Nuclear glutaredoxin 3 is critical for protection against oxidative stress-induced cell death.
Identifieur interne : 000527 ( Main/Exploration ); précédent : 000526; suivant : 000528Nuclear glutaredoxin 3 is critical for protection against oxidative stress-induced cell death.
Auteurs : Khanh Pham [États-Unis] ; Rituraj Pal [États-Unis] ; Ying Qu [États-Unis] ; Xi Liu [République populaire de Chine] ; Han Yu [États-Unis] ; Stephen L. Shiao [États-Unis] ; Xinquan Wang [République populaire de Chine] ; E. O'Brian Smith [États-Unis] ; Xiaojiang Cui [États-Unis] ; George G. Rodney [États-Unis] ; Ninghui Cheng [États-Unis]Source :
- Free radical biology & medicine [ 1873-4596 ] ; 2015.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Carrier Proteins, Reactive Oxygen Species.
- metabolism : Cell Nucleus, Subcellular Fractions.
- Cell Line, Tumor, Humans, Oxidative Stress.
Abstract
Mammalian glutaredoxin 3 (Grx3) has been shown to be critical in maintaining redox homeostasis and regulating cell survival pathways in cancer cells. However, the regulation of Grx3 is not fully understood. In the present study, we investigate the subcellular localization of Grx3 under normal growth and oxidative stress conditions. Both fluorescence imaging of Grx3-RFP fusion and Western blot analysis of cellular fractionation indicate that Grx3 is predominantly localized in the cytoplasm under normal growth conditions, whereas under oxidizing conditions, Grx3 is translocated into and accumulated in the nucleus. Grx3 nuclear accumulation was reversible in a redox-dependent fashion. Further analysis indicates that neither the N-terminal Trx-like domain nor the two catalytic cysteine residues in the active CGFS motif of Grx3 are involved in its nuclear translocation. Decreased levels of Grx3 render cells susceptible to cellular oxidative stress, whereas overexpression of nuclear-targeted Grx3 is sufficient to suppress cells' sensitivity to oxidant treatments and reduce reactive oxygen species production. These findings provide novel insights into the regulation of Grx3, which is crucial for cell survival against environmental insults.
DOI: 10.1016/j.freeradbiomed.2015.05.003
PubMed: 25975981
PubMed Central: PMC4902114
Affiliations:
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O'Brian Smith</name><affiliation wicri:level="2"><nlm:affiliation>USDA/ARS Children׳s Nutrition Research Center, Department of Pediatrics, Houston, TX 77030, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>USDA/ARS Children׳s Nutrition Research Center, Department of Pediatrics, Houston, TX 77030</wicri:regionArea><placeName><region type="state">Texas</region></placeName></affiliation></author><author><name sortKey="Cui, Xiaojiang" sort="Cui, Xiaojiang" uniqKey="Cui X" first="Xiaojiang" last="Cui">Xiaojiang Cui</name><affiliation wicri:level="2"><nlm:affiliation>Department of Surgery and Department of Obstetrics and Gynecology, Samuel Oschin Comprehensive Cancer Institute, Cedars Sinai Medical Center, Los Angeles, CA 90048, USA. 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Rodney</name><affiliation wicri:level="2"><nlm:affiliation>Department of Molecular Physiology & Biophysics, Baylor College of Medicine, Houston, TX 77030, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular Physiology & Biophysics, Baylor College of Medicine, Houston, TX 77030</wicri:regionArea><placeName><region type="state">Texas</region></placeName></affiliation></author><author><name sortKey="Cheng, Ninghui" sort="Cheng, Ninghui" uniqKey="Cheng N" first="Ninghui" last="Cheng">Ninghui Cheng</name><affiliation wicri:level="2"><nlm:affiliation>USDA/ARS Children׳s Nutrition Research Center, Department of Pediatrics, Houston, TX 77030, USA. 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Shiao</name><affiliation wicri:level="2"><nlm:affiliation>Radiation Oncology and Biochemical Sciences, Cedars Sinai Medical Center, Los Angeles, CA 90048, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Radiation Oncology and Biochemical Sciences, Cedars Sinai Medical Center, Los Angeles, CA 90048</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author><author><name sortKey="Wang, Xinquan" sort="Wang, Xinquan" uniqKey="Wang X" first="Xinquan" last="Wang">Xinquan Wang</name><affiliation wicri:level="1"><nlm:affiliation>Ministry of Education Key Laboratory of Protein Science, Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Ministry of Education Key Laboratory of Protein Science, Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></author><author><name sortKey="O Brian Smith, E" sort="O Brian Smith, E" uniqKey="O Brian Smith E" first="E" last="O'Brian Smith">E. O'Brian Smith</name><affiliation wicri:level="2"><nlm:affiliation>USDA/ARS Children׳s Nutrition Research Center, Department of Pediatrics, Houston, TX 77030, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>USDA/ARS Children׳s Nutrition Research Center, Department of Pediatrics, Houston, TX 77030</wicri:regionArea><placeName><region type="state">Texas</region></placeName></affiliation></author><author><name sortKey="Cui, Xiaojiang" sort="Cui, Xiaojiang" uniqKey="Cui X" first="Xiaojiang" last="Cui">Xiaojiang Cui</name><affiliation wicri:level="2"><nlm:affiliation>Department of Surgery and Department of Obstetrics and Gynecology, Samuel Oschin Comprehensive Cancer Institute, Cedars Sinai Medical Center, Los Angeles, CA 90048, USA. Electronic address: Xiaojiang.Cui@cshs.org.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Surgery and Department of Obstetrics and Gynecology, Samuel Oschin Comprehensive Cancer Institute, Cedars Sinai Medical Center, Los Angeles, CA 90048</wicri:regionArea><placeName><region type="state">Californie</region></placeName></affiliation></author><author><name sortKey="Rodney, George G" sort="Rodney, George G" uniqKey="Rodney G" first="George G" last="Rodney">George G. Rodney</name><affiliation wicri:level="2"><nlm:affiliation>Department of Molecular Physiology & Biophysics, Baylor College of Medicine, Houston, TX 77030, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular Physiology & Biophysics, Baylor College of Medicine, Houston, TX 77030</wicri:regionArea><placeName><region type="state">Texas</region></placeName></affiliation></author><author><name sortKey="Cheng, Ninghui" sort="Cheng, Ninghui" uniqKey="Cheng N" first="Ninghui" last="Cheng">Ninghui Cheng</name><affiliation wicri:level="2"><nlm:affiliation>USDA/ARS Children׳s Nutrition Research Center, Department of Pediatrics, Houston, TX 77030, USA. Electronic address: ncheng@bcm.edu.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>USDA/ARS Children׳s Nutrition Research Center, Department of Pediatrics, Houston, TX 77030</wicri:regionArea><placeName><region type="state">Texas</region></placeName></affiliation></author></analytic><series><title level="j">Free radical biology & medicine</title><idno type="eISSN">1873-4596</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Carrier Proteins (metabolism)</term><term>Cell Line, Tumor (MeSH)</term><term>Cell Nucleus (metabolism)</term><term>Humans (MeSH)</term><term>Oxidative Stress (MeSH)</term><term>Reactive Oxygen Species (metabolism)</term><term>Subcellular Fractions (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Espèces réactives de l'oxygène (métabolisme)</term><term>Fractions subcellulaires (métabolisme)</term><term>Humains (MeSH)</term><term>Lignée cellulaire tumorale (MeSH)</term><term>Noyau de la cellule (métabolisme)</term><term>Protéines de transport (métabolisme)</term><term>Stress oxydatif (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carrier Proteins</term><term>Reactive Oxygen Species</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Nucleus</term><term>Subcellular Fractions</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Espèces réactives de l'oxygène</term><term>Fractions subcellulaires</term><term>Noyau de la cellule</term><term>Protéines de transport</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line, Tumor</term><term>Humans</term><term>Oxidative Stress</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term><term>Lignée cellulaire tumorale</term><term>Stress oxydatif</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Mammalian glutaredoxin 3 (Grx3) has been shown to be critical in maintaining redox homeostasis and regulating cell survival pathways in cancer cells. However, the regulation of Grx3 is not fully understood. In the present study, we investigate the subcellular localization of Grx3 under normal growth and oxidative stress conditions. Both fluorescence imaging of Grx3-RFP fusion and Western blot analysis of cellular fractionation indicate that Grx3 is predominantly localized in the cytoplasm under normal growth conditions, whereas under oxidizing conditions, Grx3 is translocated into and accumulated in the nucleus. Grx3 nuclear accumulation was reversible in a redox-dependent fashion. Further analysis indicates that neither the N-terminal Trx-like domain nor the two catalytic cysteine residues in the active CGFS motif of Grx3 are involved in its nuclear translocation. Decreased levels of Grx3 render cells susceptible to cellular oxidative stress, whereas overexpression of nuclear-targeted Grx3 is sufficient to suppress cells' sensitivity to oxidant treatments and reduce reactive oxygen species production. These findings provide novel insights into the regulation of Grx3, which is crucial for cell survival against environmental insults. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25975981</PMID><DateCompleted><Year>2016</Year><Month>05</Month><Day>26</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-4596</ISSN><JournalIssue CitedMedium="Internet"><Volume>85</Volume><PubDate><Year>2015</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Free radical biology & medicine</Title><ISOAbbreviation>Free Radic Biol Med</ISOAbbreviation></Journal><ArticleTitle>Nuclear glutaredoxin 3 is critical for protection against oxidative stress-induced cell death.</ArticleTitle><Pagination><MedlinePgn>197-206</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.freeradbiomed.2015.05.003</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0891-5849(15)00209-9</ELocationID><Abstract><AbstractText>Mammalian glutaredoxin 3 (Grx3) has been shown to be critical in maintaining redox homeostasis and regulating cell survival pathways in cancer cells. However, the regulation of Grx3 is not fully understood. In the present study, we investigate the subcellular localization of Grx3 under normal growth and oxidative stress conditions. Both fluorescence imaging of Grx3-RFP fusion and Western blot analysis of cellular fractionation indicate that Grx3 is predominantly localized in the cytoplasm under normal growth conditions, whereas under oxidizing conditions, Grx3 is translocated into and accumulated in the nucleus. Grx3 nuclear accumulation was reversible in a redox-dependent fashion. Further analysis indicates that neither the N-terminal Trx-like domain nor the two catalytic cysteine residues in the active CGFS motif of Grx3 are involved in its nuclear translocation. Decreased levels of Grx3 render cells susceptible to cellular oxidative stress, whereas overexpression of nuclear-targeted Grx3 is sufficient to suppress cells' sensitivity to oxidant treatments and reduce reactive oxygen species production. These findings provide novel insights into the regulation of Grx3, which is crucial for cell survival against environmental insults. </AbstractText><CopyrightInformation>Copyright © 2015 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Pham</LastName><ForeName>Khanh</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>USDA/ARS Children׳s Nutrition Research Center, Department of Pediatrics, Houston, TX 77030, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pal</LastName><ForeName>Rituraj</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Molecular Physiology & Biophysics, Baylor College of Medicine, Houston, TX 77030, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Qu</LastName><ForeName>Ying</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Surgery and Department of Obstetrics and Gynecology, Samuel Oschin Comprehensive Cancer Institute, Cedars Sinai Medical Center, Los Angeles, CA 90048, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Xi</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>Ministry of Education Key Laboratory of Protein Science, Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yu</LastName><ForeName>Han</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>USDA/ARS Children׳s Nutrition Research Center, Department of Pediatrics, Houston, TX 77030, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shiao</LastName><ForeName>Stephen L</ForeName><Initials>SL</Initials><AffiliationInfo><Affiliation>Radiation Oncology and Biochemical Sciences, Cedars Sinai Medical Center, Los Angeles, CA 90048, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Xinquan</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>Ministry of Education Key Laboratory of Protein Science, Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>O'Brian Smith</LastName><ForeName>E</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>USDA/ARS Children׳s Nutrition Research Center, Department of Pediatrics, Houston, TX 77030, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cui</LastName><ForeName>Xiaojiang</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>Department of Surgery and Department of Obstetrics and Gynecology, Samuel Oschin Comprehensive Cancer Institute, Cedars Sinai Medical Center, Los Angeles, CA 90048, USA. Electronic address: Xiaojiang.Cui@cshs.org.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rodney</LastName><ForeName>George G</ForeName><Initials>GG</Initials><AffiliationInfo><Affiliation>Department of Molecular Physiology & Biophysics, Baylor College of Medicine, Houston, TX 77030, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cheng</LastName><ForeName>Ninghui</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>USDA/ARS Children׳s Nutrition Research Center, Department of Pediatrics, Houston, TX 77030, USA. Electronic address: ncheng@bcm.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 AR061370</GrantID><Acronym>AR</Acronym><Agency>NIAMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 CA151610</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>CA151610</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01AR061370</GrantID><Acronym>AR</Acronym><Agency>NIAMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>05</Month><Day>11</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Free Radic Biol Med</MedlineTA><NlmUniqueID>8709159</NlmUniqueID><ISSNLinking>0891-5849</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002352">Carrier Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C404105">GLRX3 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017382">Reactive Oxygen Species</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002352" MajorTopicYN="N">Carrier Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045744" MajorTopicYN="N">Cell Line, Tumor</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002467" MajorTopicYN="N">Cell Nucleus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="Y">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017382" MajorTopicYN="N">Reactive Oxygen Species</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013347" MajorTopicYN="N">Subcellular Fractions</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Cell death</Keyword><Keyword MajorTopicYN="N">Free radicals</Keyword><Keyword 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Pham</name></region><name sortKey="Cheng, Ninghui" sort="Cheng, Ninghui" uniqKey="Cheng N" first="Ninghui" last="Cheng">Ninghui Cheng</name><name sortKey="Cui, Xiaojiang" sort="Cui, Xiaojiang" uniqKey="Cui X" first="Xiaojiang" last="Cui">Xiaojiang Cui</name><name sortKey="O Brian Smith, E" sort="O Brian Smith, E" uniqKey="O Brian Smith E" first="E" last="O'Brian Smith">E. O'Brian Smith</name><name sortKey="Pal, Rituraj" sort="Pal, Rituraj" uniqKey="Pal R" first="Rituraj" last="Pal">Rituraj Pal</name><name sortKey="Qu, Ying" sort="Qu, Ying" uniqKey="Qu Y" first="Ying" last="Qu">Ying Qu</name><name sortKey="Rodney, George G" sort="Rodney, George G" uniqKey="Rodney G" first="George G" last="Rodney">George G. Rodney</name><name sortKey="Shiao, Stephen L" sort="Shiao, Stephen L" uniqKey="Shiao S" first="Stephen L" last="Shiao">Stephen L. Shiao</name><name sortKey="Yu, Han" sort="Yu, Han" uniqKey="Yu H" first="Han" last="Yu">Han Yu</name></country><country name="République populaire de Chine"><noRegion><name sortKey="Liu, Xi" sort="Liu, Xi" uniqKey="Liu X" first="Xi" last="Liu">Xi Liu</name></noRegion><name sortKey="Wang, Xinquan" sort="Wang, Xinquan" uniqKey="Wang X" first="Xinquan" last="Wang">Xinquan Wang</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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