Glutaredoxin 2 reduces both thioredoxin 2 and thioredoxin 1 and protects cells from apoptosis induced by auranofin and 4-hydroxynonenal.
Identifieur interne : 000654 ( Main/Exploration ); précédent : 000653; suivant : 000655Glutaredoxin 2 reduces both thioredoxin 2 and thioredoxin 1 and protects cells from apoptosis induced by auranofin and 4-hydroxynonenal.
Auteurs : Huihui Zhang [Suède] ; Yatao Du ; Xu Zhang ; Jun Lu ; Arne HolmgrenSource :
- Antioxidants & redox signaling [ 1557-7716 ] ; 2014.
Descripteurs français
- KwdFr :
- Aldéhydes (pharmacologie), Apoptose (effets des médicaments et des substances chimiques), Auranofine (pharmacologie), Cellules HeLa (MeSH), Glutarédoxines (métabolisme), Humains (MeSH), Oxydoréduction (MeSH), Protéines mitochondriales (métabolisme), Relation dose-effet des médicaments (MeSH), Relation structure-activité (MeSH), Stress oxydatif (MeSH), Thioredoxin-disulfide reductase (métabolisme), Thiorédoxines (métabolisme).
- MESH :
- effets des médicaments et des substances chimiques : Apoptose.
- métabolisme : Glutarédoxines, Protéines mitochondriales, Thioredoxin-disulfide reductase, Thiorédoxines.
- pharmacologie : Aldéhydes, Auranofine.
- Cellules HeLa, Humains, Oxydoréduction, Relation dose-effet des médicaments, Relation structure-activité, Stress oxydatif.
English descriptors
- KwdEn :
- Aldehydes (pharmacology), Apoptosis (drug effects), Auranofin (pharmacology), Dose-Response Relationship, Drug (MeSH), Glutaredoxins (metabolism), HeLa Cells (MeSH), Humans (MeSH), Mitochondrial Proteins (metabolism), Oxidation-Reduction (MeSH), Oxidative Stress (MeSH), Structure-Activity Relationship (MeSH), Thioredoxin-Disulfide Reductase (metabolism), Thioredoxins (metabolism).
- MESH :
- chemical , metabolism : Glutaredoxins, Mitochondrial Proteins, Thioredoxin-Disulfide Reductase, Thioredoxins.
- chemical , pharmacology : Aldehydes, Auranofin.
- drug effects : Apoptosis.
- Dose-Response Relationship, Drug, HeLa Cells, Humans, Oxidation-Reduction, Oxidative Stress, Structure-Activity Relationship.
Abstract
AIMS
Mitochondrial thioredoxin (Trx) is critical for defense against oxidative stress-induced cell apoptosis. To date, mitochondrial thioredoxin reductase (TrxR) is the only known enzyme catalyzing Trx2 reduction in mitochondria. However, TrxR is sensitive to inactivation by exo/endogenous electrophiles, for example, 4-hydroxynonenal (HNE). In this study, we characterized the mitochondrial glutaredoxin 2 (Grx2) system as a backup for the mitochondrial TrxR. Meanwhile, as Grx2 is also present in the cytosol/nucleus of certain cancer cell lines, the reducing activity of Grx2 on Trx1 was also tested.
RESULTS
Glutathione alone could reduce oxidized Trx2, and the presence of physiological concentrations of Grx2 markedly increased the reaction rate. HeLa cells with Grx2 overexpression (particularly in the mitochondria) exhibited higher viabilities than the wild-type cells after treatment with TrxR inhibitors (Auranofin or HNE), whereas knockdown of Grx2 sensitized the cells to TrxR inhibitors. Accordingly, Grx2 overexpression in the mitochondria had protected Trx2 from oxidation by HNE treatment, whereas Grx2 knockdown had sensitized Trx2 to oxidation. On the other hand, Grx2 reduced Trx1 with similar activities as that of Trx2. Overexpression of Grx2 in the cytosol had protected Trx1 from oxidation, indicating a supportive role of Grx2 in the cytosolic redox balance of cancer cells.
INNOVATION
This work explores the reductase activity of Grx2 on Trx2/1, and demonstrates the physiological importance of the activity by using in vivo redox western blot assays.
CONCLUSION
Grx2 system could help to keep Trx2/1 reduced during an oxidative stress, thereby contributing to the anti-apoptotic signaling.
DOI: 10.1089/ars.2013.5499
PubMed: 24295294
PubMed Central: PMC4098818
Affiliations:
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Le document en format XML
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uniqKey="Zhang X" first="Xu" last="Zhang">Xu Zhang</name></author><author><name sortKey="Lu, Jun" sort="Lu, Jun" uniqKey="Lu J" first="Jun" last="Lu">Jun Lu</name></author><author><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:24295294</idno><idno type="pmid">24295294</idno><idno type="doi">10.1089/ars.2013.5499</idno><idno type="pmc">PMC4098818</idno><idno type="wicri:Area/Main/Corpus">000680</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000680</idno><idno type="wicri:Area/Main/Curation">000680</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000680</idno><idno type="wicri:Area/Main/Exploration">000680</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Glutaredoxin 2 reduces both thioredoxin 2 and thioredoxin 1 and protects cells from apoptosis induced by auranofin and 4-hydroxynonenal.</title><author><name sortKey="Zhang, Huihui" sort="Zhang, Huihui" uniqKey="Zhang H" first="Huihui" last="Zhang">Huihui Zhang</name><affiliation wicri:level="3"><nlm:affiliation>Division of Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institute , Stockholm, Sweden .</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Division of Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institute , Stockholm</wicri:regionArea><placeName><settlement type="city">Stockholm</settlement><region nuts="2">Svealand</region></placeName></affiliation></author><author><name sortKey="Du, Yatao" sort="Du, Yatao" uniqKey="Du Y" first="Yatao" last="Du">Yatao Du</name></author><author><name sortKey="Zhang, Xu" sort="Zhang, Xu" uniqKey="Zhang X" first="Xu" last="Zhang">Xu Zhang</name></author><author><name sortKey="Lu, Jun" sort="Lu, Jun" uniqKey="Lu J" first="Jun" last="Lu">Jun Lu</name></author><author><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name></author></analytic><series><title level="j">Antioxidants & redox signaling</title><idno type="eISSN">1557-7716</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aldehydes (pharmacology)</term><term>Apoptosis (drug effects)</term><term>Auranofin (pharmacology)</term><term>Dose-Response Relationship, Drug (MeSH)</term><term>Glutaredoxins (metabolism)</term><term>HeLa Cells (MeSH)</term><term>Humans (MeSH)</term><term>Mitochondrial Proteins (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidative Stress (MeSH)</term><term>Structure-Activity Relationship (MeSH)</term><term>Thioredoxin-Disulfide Reductase (metabolism)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Aldéhydes (pharmacologie)</term><term>Apoptose (effets des médicaments et des substances chimiques)</term><term>Auranofine (pharmacologie)</term><term>Cellules HeLa (MeSH)</term><term>Glutarédoxines (métabolisme)</term><term>Humains (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Protéines mitochondriales (métabolisme)</term><term>Relation dose-effet des médicaments (MeSH)</term><term>Relation structure-activité (MeSH)</term><term>Stress oxydatif (MeSH)</term><term>Thioredoxin-disulfide reductase (métabolisme)</term><term>Thiorédoxines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term><term>Mitochondrial Proteins</term><term>Thioredoxin-Disulfide Reductase</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Aldehydes</term><term>Auranofin</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Apoptosis</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Apoptose</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutarédoxines</term><term>Protéines mitochondriales</term><term>Thioredoxin-disulfide reductase</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Aldéhydes</term><term>Auranofine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Dose-Response Relationship, Drug</term><term>HeLa Cells</term><term>Humans</term><term>Oxidation-Reduction</term><term>Oxidative Stress</term><term>Structure-Activity Relationship</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cellules HeLa</term><term>Humains</term><term>Oxydoréduction</term><term>Relation dose-effet des médicaments</term><term>Relation structure-activité</term><term>Stress oxydatif</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>AIMS</b></p><p>Mitochondrial thioredoxin (Trx) is critical for defense against oxidative stress-induced cell apoptosis. To date, mitochondrial thioredoxin reductase (TrxR) is the only known enzyme catalyzing Trx2 reduction in mitochondria. However, TrxR is sensitive to inactivation by exo/endogenous electrophiles, for example, 4-hydroxynonenal (HNE). In this study, we characterized the mitochondrial glutaredoxin 2 (Grx2) system as a backup for the mitochondrial TrxR. Meanwhile, as Grx2 is also present in the cytosol/nucleus of certain cancer cell lines, the reducing activity of Grx2 on Trx1 was also tested.</p></div><div type="abstract" xml:lang="en"><p><b>RESULTS</b></p><p>Glutathione alone could reduce oxidized Trx2, and the presence of physiological concentrations of Grx2 markedly increased the reaction rate. HeLa cells with Grx2 overexpression (particularly in the mitochondria) exhibited higher viabilities than the wild-type cells after treatment with TrxR inhibitors (Auranofin or HNE), whereas knockdown of Grx2 sensitized the cells to TrxR inhibitors. Accordingly, Grx2 overexpression in the mitochondria had protected Trx2 from oxidation by HNE treatment, whereas Grx2 knockdown had sensitized Trx2 to oxidation. On the other hand, Grx2 reduced Trx1 with similar activities as that of Trx2. Overexpression of Grx2 in the cytosol had protected Trx1 from oxidation, indicating a supportive role of Grx2 in the cytosolic redox balance of cancer cells.</p></div><div type="abstract" xml:lang="en"><p><b>INNOVATION</b></p><p>This work explores the reductase activity of Grx2 on Trx2/1, and demonstrates the physiological importance of the activity by using in vivo redox western blot assays.</p></div><div type="abstract" xml:lang="en"><p><b>CONCLUSION</b></p><p>Grx2 system could help to keep Trx2/1 reduced during an oxidative stress, thereby contributing to the anti-apoptotic signaling.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24295294</PMID><DateCompleted><Year>2015</Year><Month>04</Month><Day>19</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1557-7716</ISSN><JournalIssue CitedMedium="Internet"><Volume>21</Volume><Issue>5</Issue><PubDate><Year>2014</Year><Month>Aug</Month><Day>10</Day></PubDate></JournalIssue><Title>Antioxidants & redox signaling</Title><ISOAbbreviation>Antioxid Redox Signal</ISOAbbreviation></Journal><ArticleTitle>Glutaredoxin 2 reduces both thioredoxin 2 and thioredoxin 1 and protects cells from apoptosis induced by auranofin and 4-hydroxynonenal.</ArticleTitle><Pagination><MedlinePgn>669-81</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1089/ars.2013.5499</ELocationID><Abstract><AbstractText Label="AIMS" NlmCategory="OBJECTIVE">Mitochondrial thioredoxin (Trx) is critical for defense against oxidative stress-induced cell apoptosis. To date, mitochondrial thioredoxin reductase (TrxR) is the only known enzyme catalyzing Trx2 reduction in mitochondria. However, TrxR is sensitive to inactivation by exo/endogenous electrophiles, for example, 4-hydroxynonenal (HNE). In this study, we characterized the mitochondrial glutaredoxin 2 (Grx2) system as a backup for the mitochondrial TrxR. Meanwhile, as Grx2 is also present in the cytosol/nucleus of certain cancer cell lines, the reducing activity of Grx2 on Trx1 was also tested.</AbstractText><AbstractText Label="RESULTS" NlmCategory="RESULTS">Glutathione alone could reduce oxidized Trx2, and the presence of physiological concentrations of Grx2 markedly increased the reaction rate. HeLa cells with Grx2 overexpression (particularly in the mitochondria) exhibited higher viabilities than the wild-type cells after treatment with TrxR inhibitors (Auranofin or HNE), whereas knockdown of Grx2 sensitized the cells to TrxR inhibitors. Accordingly, Grx2 overexpression in the mitochondria had protected Trx2 from oxidation by HNE treatment, whereas Grx2 knockdown had sensitized Trx2 to oxidation. On the other hand, Grx2 reduced Trx1 with similar activities as that of Trx2. Overexpression of Grx2 in the cytosol had protected Trx1 from oxidation, indicating a supportive role of Grx2 in the cytosolic redox balance of cancer cells.</AbstractText><AbstractText Label="INNOVATION" NlmCategory="METHODS">This work explores the reductase activity of Grx2 on Trx2/1, and demonstrates the physiological importance of the activity by using in vivo redox western blot assays.</AbstractText><AbstractText Label="CONCLUSION" NlmCategory="CONCLUSIONS">Grx2 system could help to keep Trx2/1 reduced during an oxidative stress, thereby contributing to the anti-apoptotic signaling.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Huihui</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Division of Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institute , Stockholm, Sweden .</Affiliation></AffiliationInfo></Author><Author 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Jul 13;276(28):26269-75</Citation><ArticleIdList><ArticleId IdType="pubmed">11297543</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country><region><li>Svealand</li></region><settlement><li>Stockholm</li></settlement></list><tree><noCountry><name sortKey="Du, Yatao" sort="Du, Yatao" uniqKey="Du Y" first="Yatao" last="Du">Yatao Du</name><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name><name sortKey="Lu, Jun" sort="Lu, Jun" uniqKey="Lu J" first="Jun" last="Lu">Jun Lu</name><name sortKey="Zhang, Xu" sort="Zhang, Xu" uniqKey="Zhang X" first="Xu" last="Zhang">Xu Zhang</name></noCountry><country name="Suède"><region name="Svealand"><name sortKey="Zhang, Huihui" sort="Zhang, Huihui" uniqKey="Zhang H" first="Huihui" last="Zhang">Huihui Zhang</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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