Knockout of mitochondrial thioredoxin reductase stabilizes prolyl hydroxylase 2 and inhibits tumor growth and tumor-derived angiogenesis.
Identifieur interne : 000538 ( Main/Exploration ); précédent : 000537; suivant : 000539Knockout of mitochondrial thioredoxin reductase stabilizes prolyl hydroxylase 2 and inhibits tumor growth and tumor-derived angiogenesis.
Auteurs : Juliane Hellfritsch [Allemagne] ; Julian Kirsch ; Manuela Schneider ; Tamara Fluege ; Markus Wortmann ; Jeroen Frijhoff ; Markus Dagnell ; Theres Fey ; Irene Esposito ; Pirkko Kölle ; Kristin Pogoda ; José Pedro Friedmann Angeli ; Irina Ingold ; Peter Kuhlencordt ; Arne Östman ; Ulrich Pohl ; Marcus Conrad ; Heike BeckSource :
- Antioxidants & redox signaling [ 1557-7716 ] ; 2015.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Cellules cultivées (MeSH), Espèces réactives de l'oxygène (métabolisme), Hypoxia-inducible factor-proline dioxygenases (génétique), Hypoxia-inducible factor-proline dioxygenases (métabolisme), Hétérogreffes (MeSH), Mitochondries (métabolisme), Néovascularisation pathologique (métabolisme), Prolifération cellulaire (MeSH), Souris (MeSH), Souris transgéniques (MeSH), Sous-unité alpha du facteur-1 induit par l'hypoxie (métabolisme), Techniques de knock-down de gènes (MeSH), Thioredoxin reductase 2 (génétique), Transplantation tumorale (MeSH).
- MESH :
- génétique : Hypoxia-inducible factor-proline dioxygenases, Thioredoxin reductase 2.
- métabolisme : Espèces réactives de l'oxygène, Hypoxia-inducible factor-proline dioxygenases, Mitochondries, Néovascularisation pathologique, Sous-unité alpha du facteur-1 induit par l'hypoxie.
- Animaux, Cellules cultivées, Hétérogreffes, Prolifération cellulaire, Souris, Souris transgéniques, Techniques de knock-down de gènes, Transplantation tumorale.
English descriptors
- KwdEn :
- Animals (MeSH), Cell Proliferation (MeSH), Cells, Cultured (MeSH), Gene Knockdown Techniques (MeSH), Heterografts (MeSH), Hypoxia-Inducible Factor 1, alpha Subunit (metabolism), Hypoxia-Inducible Factor-Proline Dioxygenases (genetics), Hypoxia-Inducible Factor-Proline Dioxygenases (metabolism), Mice (MeSH), Mice, Transgenic (MeSH), Mitochondria (metabolism), Neoplasm Transplantation (MeSH), Neovascularization, Pathologic (metabolism), Reactive Oxygen Species (metabolism), Thioredoxin Reductase 2 (genetics).
- MESH :
- chemical , genetics : Hypoxia-Inducible Factor-Proline Dioxygenases, Thioredoxin Reductase 2.
- chemical , metabolism : Hypoxia-Inducible Factor 1, alpha Subunit, Hypoxia-Inducible Factor-Proline Dioxygenases, Reactive Oxygen Species.
- metabolism : Mitochondria, Neovascularization, Pathologic.
- Animals, Cell Proliferation, Cells, Cultured, Gene Knockdown Techniques, Heterografts, Mice, Mice, Transgenic, Neoplasm Transplantation.
Abstract
AIMS
Mitochondrial thioredoxin reductase (Txnrd2) is a central player in the control of mitochondrial hydrogen peroxide (H2O2) abundance by serving as a direct electron donor to the thioredoxin-peroxiredoxin axis. In this study, we investigated the impact of targeted disruption of Txnrd2 on tumor growth.
RESULTS
Tumor cells with a Txnrd2 deficiency failed to activate hypoxia-inducible factor-1α (Hif-1α) signaling; it rather caused PHD2 accumulation, Hif-1α degradation and decreased vascular endothelial growth factor (VEGF) levels, ultimately leading to reduced tumor growth and tumor vascularization. Increased c-Jun NH2-terminal Kinase (JNK) activation proved to be the molecular link between the loss of Txnrd2, an altered mitochondrial redox balance with compensatory upregulation of glutaredoxin-2, and elevated PHD2 expression.
INNOVATION
Our data provide compelling evidence for a yet-unrecognized mitochondrial Txnrd-driven, regulatory mechanism that ultimately prevents cellular Hif-1α accumulation. In addition, simultaneous targeting of both the mitochondrial thioredoxin and glutathione systems was used as an efficient therapeutic approach in hindering tumor growth.
CONCLUSION
This work demonstrates an unexpected regulatory link between mitochondrial Txnrd and the JNK-PHD2-Hif-1α axis, which highlights how the loss of Txnrd2 and the resulting altered mitochondrial redox balance impairs tumor growth as well as tumor-related angiogenesis. Furthermore, it opens a new avenue for a therapeutic approach to hinder tumor growth by the simultaneous targeting of both the mitochondrial thioredoxin and glutathione systems.
DOI: 10.1089/ars.2014.5889
PubMed: 25647640
PubMed Central: PMC4376289
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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sortKey="Pohl, Ulrich" sort="Pohl, Ulrich" uniqKey="Pohl U" first="Ulrich" last="Pohl">Ulrich Pohl</name></author><author><name sortKey="Conrad, Marcus" sort="Conrad, Marcus" uniqKey="Conrad M" first="Marcus" last="Conrad">Marcus Conrad</name></author><author><name sortKey="Beck, Heike" sort="Beck, Heike" uniqKey="Beck H" first="Heike" last="Beck">Heike Beck</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:25647640</idno><idno type="pmid">25647640</idno><idno type="doi">10.1089/ars.2014.5889</idno><idno type="pmc">PMC4376289</idno><idno type="wicri:Area/Main/Corpus">000557</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000557</idno><idno type="wicri:Area/Main/Curation">000557</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000557</idno><idno 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type="city">Munich</settlement></placeName></affiliation></author><author><name sortKey="Kirsch, Julian" sort="Kirsch, Julian" uniqKey="Kirsch J" first="Julian" last="Kirsch">Julian Kirsch</name></author><author><name sortKey="Schneider, Manuela" sort="Schneider, Manuela" uniqKey="Schneider M" first="Manuela" last="Schneider">Manuela Schneider</name></author><author><name sortKey="Fluege, Tamara" sort="Fluege, Tamara" uniqKey="Fluege T" first="Tamara" last="Fluege">Tamara Fluege</name></author><author><name sortKey="Wortmann, Markus" sort="Wortmann, Markus" uniqKey="Wortmann M" first="Markus" last="Wortmann">Markus Wortmann</name></author><author><name sortKey="Frijhoff, Jeroen" sort="Frijhoff, Jeroen" uniqKey="Frijhoff J" first="Jeroen" last="Frijhoff">Jeroen Frijhoff</name></author><author><name sortKey="Dagnell, Markus" sort="Dagnell, Markus" uniqKey="Dagnell M" first="Markus" last="Dagnell">Markus Dagnell</name></author><author><name sortKey="Fey, Theres" sort="Fey, Theres" uniqKey="Fey T" first="Theres" last="Fey">Theres Fey</name></author><author><name sortKey="Esposito, Irene" sort="Esposito, Irene" uniqKey="Esposito I" first="Irene" last="Esposito">Irene Esposito</name></author><author><name sortKey="Kolle, Pirkko" sort="Kolle, Pirkko" uniqKey="Kolle P" first="Pirkko" last="Kölle">Pirkko Kölle</name></author><author><name sortKey="Pogoda, Kristin" sort="Pogoda, Kristin" uniqKey="Pogoda K" first="Kristin" last="Pogoda">Kristin Pogoda</name></author><author><name sortKey="Angeli, Jose Pedro Friedmann" sort="Angeli, Jose Pedro Friedmann" uniqKey="Angeli J" first="José Pedro Friedmann" last="Angeli">José Pedro Friedmann Angeli</name></author><author><name sortKey="Ingold, Irina" sort="Ingold, Irina" uniqKey="Ingold I" first="Irina" last="Ingold">Irina Ingold</name></author><author><name sortKey="Kuhlencordt, Peter" sort="Kuhlencordt, Peter" uniqKey="Kuhlencordt P" first="Peter" last="Kuhlencordt">Peter Kuhlencordt</name></author><author><name sortKey="Ostman, Arne" sort="Ostman, Arne" uniqKey="Ostman A" first="Arne" last="Östman">Arne Östman</name></author><author><name sortKey="Pohl, Ulrich" sort="Pohl, Ulrich" uniqKey="Pohl U" first="Ulrich" last="Pohl">Ulrich Pohl</name></author><author><name sortKey="Conrad, Marcus" sort="Conrad, Marcus" uniqKey="Conrad M" first="Marcus" last="Conrad">Marcus Conrad</name></author><author><name sortKey="Beck, Heike" sort="Beck, Heike" uniqKey="Beck H" first="Heike" last="Beck">Heike Beck</name></author></analytic><series><title level="j">Antioxidants & redox signaling</title><idno type="eISSN">1557-7716</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Cell Proliferation (MeSH)</term><term>Cells, Cultured (MeSH)</term><term>Gene Knockdown Techniques (MeSH)</term><term>Heterografts (MeSH)</term><term>Hypoxia-Inducible Factor 1, alpha Subunit (metabolism)</term><term>Hypoxia-Inducible Factor-Proline Dioxygenases (genetics)</term><term>Hypoxia-Inducible Factor-Proline Dioxygenases (metabolism)</term><term>Mice (MeSH)</term><term>Mice, Transgenic (MeSH)</term><term>Mitochondria (metabolism)</term><term>Neoplasm Transplantation (MeSH)</term><term>Neovascularization, Pathologic (metabolism)</term><term>Reactive Oxygen Species (metabolism)</term><term>Thioredoxin Reductase 2 (genetics)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Cellules cultivées (MeSH)</term><term>Espèces réactives de l'oxygène (métabolisme)</term><term>Hypoxia-inducible factor-proline dioxygenases (génétique)</term><term>Hypoxia-inducible factor-proline dioxygenases (métabolisme)</term><term>Hétérogreffes (MeSH)</term><term>Mitochondries (métabolisme)</term><term>Néovascularisation pathologique (métabolisme)</term><term>Prolifération cellulaire (MeSH)</term><term>Souris (MeSH)</term><term>Souris transgéniques (MeSH)</term><term>Sous-unité alpha du facteur-1 induit par l'hypoxie (métabolisme)</term><term>Techniques de knock-down de gènes (MeSH)</term><term>Thioredoxin reductase 2 (génétique)</term><term>Transplantation tumorale (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Hypoxia-Inducible Factor-Proline Dioxygenases</term><term>Thioredoxin Reductase 2</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Hypoxia-Inducible Factor 1, alpha Subunit</term><term>Hypoxia-Inducible Factor-Proline Dioxygenases</term><term>Reactive Oxygen Species</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Hypoxia-inducible factor-proline dioxygenases</term><term>Thioredoxin reductase 2</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Mitochondria</term><term>Neovascularization, Pathologic</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Espèces réactives de l'oxygène</term><term>Hypoxia-inducible factor-proline dioxygenases</term><term>Mitochondries</term><term>Néovascularisation pathologique</term><term>Sous-unité alpha du facteur-1 induit par l'hypoxie</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Proliferation</term><term>Cells, Cultured</term><term>Gene Knockdown Techniques</term><term>Heterografts</term><term>Mice</term><term>Mice, Transgenic</term><term>Neoplasm Transplantation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules cultivées</term><term>Hétérogreffes</term><term>Prolifération cellulaire</term><term>Souris</term><term>Souris transgéniques</term><term>Techniques de knock-down de gènes</term><term>Transplantation tumorale</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>AIMS</b></p><p>Mitochondrial thioredoxin reductase (Txnrd2) is a central player in the control of mitochondrial hydrogen peroxide (H2O2) abundance by serving as a direct electron donor to the thioredoxin-peroxiredoxin axis. In this study, we investigated the impact of targeted disruption of Txnrd2 on tumor growth.</p></div><div type="abstract" xml:lang="en"><p><b>RESULTS</b></p><p>Tumor cells with a Txnrd2 deficiency failed to activate hypoxia-inducible factor-1α (Hif-1α) signaling; it rather caused PHD2 accumulation, Hif-1α degradation and decreased vascular endothelial growth factor (VEGF) levels, ultimately leading to reduced tumor growth and tumor vascularization. Increased c-Jun NH2-terminal Kinase (JNK) activation proved to be the molecular link between the loss of Txnrd2, an altered mitochondrial redox balance with compensatory upregulation of glutaredoxin-2, and elevated PHD2 expression.</p></div><div type="abstract" xml:lang="en"><p><b>INNOVATION</b></p><p>Our data provide compelling evidence for a yet-unrecognized mitochondrial Txnrd-driven, regulatory mechanism that ultimately prevents cellular Hif-1α accumulation. In addition, simultaneous targeting of both the mitochondrial thioredoxin and glutathione systems was used as an efficient therapeutic approach in hindering tumor growth.</p></div><div type="abstract" xml:lang="en"><p><b>CONCLUSION</b></p><p>This work demonstrates an unexpected regulatory link between mitochondrial Txnrd and the JNK-PHD2-Hif-1α axis, which highlights how the loss of Txnrd2 and the resulting altered mitochondrial redox balance impairs tumor growth as well as tumor-related angiogenesis. Furthermore, it opens a new avenue for a therapeutic approach to hinder tumor growth by the simultaneous targeting of both the mitochondrial thioredoxin and glutathione systems.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25647640</PMID><DateCompleted><Year>2015</Year><Month>11</Month><Day>09</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1557-7716</ISSN><JournalIssue CitedMedium="Internet"><Volume>22</Volume><Issue>11</Issue><PubDate><Year>2015</Year><Month>Apr</Month><Day>10</Day></PubDate></JournalIssue><Title>Antioxidants & redox signaling</Title><ISOAbbreviation>Antioxid Redox Signal</ISOAbbreviation></Journal><ArticleTitle>Knockout of mitochondrial thioredoxin reductase stabilizes prolyl hydroxylase 2 and inhibits tumor growth and tumor-derived angiogenesis.</ArticleTitle><Pagination><MedlinePgn>938-50</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1089/ars.2014.5889</ELocationID><Abstract><AbstractText Label="AIMS" NlmCategory="OBJECTIVE">Mitochondrial thioredoxin reductase (Txnrd2) is a central player in the control of mitochondrial hydrogen peroxide (H2O2) abundance by serving as a direct electron donor to the thioredoxin-peroxiredoxin axis. In this study, we investigated the impact of targeted disruption of Txnrd2 on tumor growth.</AbstractText><AbstractText Label="RESULTS" NlmCategory="RESULTS">Tumor cells with a Txnrd2 deficiency failed to activate hypoxia-inducible factor-1α (Hif-1α) signaling; it rather caused PHD2 accumulation, Hif-1α degradation and decreased vascular endothelial growth factor (VEGF) levels, ultimately leading to reduced tumor growth and tumor vascularization. Increased c-Jun NH2-terminal Kinase (JNK) activation proved to be the molecular link between the loss of Txnrd2, an altered mitochondrial redox balance with compensatory upregulation of glutaredoxin-2, and elevated PHD2 expression.</AbstractText><AbstractText Label="INNOVATION" NlmCategory="METHODS">Our data provide compelling evidence for a yet-unrecognized mitochondrial Txnrd-driven, regulatory mechanism that ultimately prevents cellular Hif-1α accumulation. In addition, simultaneous targeting of both the mitochondrial thioredoxin and glutathione systems was used as an efficient therapeutic approach in hindering tumor growth.</AbstractText><AbstractText Label="CONCLUSION" NlmCategory="CONCLUSIONS">This work demonstrates an unexpected regulatory link between mitochondrial Txnrd and the JNK-PHD2-Hif-1α axis, which highlights how the loss of Txnrd2 and the resulting altered mitochondrial redox balance impairs tumor growth as well as tumor-related angiogenesis. Furthermore, it opens a new avenue for a therapeutic approach to hinder tumor growth by the simultaneous targeting of both the mitochondrial thioredoxin and glutathione systems.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hellfritsch</LastName><ForeName>Juliane</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>1 Walter Brendel Centre of Experimental Medicine, Munich Heart Alliance, Ludwig-Maximilians-University , Munich, Germany .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kirsch</LastName><ForeName>Julian</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Schneider</LastName><ForeName>Manuela</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Fluege</LastName><ForeName>Tamara</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Wortmann</LastName><ForeName>Markus</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Frijhoff</LastName><ForeName>Jeroen</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Dagnell</LastName><ForeName>Markus</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Fey</LastName><ForeName>Theres</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Esposito</LastName><ForeName>Irene</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Kölle</LastName><ForeName>Pirkko</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Pogoda</LastName><ForeName>Kristin</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Angeli</LastName><ForeName>José Pedro Friedmann</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>Ingold</LastName><ForeName>Irina</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Kuhlencordt</LastName><ForeName>Peter</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Östman</LastName><ForeName>Arne</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Pohl</LastName><ForeName>Ulrich</ForeName><Initials>U</Initials></Author><Author ValidYN="Y"><LastName>Conrad</LastName><ForeName>Marcus</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Beck</LastName><ForeName>Heike</ForeName><Initials>H</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</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="C497443">Hif1a protein, mouse</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051795">Hypoxia-Inducible Factor 1, alpha Subunit</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017382">Reactive Oxygen Species</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.14.11.29</RegistryNumber><NameOfSubstance UI="C490189">Egln1 protein, mouse</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.14.11.29</RegistryNumber><NameOfSubstance UI="D064799">Hypoxia-Inducible Factor-Proline Dioxygenases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.9</RegistryNumber><NameOfSubstance UI="D054482">Thioredoxin Reductase 2</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.9</RegistryNumber><NameOfSubstance UI="C516128">Txnrd2 protein, mouse</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D049109" MajorTopicYN="Y">Cell Proliferation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002478" MajorTopicYN="N">Cells, Cultured</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055785" MajorTopicYN="N">Gene Knockdown Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D064593" MajorTopicYN="N">Heterografts</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051795" MajorTopicYN="N">Hypoxia-Inducible Factor 1, alpha Subunit</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D064799" MajorTopicYN="N">Hypoxia-Inducible Factor-Proline Dioxygenases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName 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