Nuclear redox signaling.
Identifieur interne : 000A13 ( Main/Exploration ); précédent : 000A12; suivant : 000A14Nuclear redox signaling.
Auteurs : Margarete Lukosz [Allemagne] ; Sascha Jakob ; Nicole Büchner ; Tim-Christian Zschauer ; Joachim Altschmied ; Judith HaendelerSource :
- Antioxidants & redox signaling [ 1557-7716 ] ; 2010.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Noyau de la cellule.
- métabolisme : Espèces réactives de l'oxygène, Facteurs de transcription, Noyau de la cellule.
- Animaux, Humains, Oxydoréduction, Transduction du signal.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Reactive Oxygen Species, Transcription Factors.
- enzymology : Cell Nucleus.
- metabolism : Cell Nucleus.
- Animals, Humans, Oxidation-Reduction, Signal Transduction.
Abstract
Reactive oxygen species have been described to modulate proteins within the cell, a process called redox regulation. However, the importance of compartment-specific redox regulation has been neglected for a long time. In the early 1980s and 1990s, many in vitro studies introduced the possibility that nuclear redox signaling exists. However, the functional relevance for that has been greatly disregarded. Recently, it has become evident that nuclear redox signaling is indeed one important signaling mechanism regulating a variety of cellular functions. Transcription factors, and even kinases and phosphatases, have been described to be redox regulated in the nucleus. This review describes several of these proteins in closer detail and explains their functions resulting from nuclear localization and redox regulation. Moreover, the redox state of the nucleus and several important nuclear redox regulators [Thioredoxin-1 (Trx-1), Glutaredoxins (Grxs), Peroxiredoxins (Prxs), and APEX nuclease (multifunctional DNA-repair enzyme) 1 (APEX1)] are introduced more precisely, and their necessity for regulation of transcription factors is emphasized.
DOI: 10.1089/ars.2009.2609
PubMed: 19737086
Affiliations:
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uniqKey="Jakob S" first="Sascha" last="Jakob">Sascha Jakob</name></author><author><name sortKey="Buchner, Nicole" sort="Buchner, Nicole" uniqKey="Buchner N" first="Nicole" last="Büchner">Nicole Büchner</name></author><author><name sortKey="Zschauer, Tim Christian" sort="Zschauer, Tim Christian" uniqKey="Zschauer T" first="Tim-Christian" last="Zschauer">Tim-Christian Zschauer</name></author><author><name sortKey="Altschmied, Joachim" sort="Altschmied, Joachim" uniqKey="Altschmied J" first="Joachim" last="Altschmied">Joachim Altschmied</name></author><author><name sortKey="Haendeler, Judith" sort="Haendeler, Judith" uniqKey="Haendeler J" first="Judith" last="Haendeler">Judith Haendeler</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2010">2010</date><idno type="RBID">pubmed:19737086</idno><idno type="pmid">19737086</idno><idno type="doi">10.1089/ars.2009.2609</idno><idno type="wicri:Area/Main/Corpus">000A78</idno><idno type="wicri:explorRef" 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(MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Reactive Oxygen Species</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Noyau de la cellule</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Cell Nucleus</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Nucleus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Espèces réactives de l'oxygène</term><term>Facteurs de transcription</term><term>Noyau de la cellule</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term><term>Oxidation-Reduction</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Humains</term><term>Oxydoréduction</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Reactive oxygen species have been described to modulate proteins within the cell, a process called redox regulation. However, the importance of compartment-specific redox regulation has been neglected for a long time. In the early 1980s and 1990s, many in vitro studies introduced the possibility that nuclear redox signaling exists. However, the functional relevance for that has been greatly disregarded. Recently, it has become evident that nuclear redox signaling is indeed one important signaling mechanism regulating a variety of cellular functions. Transcription factors, and even kinases and phosphatases, have been described to be redox regulated in the nucleus. This review describes several of these proteins in closer detail and explains their functions resulting from nuclear localization and redox regulation. Moreover, the redox state of the nucleus and several important nuclear redox regulators [Thioredoxin-1 (Trx-1), Glutaredoxins (Grxs), Peroxiredoxins (Prxs), and APEX nuclease (multifunctional DNA-repair enzyme) 1 (APEX1)] are introduced more precisely, and their necessity for regulation of transcription factors is emphasized.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19737086</PMID><DateCompleted><Year>2010</Year><Month>10</Month><Day>25</Day></DateCompleted><DateRevised><Year>2010</Year><Month>03</Month><Day>01</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1557-7716</ISSN><JournalIssue CitedMedium="Internet"><Volume>12</Volume><Issue>6</Issue><PubDate><Year>2010</Year><Month>Mar</Month><Day>15</Day></PubDate></JournalIssue><Title>Antioxidants & redox signaling</Title><ISOAbbreviation>Antioxid Redox Signal</ISOAbbreviation></Journal><ArticleTitle>Nuclear redox signaling.</ArticleTitle><Pagination><MedlinePgn>713-42</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1089/ars.2009.2609</ELocationID><Abstract><AbstractText>Reactive oxygen species have been described to modulate proteins within the cell, a process called redox regulation. However, the importance of compartment-specific redox regulation has been neglected for a long time. In the early 1980s and 1990s, many in vitro studies introduced the possibility that nuclear redox signaling exists. However, the functional relevance for that has been greatly disregarded. Recently, it has become evident that nuclear redox signaling is indeed one important signaling mechanism regulating a variety of cellular functions. Transcription factors, and even kinases and phosphatases, have been described to be redox regulated in the nucleus. This review describes several of these proteins in closer detail and explains their functions resulting from nuclear localization and redox regulation. Moreover, the redox state of the nucleus and several important nuclear redox regulators [Thioredoxin-1 (Trx-1), Glutaredoxins (Grxs), Peroxiredoxins (Prxs), and APEX nuclease (multifunctional DNA-repair enzyme) 1 (APEX1)] are introduced more precisely, and their necessity for regulation of transcription factors is emphasized.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lukosz</LastName><ForeName>Margarete</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Molecular Cell & Aging Research, IUF (Institute for Molecular Preventive Medicine), At the University of Duesseldorf gGmbH, Auf'm Hennekamp 50, 40225 Duesseldorf, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jakob</LastName><ForeName>Sascha</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Büchner</LastName><ForeName>Nicole</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Zschauer</LastName><ForeName>Tim-Christian</ForeName><Initials>TC</Initials></Author><Author ValidYN="Y"><LastName>Altschmied</LastName><ForeName>Joachim</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Haendeler</LastName><ForeName>Judith</ForeName><Initials>J</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Antioxid Redox Signal</MedlineTA><NlmUniqueID>100888899</NlmUniqueID><ISSNLinking>1523-0864</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017382">Reactive Oxygen Species</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014157">Transcription Factors</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002467" MajorTopicYN="N">Cell Nucleus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017382" MajorTopicYN="N">Reactive Oxygen Species</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="Y">Signal Transduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014157" MajorTopicYN="N">Transcription Factors</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><NumberOfReferences>263</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>9</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>9</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2010</Year><Month>10</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19737086</ArticleId><ArticleId IdType="doi">10.1089/ars.2009.2609</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country><region><li>District de Düsseldorf</li><li>Rhénanie-du-Nord-Westphalie</li></region><settlement><li>Düsseldorf</li></settlement></list><tree><noCountry><name sortKey="Altschmied, Joachim" sort="Altschmied, Joachim" uniqKey="Altschmied J" first="Joachim" last="Altschmied">Joachim Altschmied</name><name sortKey="Buchner, Nicole" sort="Buchner, Nicole" uniqKey="Buchner N" first="Nicole" last="Büchner">Nicole Büchner</name><name sortKey="Haendeler, Judith" sort="Haendeler, Judith" uniqKey="Haendeler J" first="Judith" last="Haendeler">Judith Haendeler</name><name sortKey="Jakob, Sascha" sort="Jakob, Sascha" uniqKey="Jakob S" first="Sascha" last="Jakob">Sascha Jakob</name><name sortKey="Zschauer, Tim Christian" sort="Zschauer, Tim Christian" uniqKey="Zschauer T" first="Tim-Christian" last="Zschauer">Tim-Christian Zschauer</name></noCountry><country name="Allemagne"><region name="Rhénanie-du-Nord-Westphalie"><name sortKey="Lukosz, Margarete" sort="Lukosz, Margarete" uniqKey="Lukosz M" first="Margarete" last="Lukosz">Margarete Lukosz</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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