Role of glutaredoxin in metabolic oxidative stress. Glutaredoxin as a sensor of oxidative stress mediated by H2O2.
Identifieur interne : 000F70 ( Main/Exploration ); précédent : 000F69; suivant : 000F71Role of glutaredoxin in metabolic oxidative stress. Glutaredoxin as a sensor of oxidative stress mediated by H2O2.
Auteurs : Jae J. Song [États-Unis] ; Juong G. Rhee ; Mohan Suntharalingam ; Susan A. Walsh ; Douglas R. Spitz ; Yong J. LeeSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2002.
Descripteurs français
- KwdFr :
- Acétylcystéine (pharmacologie), Amorces ADN (MeSH), Cellules cancéreuses en culture (MeSH), Glucose (métabolisme), Glutarédoxines (MeSH), Humains (MeSH), Modèles théoriques (MeSH), Oxidoreductases (MeSH), Peroxyde d'hydrogène (pharmacologie), Protéines (génétique), Protéines (physiologie), Stress oxydatif (physiologie), Système de signalisation des MAP kinases (MeSH), Séquence nucléotidique (MeSH), Transduction du signal (physiologie).
- MESH :
- génétique : Protéines.
- métabolisme : Glucose.
- pharmacologie : Acétylcystéine, Peroxyde d'hydrogène.
- physiologie : Protéines, Stress oxydatif, Transduction du signal.
- Amorces ADN, Cellules cancéreuses en culture, Glutarédoxines, Humains, Modèles théoriques, Oxidoreductases, Système de signalisation des MAP kinases, Séquence nucléotidique.
English descriptors
- KwdEn :
- Acetylcysteine (pharmacology), Base Sequence (MeSH), DNA Primers (MeSH), Glucose (metabolism), Glutaredoxins (MeSH), Humans (MeSH), Hydrogen Peroxide (pharmacology), MAP Kinase Signaling System (MeSH), Models, Theoretical (MeSH), Oxidative Stress (physiology), Oxidoreductases (MeSH), Proteins (genetics), Proteins (physiology), Signal Transduction (physiology), Tumor Cells, Cultured (MeSH).
- MESH :
- chemical , genetics : Proteins.
- chemical , metabolism : Glucose.
- chemical , pharmacology : Acetylcysteine, Hydrogen Peroxide.
- physiology : Oxidative Stress, Proteins, Signal Transduction.
- Base Sequence, DNA Primers, Glutaredoxins, Humans, MAP Kinase Signaling System, Models, Theoretical, Oxidoreductases, Tumor Cells, Cultured.
Abstract
Epitope-tagged glutaredoxin (GRX) was utilized to determine the role of GRX in oxidative stress-induced signaling and cytotoxicity in glucose-deprived human cancer cells (MCF-7/ADR and DU-145). GRX-overexpressing cells demonstrated resistance to glucose deprivation-induced cytotoxicity and decreased activation of c-Jun N-terminal kinase (JNK1). Deletion mutants showed the C-terminal portion of apoptosis signal-regulating kinase 1 (ASK1) bound GRX, and glucose deprivation disrupted binding. Treatment with l-buthionine-(S,R)-sulfoximine reduced glutathione content by 99% and prevented glucose deprivation-induced dissociation of GRX from ASK1. A thiol antioxidant, N-acetyl-l-cysteine, or overexpression of an H(2)O(2) scavenger, catalase, inhibited glucose deprivation-induced dissociation of GRX from ASK1. GRX active site cysteine residues (Cys(22) and Cys(25)) were required for dissociation of GRX from ASK1 during glucose deprivation. Kinase assays revealed that SEK1 and JNK1 were regulated in an ASK1-dependent fashion during glucose deprivation. Overexpression of GRX or catalase inhibited activation of ASK1-SEK1-JNK1 signaling during glucose deprivation. These results demonstrate that GRX is a negative regulator of ASK1 and dissociation of GRX from ASK1 activates ASK1-SEK1-JNK1 signaling leading to cytotoxicity during glucose deprivation. These results support the hypothesis that the GRX-ASK1 interaction is redox sensitive and regulated in a glutathione-dependent fashion by H(2)O(2).
DOI: 10.1074/jbc.M206826200
PubMed: 12244106
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Rhee</name></author><author><name sortKey="Suntharalingam, Mohan" sort="Suntharalingam, Mohan" uniqKey="Suntharalingam M" first="Mohan" last="Suntharalingam">Mohan Suntharalingam</name></author><author><name sortKey="Walsh, Susan A" sort="Walsh, Susan A" uniqKey="Walsh S" first="Susan A" last="Walsh">Susan A. Walsh</name></author><author><name sortKey="Spitz, Douglas R" sort="Spitz, Douglas R" uniqKey="Spitz D" first="Douglas R" last="Spitz">Douglas R. Spitz</name></author><author><name sortKey="Lee, Yong J" sort="Lee, Yong J" uniqKey="Lee Y" first="Yong J" last="Lee">Yong J. Lee</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2002">2002</date><idno type="RBID">pubmed:12244106</idno><idno type="pmid">12244106</idno><idno type="doi">10.1074/jbc.M206826200</idno><idno type="wicri:Area/Main/Corpus">000F67</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000F67</idno><idno type="wicri:Area/Main/Curation">000F67</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000F67</idno><idno type="wicri:Area/Main/Exploration">000F67</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Role of glutaredoxin in metabolic oxidative stress. Glutaredoxin as a sensor of oxidative stress mediated by H2O2.</title><author><name sortKey="Song, Jae J" sort="Song, Jae J" uniqKey="Song J" first="Jae J" last="Song">Jae J. Song</name><affiliation wicri:level="4"><nlm:affiliation>Department of Surgery and Cancer Institute, University of Pittsburgh, Pittsburgh, Pennsylvania 15232, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Surgery and Cancer Institute, University of Pittsburgh, Pittsburgh, Pennsylvania 15232</wicri:regionArea><orgName type="university">Université de Pittsburgh</orgName><placeName><settlement type="city">Pittsburgh</settlement><region type="state">Pennsylvanie</region></placeName></affiliation></author><author><name sortKey="Rhee, Juong G" sort="Rhee, Juong G" uniqKey="Rhee J" first="Juong G" last="Rhee">Juong G. Rhee</name></author><author><name sortKey="Suntharalingam, Mohan" sort="Suntharalingam, Mohan" uniqKey="Suntharalingam M" first="Mohan" last="Suntharalingam">Mohan Suntharalingam</name></author><author><name sortKey="Walsh, Susan A" sort="Walsh, Susan A" uniqKey="Walsh S" first="Susan A" last="Walsh">Susan A. Walsh</name></author><author><name sortKey="Spitz, Douglas R" sort="Spitz, Douglas R" uniqKey="Spitz D" first="Douglas R" last="Spitz">Douglas R. Spitz</name></author><author><name sortKey="Lee, Yong J" sort="Lee, Yong J" uniqKey="Lee Y" first="Yong J" last="Lee">Yong J. Lee</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2002" type="published">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acetylcysteine (pharmacology)</term><term>Base Sequence (MeSH)</term><term>DNA Primers (MeSH)</term><term>Glucose (metabolism)</term><term>Glutaredoxins (MeSH)</term><term>Humans (MeSH)</term><term>Hydrogen Peroxide (pharmacology)</term><term>MAP Kinase Signaling System (MeSH)</term><term>Models, Theoretical (MeSH)</term><term>Oxidative Stress (physiology)</term><term>Oxidoreductases (MeSH)</term><term>Proteins (genetics)</term><term>Proteins (physiology)</term><term>Signal Transduction (physiology)</term><term>Tumor Cells, Cultured (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acétylcystéine (pharmacologie)</term><term>Amorces ADN (MeSH)</term><term>Cellules cancéreuses en culture (MeSH)</term><term>Glucose (métabolisme)</term><term>Glutarédoxines (MeSH)</term><term>Humains (MeSH)</term><term>Modèles théoriques (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Peroxyde d'hydrogène (pharmacologie)</term><term>Protéines (génétique)</term><term>Protéines (physiologie)</term><term>Stress oxydatif (physiologie)</term><term>Système de signalisation des MAP kinases (MeSH)</term><term>Séquence nucléotidique (MeSH)</term><term>Transduction du signal (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glucose</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Acetylcysteine</term><term>Hydrogen Peroxide</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glucose</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Acétylcystéine</term><term>Peroxyde d'hydrogène</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Protéines</term><term>Stress oxydatif</term><term>Transduction du signal</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Oxidative Stress</term><term>Proteins</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Base Sequence</term><term>DNA Primers</term><term>Glutaredoxins</term><term>Humans</term><term>MAP Kinase Signaling System</term><term>Models, Theoretical</term><term>Oxidoreductases</term><term>Tumor Cells, Cultured</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Amorces ADN</term><term>Cellules cancéreuses en culture</term><term>Glutarédoxines</term><term>Humains</term><term>Modèles théoriques</term><term>Oxidoreductases</term><term>Système de signalisation des MAP kinases</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Epitope-tagged glutaredoxin (GRX) was utilized to determine the role of GRX in oxidative stress-induced signaling and cytotoxicity in glucose-deprived human cancer cells (MCF-7/ADR and DU-145). GRX-overexpressing cells demonstrated resistance to glucose deprivation-induced cytotoxicity and decreased activation of c-Jun N-terminal kinase (JNK1). Deletion mutants showed the C-terminal portion of apoptosis signal-regulating kinase 1 (ASK1) bound GRX, and glucose deprivation disrupted binding. Treatment with l-buthionine-(S,R)-sulfoximine reduced glutathione content by 99% and prevented glucose deprivation-induced dissociation of GRX from ASK1. A thiol antioxidant, N-acetyl-l-cysteine, or overexpression of an H(2)O(2) scavenger, catalase, inhibited glucose deprivation-induced dissociation of GRX from ASK1. GRX active site cysteine residues (Cys(22) and Cys(25)) were required for dissociation of GRX from ASK1 during glucose deprivation. Kinase assays revealed that SEK1 and JNK1 were regulated in an ASK1-dependent fashion during glucose deprivation. Overexpression of GRX or catalase inhibited activation of ASK1-SEK1-JNK1 signaling during glucose deprivation. These results demonstrate that GRX is a negative regulator of ASK1 and dissociation of GRX from ASK1 activates ASK1-SEK1-JNK1 signaling leading to cytotoxicity during glucose deprivation. These results support the hypothesis that the GRX-ASK1 interaction is redox sensitive and regulated in a glutathione-dependent fashion by H(2)O(2).</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12244106</PMID><DateCompleted><Year>2003</Year><Month>01</Month><Day>08</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>277</Volume><Issue>48</Issue><PubDate><Year>2002</Year><Month>Nov</Month><Day>29</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Role of glutaredoxin in metabolic oxidative stress. Glutaredoxin as a sensor of oxidative stress mediated by H2O2.</ArticleTitle><Pagination><MedlinePgn>46566-75</MedlinePgn></Pagination><Abstract><AbstractText>Epitope-tagged glutaredoxin (GRX) was utilized to determine the role of GRX in oxidative stress-induced signaling and cytotoxicity in glucose-deprived human cancer cells (MCF-7/ADR and DU-145). GRX-overexpressing cells demonstrated resistance to glucose deprivation-induced cytotoxicity and decreased activation of c-Jun N-terminal kinase (JNK1). Deletion mutants showed the C-terminal portion of apoptosis signal-regulating kinase 1 (ASK1) bound GRX, and glucose deprivation disrupted binding. Treatment with l-buthionine-(S,R)-sulfoximine reduced glutathione content by 99% and prevented glucose deprivation-induced dissociation of GRX from ASK1. A thiol antioxidant, N-acetyl-l-cysteine, or overexpression of an H(2)O(2) scavenger, catalase, inhibited glucose deprivation-induced dissociation of GRX from ASK1. GRX active site cysteine residues (Cys(22) and Cys(25)) were required for dissociation of GRX from ASK1 during glucose deprivation. Kinase assays revealed that SEK1 and JNK1 were regulated in an ASK1-dependent fashion during glucose deprivation. Overexpression of GRX or catalase inhibited activation of ASK1-SEK1-JNK1 signaling during glucose deprivation. These results demonstrate that GRX is a negative regulator of ASK1 and dissociation of GRX from ASK1 activates ASK1-SEK1-JNK1 signaling leading to cytotoxicity during glucose deprivation. These results support the hypothesis that the GRX-ASK1 interaction is redox sensitive and regulated in a glutathione-dependent fashion by H(2)O(2).</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Song</LastName><ForeName>Jae J</ForeName><Initials>JJ</Initials><AffiliationInfo><Affiliation>Department of Surgery and Cancer Institute, University of Pittsburgh, Pittsburgh, Pennsylvania 15232, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rhee</LastName><ForeName>Juong G</ForeName><Initials>JG</Initials></Author><Author ValidYN="Y"><LastName>Suntharalingam</LastName><ForeName>Mohan</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Walsh</LastName><ForeName>Susan A</ForeName><Initials>SA</Initials></Author><Author ValidYN="Y"><LastName>Spitz</LastName><ForeName>Douglas R</ForeName><Initials>DR</Initials></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Yong J</ForeName><Initials>YJ</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>CA48000</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>CA66081</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>HL51469</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2002</Year><Month>09</Month><Day>19</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol 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MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020935" MajorTopicYN="N">MAP Kinase Signaling System</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008962" MajorTopicYN="N">Models, Theoretical</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014407" MajorTopicYN="N">Tumor Cells, Cultured</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>9</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2003</Year><Month>1</Month><Day>9</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>9</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12244106</ArticleId><ArticleId IdType="doi">10.1074/jbc.M206826200</ArticleId><ArticleId IdType="pii">M206826200</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Pennsylvanie</li></region><settlement><li>Pittsburgh</li></settlement><orgName><li>Université de Pittsburgh</li></orgName></list><tree><noCountry><name sortKey="Lee, Yong J" sort="Lee, Yong J" uniqKey="Lee Y" first="Yong J" last="Lee">Yong J. Lee</name><name sortKey="Rhee, Juong G" sort="Rhee, Juong G" uniqKey="Rhee J" first="Juong G" last="Rhee">Juong G. Rhee</name><name sortKey="Spitz, Douglas R" sort="Spitz, Douglas R" uniqKey="Spitz D" first="Douglas R" last="Spitz">Douglas R. Spitz</name><name sortKey="Suntharalingam, Mohan" sort="Suntharalingam, Mohan" uniqKey="Suntharalingam M" first="Mohan" last="Suntharalingam">Mohan Suntharalingam</name><name sortKey="Walsh, Susan A" sort="Walsh, Susan A" uniqKey="Walsh S" first="Susan A" last="Walsh">Susan A. Walsh</name></noCountry><country name="États-Unis"><region name="Pennsylvanie"><name sortKey="Song, Jae J" sort="Song, Jae J" uniqKey="Song J" first="Jae J" last="Song">Jae J. Song</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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