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Overview on Peroxiredoxin

  • Rhee, Sue Goo (Yonsei Biomedical Research Institute, Yonsei University College of Medicine)
  • Published : 2016.01.31
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Abstract

Peroxiredoxins (Prxs) are a very large and highly conserved family of peroxidases that reduce peroxides, with a conserved cysteine residue, designated the "peroxidatic" Cys ($C_P$) serving as the site of oxidation by peroxides (Hall et al., 2011; Rhee et al., 2012). Peroxides oxidize the $C_P$-SH to cysteine sulfenic acid ($C_P$-SOH), which then reacts with another cysteine residue, named the "resolving" Cys ($C_R$) to form a disulfide that is subsequently reduced by an appropriate electron donor to complete a catalytic cycle. This overview summarizes the status of studies on Prxs and relates the following 10 minireviews.

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References

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  46. Saccharomyces cerevisiae TSA1의 보존된 아스파트산 잔기 및 세린 잔기의 변이가 과산화효소 활성 및 샤페론 활성에 미치는 영향 vol.45, pp.1, 2016, https://doi.org/10.4014/mbl.1702.02003
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  59. Upregulation of Peroxiredoxin 3 Protects Afg3l 2-KO Cortical Neurons In Vitro from Oxidative Stress: A Paradigm for Neuronal Cell Survival under Neurodegenerative Conditions vol.2019, pp.None, 2016, https://doi.org/10.1155/2019/4721950
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  61. Antioxidants Special Issue: Peroxiredoxin 6 as a Unique Member of the Peroxiredoxin Family vol.8, pp.4, 2019, https://doi.org/10.3390/antiox8040107
  62. Protein Redox State Monitoring Studies of Thiol Reactivity vol.8, pp.5, 2016, https://doi.org/10.3390/antiox8050143
  63. Frugoside Induces Mitochondria-Mediated Apoptotic Cell Death through Inhibition of Sulfiredoxin Expression in Melanoma Cells vol.11, pp.6, 2019, https://doi.org/10.3390/cancers11060854
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  69. Protective role of exogenous recombinant peroxiredoxin 6 under ischemia-reperfusion injury of kidney vol.378, pp.2, 2019, https://doi.org/10.1007/s00441-019-03073-z
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  71. Involvement of peroxiredoxin 2 in cumulus expansion and oocyte maturation in mice vol.32, pp.8, 2020, https://doi.org/10.1071/rd19310
  72. Protective Role of Peroxiredoxins against Reactive Oxygen Species in Neonatal Rat Testicular Gonocytes vol.9, pp.1, 2020, https://doi.org/10.3390/antiox9010032
  73. Redox Signaling from Mitochondria: Signal Propagation and Its Targets vol.10, pp.1, 2016, https://doi.org/10.3390/biom10010093
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  75. Proteomic Analysis of Stationary Growth Stage Adaptation and Nutritional Deficiency Response of Brucella abortus vol.11, pp.None, 2016, https://doi.org/10.3389/fmicb.2020.598797
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  78. Triple Combination of Ascorbate, Menadione and the Inhibition of Peroxiredoxin-1 Produces Synergistic Cytotoxic Effects in Triple-Negative Breast Cancer Cells vol.9, pp.4, 2020, https://doi.org/10.3390/antiox9040320
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  82. The interplay between oxidative stress and bioenergetic failure in neuropsychiatric illnesses: can we explain it and can we treat it? vol.47, pp.7, 2016, https://doi.org/10.1007/s11033-020-05590-5
  83. Use of peroxiredoxin for preconditioning of heterotopic heart transplantation in a rat vol.22, pp.2, 2020, https://doi.org/10.15825/1995-1191-2020-2-158-164
  84. Whey protein boosts the antioxidant profile of rats by enhancing the activities of crucial antioxidant enzymes in a tissue-specific manner vol.142, pp.None, 2016, https://doi.org/10.1016/j.fct.2020.111508
  85. Enzymatic Antioxidant Signatures in Hyperthermophilic Archaea vol.9, pp.8, 2020, https://doi.org/10.3390/antiox9080703
  86. Deficiency of peroxiredoxin 2 exacerbates angiotensin II-induced abdominal aortic aneurysm vol.52, pp.9, 2020, https://doi.org/10.1038/s12276-020-00498-3
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  88. Protein signatures of seminal plasma from bulls with contrasting frozen-thawed sperm viability vol.10, pp.None, 2016, https://doi.org/10.1038/s41598-020-71015-9
  89. Testis-specific peroxiredoxin 4 variant is not absolutely required for spermatogenesis and fertility in mice vol.10, pp.1, 2020, https://doi.org/10.1038/s41598-020-74667-9
  90. Unlocking Survival Mechanisms for Metal and Oxidative Stress in the Extremely Acidophilic, Halotolerant Acidihalobacter Genus vol.11, pp.12, 2016, https://doi.org/10.3390/genes11121392
  91. Oxidative Stress and Antioxidant Treatments in Cardiovascular Diseases vol.9, pp.12, 2016, https://doi.org/10.3390/antiox9121292
  92. Assessment of Potential Prognostic Value of Peroxiredoxin 1 in Oral Squamous Cell Carcinoma vol.13, pp.None, 2016, https://doi.org/10.2147/cmar.s319048
  93. Post-Translational Modification of Cysteines: A Key Determinant of Endoplasmic Reticulum-Mitochondria Contacts (MERCs) vol.4, pp.None, 2016, https://doi.org/10.1177/25152564211001213
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  96. De novo assembly and functional annotation of blood transcriptome of loggerhead turtle, and in silico characterization of peroxiredoxins and thioredoxins vol.9, pp.None, 2021, https://doi.org/10.7717/peerj.12395
  97. Sex-Biased Gene Expression of Mesobuthus martensii Collected from Gansu Province, China, Reveals Their Different Therapeutic Potentials vol.2021, pp.None, 2016, https://doi.org/10.1155/2021/1967158
  98. Emerging Evidence Highlighting the Importance of Redox Dysregulation in the Pathogenesis of Amyotrophic Lateral Sclerosis (ALS) vol.14, pp.None, 2016, https://doi.org/10.3389/fncel.2020.581950
  99. Protein Expression of Angiotensin-Converting Enzyme 2 (ACE2) is Upregulated in Brains with Alzheimer’s Disease vol.22, pp.4, 2016, https://doi.org/10.3390/ijms22041687
  100. The Dawn of Mitophagy: What Do We Know by Now? vol.19, pp.2, 2016, https://doi.org/10.2174/1570159x18666200522202319
  101. Tyrosine Phosphorylation Modulates Peroxiredoxin-2 Activity in Normal and Diseased Red Cells vol.10, pp.2, 2016, https://doi.org/10.3390/antiox10020206
  102. Fighting Bisphenol A-Induced Male Infertility: The Power of Antioxidants vol.10, pp.2, 2016, https://doi.org/10.3390/antiox10020289
  103. Physical Activity and Redox Balance in the Elderly: Signal Transduction Mechanisms vol.11, pp.5, 2016, https://doi.org/10.3390/app11052228
  104. Stoichiometric Thiol Redox Proteomics for Quantifying Cellular Responses to Perturbations vol.10, pp.3, 2016, https://doi.org/10.3390/antiox10030499
  105. The Role of Non-Coding RNAs in the Neuroprotective Effects of Glutathione vol.22, pp.8, 2021, https://doi.org/10.3390/ijms22084245
  106. Induction of apoptosis in indole-3-carbinol-treated lung cancer H1299 cells via ROS level elevation vol.40, pp.5, 2016, https://doi.org/10.1177/0960327120969968
  107. Peroxiredoxins—The Underrated Actors during Virus-Induced Oxidative Stress vol.10, pp.6, 2016, https://doi.org/10.3390/antiox10060977
  108. β-Hydroxybutyrate, a Ketone Body, Potentiates the Antioxidant Defense via Thioredoxin 1 Upregulation in Cardiomyocytes vol.10, pp.7, 2016, https://doi.org/10.3390/antiox10071153
  109. H2O2 Induces Major Phosphorylation Changes in Critical Regulators of Signal Transduction, Gene Expression, Metabolism and Developmental Networks in Aspergillus nidulans vol.7, pp.8, 2016, https://doi.org/10.3390/jof7080624
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  112. Label-free proteomic analysis reveals differentially expressed Wolbachia proteins in Tyrophagus putrescentiae: Mite allergens and markers reflecting population-related proteome differences vol.249, pp.None, 2021, https://doi.org/10.1016/j.jprot.2021.104356
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  114. PRDX1 is essential for the viability and maintenance of reactive oxygen species in chicken DT40 vol.43, pp.1, 2016, https://doi.org/10.1186/s41021-021-00211-4
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  116. Adaptative Up-Regulation of PRX2 and PRX5 Expression Characterizes Brain from a Mouse Model of Chorea-Acanthocytosis vol.11, pp.1, 2022, https://doi.org/10.3390/antiox11010076