
COLONNA, R ;
BERNARDI, P .
TOXICOLOGY, 1995, 99 (1-2) :77-88
[7]   Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 Å resolution [J].
Declercq, JP ;
Evrard, C ;
Clippe, A ;
Vander Stricht, D ;
Bernard, A ;
Knoops, B .
JOURNAL OF MOLECULAR BIOLOGY, 2001, 311 (04) :751-759
[8]   Glutathione and trypanothione in parasitic hydroperoxide metabolism [J].
Flohé, L ;
Hecht, HJ ;
Steinert, P .
FREE RADICAL BIOLOGY AND MEDICINE, 1999, 27 (9-10) :966-984
[9]   Advances in our understanding of peroxiredoxin, a multifunctional, mammalian redox protein [J].
Fujii, J ;
Ikeda, Y .
REDOX REPORT, 2002, 7 (03) :123-130
[10]  
Halliwell B, 1996, ANNU REV NUTR, V16, P33, DOI 10.1146/annurev.nu.16.070196.000341