Overexpression of glutaredoxin 2 attenuates apoptosis by preventing cytochrome c release.
Identifieur interne : 000E02 ( Main/Exploration ); précédent : 000E01; suivant : 000E03Overexpression of glutaredoxin 2 attenuates apoptosis by preventing cytochrome c release.
Auteurs : Mari Enoksson [Suède] ; Aristi Potamitou Fernandes ; Stefanie Prast ; Christopher Horst Lillig ; Arne Holmgren ; Sten OrreniusSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 2005.
Descripteurs français
- KwdFr :
- Apoptose (effets des médicaments et des substances chimiques), Apoptose (physiologie), Cardiolipides (métabolisme), Caspases (métabolisme), Cellules cancéreuses en culture (MeSH), Cytochromes c (antagonistes et inhibiteurs), Cytochromes c (métabolisme), Cytosol (métabolisme), Doxorubicine (pharmacologie), Désoxyglucose (pharmacologie), Glutarédoxines (MeSH), Humains (MeSH), Mitochondries (métabolisme), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Oxidoreductases (pharmacologie), Oxydoréduction (effets des médicaments et des substances chimiques), Régulation de l'expression des gènes (MeSH).
- MESH :
- antagonistes et inhibiteurs : Cytochromes c.
- effets des médicaments et des substances chimiques : Apoptose, Oxydoréduction.
- génétique : Oxidoreductases.
- métabolisme : Cardiolipides, Caspases, Cytochromes c, Cytosol, Mitochondries, Oxidoreductases.
- pharmacologie : Doxorubicine, Désoxyglucose, Oxidoreductases.
- physiologie : Apoptose.
- Cellules cancéreuses en culture, Glutarédoxines, Humains, Régulation de l'expression des gènes.
English descriptors
- KwdEn :
- Apoptosis (drug effects), Apoptosis (physiology), Cardiolipins (metabolism), Caspases (metabolism), Cytochromes c (antagonists & inhibitors), Cytochromes c (metabolism), Cytosol (metabolism), Deoxyglucose (pharmacology), Doxorubicin (pharmacology), Gene Expression Regulation (MeSH), Glutaredoxins (MeSH), Humans (MeSH), Mitochondria (metabolism), Oxidation-Reduction (drug effects), Oxidoreductases (genetics), Oxidoreductases (metabolism), Oxidoreductases (pharmacology), Tumor Cells, Cultured (MeSH).
- MESH :
- chemical , antagonists & inhibitors : Cytochromes c.
- chemical , genetics : Oxidoreductases.
- chemical , metabolism : Cardiolipins, Caspases, Cytochromes c, Oxidoreductases.
- drug effects : Apoptosis, Oxidation-Reduction.
- metabolism : Cytosol, Mitochondria.
- chemical , pharmacology : Deoxyglucose, Doxorubicin, Oxidoreductases.
- physiology : Apoptosis.
- Gene Expression Regulation, Glutaredoxins, Humans, Tumor Cells, Cultured.
Abstract
Human mitochondrial glutaredoxin 2 (Grx2) catalyzes glutathione-dependent dithiol reaction mechanisms, reducing protein disulfides, and monothiol reactions, reducing mixed disulfides between proteins and GSH (de-/glutathionylation). Here, we have overexpressed Grx2 in HeLa cells in its mitochondrial form (mGrx2-HeLa) as well as a truncated cytosolic form, lacking the mitochondrial translocation signal (tGrx2-HeLa). The resulting clones were less susceptible to apoptosis induced by 2-deoxy-d-glucose (2-DG) or doxorubicin (Dox). Overexpression of Grx2 inhibited cytochrome c release and caspase activation induced by both agents. In addition, Grx2 prevented 2-DG- and Dox-induced loss of cardiolipin, the phospholipid anchoring cytochrome c to the inner mitochondrial membrane. Overexpression of mGrx2 provided better protection than tGrx2 overexpression, especially after treatment with 2-DG. We propose that Grx2 facilitates the maintenance of cellular redox homeostasis upon treatment with apoptotic agents, thereby preventing cardiolipin oxidation and cytochrome c release.
DOI: 10.1016/j.bbrc.2004.12.067
PubMed: 15649413
Affiliations:
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qualifier="metabolism" xml:lang="en"><term>Cytosol</term><term>Mitochondria</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cardiolipides</term><term>Caspases</term><term>Cytochromes c</term><term>Cytosol</term><term>Mitochondries</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Doxorubicine</term><term>Désoxyglucose</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Deoxyglucose</term><term>Doxorubicin</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Apoptose</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Apoptosis</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Gene Expression Regulation</term><term>Glutaredoxins</term><term>Humans</term><term>Tumor Cells, Cultured</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cellules cancéreuses en culture</term><term>Glutarédoxines</term><term>Humains</term><term>Régulation de l'expression des gènes</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Human mitochondrial glutaredoxin 2 (Grx2) catalyzes glutathione-dependent dithiol reaction mechanisms, reducing protein disulfides, and monothiol reactions, reducing mixed disulfides between proteins and GSH (de-/glutathionylation). Here, we have overexpressed Grx2 in HeLa cells in its mitochondrial form (mGrx2-HeLa) as well as a truncated cytosolic form, lacking the mitochondrial translocation signal (tGrx2-HeLa). The resulting clones were less susceptible to apoptosis induced by 2-deoxy-d-glucose (2-DG) or doxorubicin (Dox). Overexpression of Grx2 inhibited cytochrome c release and caspase activation induced by both agents. In addition, Grx2 prevented 2-DG- and Dox-induced loss of cardiolipin, the phospholipid anchoring cytochrome c to the inner mitochondrial membrane. Overexpression of mGrx2 provided better protection than tGrx2 overexpression, especially after treatment with 2-DG. We propose that Grx2 facilitates the maintenance of cellular redox homeostasis upon treatment with apoptotic agents, thereby preventing cardiolipin oxidation and cytochrome c release.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15649413</PMID><DateCompleted><Year>2005</Year><Month>04</Month><Day>13</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-291X</ISSN><JournalIssue CitedMedium="Print"><Volume>327</Volume><Issue>3</Issue><PubDate><Year>2005</Year><Month>Feb</Month><Day>18</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Overexpression of glutaredoxin 2 attenuates apoptosis by preventing cytochrome c release.</ArticleTitle><Pagination><MedlinePgn>774-9</MedlinePgn></Pagination><Abstract><AbstractText>Human mitochondrial glutaredoxin 2 (Grx2) catalyzes glutathione-dependent dithiol reaction mechanisms, reducing protein disulfides, and monothiol reactions, reducing mixed disulfides between proteins and GSH (de-/glutathionylation). Here, we have overexpressed Grx2 in HeLa cells in its mitochondrial form (mGrx2-HeLa) as well as a truncated cytosolic form, lacking the mitochondrial translocation signal (tGrx2-HeLa). The resulting clones were less susceptible to apoptosis induced by 2-deoxy-d-glucose (2-DG) or doxorubicin (Dox). Overexpression of Grx2 inhibited cytochrome c release and caspase activation induced by both agents. In addition, Grx2 prevented 2-DG- and Dox-induced loss of cardiolipin, the phospholipid anchoring cytochrome c to the inner mitochondrial membrane. Overexpression of mGrx2 provided better protection than tGrx2 overexpression, especially after treatment with 2-DG. We propose that Grx2 facilitates the maintenance of cellular redox homeostasis upon treatment with apoptotic agents, thereby preventing cardiolipin oxidation and cytochrome c release.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Enoksson</LastName><ForeName>Mari</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Division of Toxicology, Institute of Environmental Medicine, Karolinska Institutet, SE-171 77 Stockholm, Sweden. Mari.Enoksson@imm.ki.se</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fernandes</LastName><ForeName>Aristi Potamitou</ForeName><Initials>AP</Initials></Author><Author ValidYN="Y"><LastName>Prast</LastName><ForeName>Stefanie</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Lillig</LastName><ForeName>Christopher Horst</ForeName><Initials>CH</Initials></Author><Author ValidYN="Y"><LastName>Holmgren</LastName><ForeName>Arne</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Orrenius</LastName><ForeName>Sten</ForeName><Initials>S</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>Biochem Biophys Res 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first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name><name sortKey="Orrenius, Sten" sort="Orrenius, Sten" uniqKey="Orrenius S" first="Sten" last="Orrenius">Sten Orrenius</name><name sortKey="Prast, Stefanie" sort="Prast, Stefanie" uniqKey="Prast S" first="Stefanie" last="Prast">Stefanie Prast</name></noCountry><country name="Suède"><noRegion><name sortKey="Enoksson, Mari" sort="Enoksson, Mari" uniqKey="Enoksson M" first="Mari" last="Enoksson">Mari Enoksson</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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