Defective Mitochondrial Peroxiredoxin-3 Results in Sensitivity to Oxidative Stress in Fanconi Anemia
Cells from patients with Fanconi anemia (FA), an inherited disorder that includes bone marrow failure and cancer predisposition, have increased sensitivity to oxidative stress through an unknown mechanism. We demonstrate that the FA group G (FANCG) protein is found in mitochondria. Wild-type but not...
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Published in | The Journal of cell biology Vol. 175; no. 2; pp. 225 - 235 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
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United States
Rockefeller University Press
23.10.2006
The Rockefeller University Press |
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Abstract | Cells from patients with Fanconi anemia (FA), an inherited disorder that includes bone marrow failure and cancer predisposition, have increased sensitivity to oxidative stress through an unknown mechanism. We demonstrate that the FA group G (FANCG) protein is found in mitochondria. Wild-type but not G546R mutant FANCG physically interacts with the mitochondrial peroxidase peroxiredoxin-3 (PRDX3). PRDX3 is deregulated in FA cells, including cleavage by a calpainlike cysteine protease and mislocalization. FA-G cells demonstrate distorted mitochondrial structures, and mitochondrial extracts have a sevenfold decrease in thioredoxin-dependent peroxidase activity. Transient overexpression of PRDX3 suppresses the sensitivity of FA-G cells to H2O
2, and decreased PRDX3 expression increases sensitivity to mitomycin C. Cells from the FA-A and -C subtypes also have PRDX3 cleavage and decreased peroxidase activity. This study demonstrates a role for the FA proteins in mitochondria witsh sensitivity to oxidative stress resulting from diminished peroxidase activity. These defects may lead to apoptosis and the accumulation of oxidative DNA damage in bone marrow precursors. |
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AbstractList | Cells from patients with Fanconi anemia (FA), an inherited disorder that includes bone marrow failure and cancer predisposition, have increased sensitivity to oxidative stress through an unknown mechanism. We demonstrate that the FA group G (FANCG) protein is found in mitochondria. Wild-type but not G546R mutant FANCG physically interacts with the mitochondrial peroxidase peroxiredoxin-3 (PRDX3). PRDX3 is deregulated in FA cells, including cleavage by a calpainlike cysteine protease and mislocalization. FA-G cells demonstrate distorted mitochondrial structures, and mitochondrial extracts have a sevenfold decrease in thioredoxin-dependent peroxidase activity. Transient overexpression of PRDX3 suppresses the sensitivity of FA-G cells to H2O2, and decreased PRDX3 expression increases sensitivity to mitomycin C. Cells from the FA-A and -C subtypes also have PRDX3 cleavage and decreased peroxidase activity. This study demonstrates a role for the FA proteins in mitochondria witsh sensitivity to oxidative stress resulting from diminished peroxidase activity. These defects may lead to apoptosis and the accumulation of oxidative DNA damage in bone marrow precursors. Cells from patients with Fanconi anemia (FA), an inherited disorder that includes bone marrow failure and cancer predisposition, have increased sensitivity to oxidative stress through an unknown mechanism. We demonstrate that the FA group G (FANCG) protein is found in mitochondria. Wild-type but not G546R mutant FANCG physically interacts with the mitochondrial peroxidase peroxiredoxin-3 (PRDX3). PRDX3 is deregulated in FA cells, including cleavage by a calpainlike cysteine protease and mislocalization. FA-G cells demonstrate distorted mitochondrial structures, and mitochondrial extracts have a sevenfold decrease in thioredoxin-dependent peroxidase activity. Transient overexpression of PRDX3 suppresses the sensitivity of FA-G cells to H 2 O 2 , and decreased PRDX3 expression increases sensitivity to mitomycin C. Cells from the FA-A and -C subtypes also have PRDX3 cleavage and decreased peroxidase activity. This study demonstrates a role for the FA proteins in mitochondria witsh sensitivity to oxidative stress resulting from diminished peroxidase activity. These defects may lead to apoptosis and the accumulation of oxidative DNA damage in bone marrow precursors. Cells from patients with Fanconi anemia (FA), an inherited disorder that includes bone marrow failure and cancer predisposition, have increased sensitivity to oxidative stress through an unknown mechanism. We demonstrate that the FA group G (FANCG) protein is found in mitochondria. Wild-type but not G546R mutant FANCG physically interacts with the mitochondrial peroxidase peroxiredoxin-3 (PRDX3). PRDX3 is deregulated in FA cells, including cleavage by a calpainlike cysteine protease and mislocalization. FA-G cells demonstrate distorted mitochondrial structures, and mitochondrial extracts have a sevenfold decrease in thioredoxin-dependent peroxidase activity. Transient overexpression of PRDX3 suppresses the sensitivity of FA-G cells to H2O2, and decreased PRDX3 expression increases sensitivity to mitomycin C. Cells from the FA-A and -C subtypes also have PRDX3 cleavage and decreased peroxidase activity. This study demonstrates a role for the FA proteins in mitochondria witsh sensitivity to oxidative stress resulting from diminished peroxidase activity. These defects may lead to apoptosis and the accumulation of oxidative DNA damage in bone marrow precursors. [PUBLICATION ABSTRACT] Cells from patients with Fanconi anemia (FA), an inherited disorder that includes bone marrow failure and cancer predisposition, have increased sensitivity to oxidative stress through an unknown mechanism. We demonstrate that the FA group G (FANCG) protein is found in mitochondria. Wild-type but not G546R mutant FANCG physically interacts with the mitochondrial peroxidase peroxiredoxin-3 (PRDX3). PRDX3 is deregulated in FA cells, including cleavage by a calpainlike cysteine protease and mislocalization. FA-G cells demonstrate distorted mitochondrial structures, and mitochondrial extracts have a sevenfold decrease in thioredoxin-dependent peroxidase activity. Transient overexpression of PRDX3 suppresses the sensitivity of FA-G cells to H2O 2, and decreased PRDX3 expression increases sensitivity to mitomycin C. Cells from the FA-A and -C subtypes also have PRDX3 cleavage and decreased peroxidase activity. This study demonstrates a role for the FA proteins in mitochondria witsh sensitivity to oxidative stress resulting from diminished peroxidase activity. These defects may lead to apoptosis and the accumulation of oxidative DNA damage in bone marrow precursors. |
Author | Kathryn S. Leung M. John Hicks Sudit S. Mukhopadhyay Philip J. Hastings Plon, Sharon E. Youssoufian, Hagop |
AuthorAffiliation | 1 Department of Pediatrics, 2 Department of Molecular and Human Genetics, and 3 Department of Pathology, Baylor College of Medicine, Houston, TX 77030 |
AuthorAffiliation_xml | – name: 1 Department of Pediatrics, 2 Department of Molecular and Human Genetics, and 3 Department of Pathology, Baylor College of Medicine, Houston, TX 77030 |
Author_xml | – sequence: 1 fullname: Sudit S. Mukhopadhyay – sequence: 2 fullname: Kathryn S. Leung – sequence: 3 fullname: M. John Hicks – sequence: 4 fullname: Philip J. Hastings – sequence: 5 givenname: Hagop surname: Youssoufian fullname: Youssoufian, Hagop – sequence: 6 givenname: Sharon E. surname: Plon fullname: Plon, Sharon E. |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/17060495$$D View this record in MEDLINE/PubMed |
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Copyright | Copyright 2006 The Rockefeller University Press Copyright Rockefeller University Press Oct 23, 2006 Copyright © 2006, The Rockefeller University Press 2006 |
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Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 H. Youssoufian's present address is ImClone Systems, Inc., New York, NY 10014. Abbreviations used in this paper: FA, Fanconi anemia; MMC, mitomycin C; MTT, 3-(4,5-dimethyl-thiazol-2yl)-2,5-diphenyl-tetrazolium bromide; NF1, nuclear factor 1; PRDX, peroxiredoxin; RIPA, radioimmunoprecipitation assay; ROS, reactive oxygen species; TR, Trx reductase; Trx, thioredoxin. S.S. Mukhopadhyay's present address is The University of Texas MD Anderson Cancer Center, Houston, TX 77030. Correspondence to Sharon E. Plon: splon@bcm.tmc.edu |
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Snippet | Cells from patients with Fanconi anemia (FA), an inherited disorder that includes bone marrow failure and cancer predisposition, have increased sensitivity to... |
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SubjectTerms | Anemia Animals Antibiotics, Antineoplastic - pharmacology Antibodies Apoptosis Calpain - metabolism Cell lines Cellular biology Cercopithecus aethiops COS Cells DNA damage Fanconi anemia Fanconi Anemia - metabolism Fanconi Anemia Complementation Group G Protein - metabolism Fibroblasts Fibroblasts - cytology Fibroblasts - drug effects Fibroblasts - metabolism Fluorescent Antibody Technique Genetic disorders HeLa Cells Humans Hydrogen Peroxide - pharmacology Immunoprecipitation Lymphocytes - cytology Lymphocytes - drug effects Lymphocytes - metabolism Mitochondria Mitochondria - metabolism Mitochondrial DNA Mitomycin - pharmacology Mutation Oxidation-Reduction Oxidative stress Oxidative Stress - drug effects Peroxidase - metabolism Peroxidases - metabolism Peroxiredoxin III Peroxiredoxins Proteins Saccharomyces cerevisiae - growth & development Saccharomyces cerevisiae - metabolism Two-Hybrid System Techniques Ubiquitin - metabolism |
Title | Defective Mitochondrial Peroxiredoxin-3 Results in Sensitivity to Oxidative Stress in Fanconi Anemia |
URI | https://www.jstor.org/stable/4152153 https://www.ncbi.nlm.nih.gov/pubmed/17060495 https://www.proquest.com/docview/217108245/abstract/ https://search.proquest.com/docview/68985422 https://pubmed.ncbi.nlm.nih.gov/PMC2064564 |
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