Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells toward doxorubicin and phenylarsine oxide.
Identifieur interne : 000E47 ( Main/Exploration ); précédent : 000E46; suivant : 000E48Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells toward doxorubicin and phenylarsine oxide.
Auteurs : Christopher Horst Lillig [Suède] ; Maria Elisabet Lönn ; Mari Enoksson ; Aristi Potamitou Fernandes ; Arne HolmgrenSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2004.
Descripteurs français
- KwdFr :
- Cadmium (pharmacologie), Cellules HeLa (MeSH), Composés de l'arsenic (pharmacologie), Doxorubicine (pharmacologie), Extinction de l'expression des gènes (MeSH), Glutarédoxines (MeSH), Humains (MeSH), Oxidoreductases (antagonistes et inhibiteurs), Oxidoreductases (génétique), Petit ARN interférent (pharmacologie), Stress oxydatif (MeSH).
- MESH :
- antagonistes et inhibiteurs : Oxidoreductases.
- génétique : Oxidoreductases.
- pharmacologie : Cadmium, Composés de l'arsenic, Doxorubicine, Petit ARN interférent.
- Cellules HeLa, Extinction de l'expression des gènes, Glutarédoxines, Humains, Stress oxydatif.
English descriptors
- KwdEn :
- MESH :
- chemical , antagonists & inhibitors : Oxidoreductases.
- chemical , genetics : Oxidoreductases.
- chemical , pharmacology : Arsenicals, Cadmium, Doxorubicin, RNA, Small Interfering.
- Gene Silencing, Glutaredoxins, HeLa Cells, Humans, Oxidative Stress.
Abstract
Glutaredoxin (Grx) belongs to the thioredoxin fold superfamily and catalyzes glutathione-dependent oxidoreductions. The recently discovered mitochondrial and nuclear Grx (Grx2) differs from the more abundant cytosolic Grx (Grx1) by its higher affinity toward S-glutathionylated proteins and by being a substrate for thioredoxin reductase. Here, we have successfully established a method to silence the expression of Grx2 in HeLa cells by using short interfering RNA to study its role in the cell. Cells with levels of Grx2 <3% of the control were dramatically sensitized to cell death induced by doxorubicin/adriamycin and phenylarsine oxide but did not show signs of a general increase in oxidative damage with respect to carbonylation and glutathionylation. The ED(50) for doxorubicin dropped from 40 to 0.7 microM and for phenylarsine oxide from 200 to 5 nM. However, no differences were detected after treatment with cadmium, a known inhibitor of Grx1. These results indicate a crucial role of Grx2 in the regulation of the mitochondrial redox status and regulation of cell death at the mitochondrial checkpoint.
DOI: 10.1073/pnas.0401896101
PubMed: 15328416
PubMed Central: PMC516552
Affiliations:
Links toward previous steps (curation, corpus...)
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qualifier="antagonists & inhibitors" xml:lang="en"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Arsenicals</term><term>Cadmium</term><term>Doxorubicin</term><term>RNA, Small Interfering</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Cadmium</term><term>Composés de l'arsenic</term><term>Doxorubicine</term><term>Petit ARN interférent</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Gene Silencing</term><term>Glutaredoxins</term><term>HeLa Cells</term><term>Humans</term><term>Oxidative Stress</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cellules HeLa</term><term>Extinction de l'expression des gènes</term><term>Glutarédoxines</term><term>Humains</term><term>Stress oxydatif</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxin (Grx) belongs to the thioredoxin fold superfamily and catalyzes glutathione-dependent oxidoreductions. The recently discovered mitochondrial and nuclear Grx (Grx2) differs from the more abundant cytosolic Grx (Grx1) by its higher affinity toward S-glutathionylated proteins and by being a substrate for thioredoxin reductase. Here, we have successfully established a method to silence the expression of Grx2 in HeLa cells by using short interfering RNA to study its role in the cell. Cells with levels of Grx2 <3% of the control were dramatically sensitized to cell death induced by doxorubicin/adriamycin and phenylarsine oxide but did not show signs of a general increase in oxidative damage with respect to carbonylation and glutathionylation. The ED(50) for doxorubicin dropped from 40 to 0.7 microM and for phenylarsine oxide from 200 to 5 nM. However, no differences were detected after treatment with cadmium, a known inhibitor of Grx1. These results indicate a crucial role of Grx2 in the regulation of the mitochondrial redox status and regulation of cell death at the mitochondrial checkpoint.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15328416</PMID><DateCompleted><Year>2004</Year><Month>09</Month><Day>30</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0027-8424</ISSN><JournalIssue CitedMedium="Print"><Volume>101</Volume><Issue>36</Issue><PubDate><Year>2004</Year><Month>Sep</Month><Day>07</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation></Journal><ArticleTitle>Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells toward doxorubicin and phenylarsine oxide.</ArticleTitle><Pagination><MedlinePgn>13227-32</MedlinePgn></Pagination><Abstract><AbstractText>Glutaredoxin (Grx) belongs to the thioredoxin fold superfamily and catalyzes glutathione-dependent oxidoreductions. The recently discovered mitochondrial and nuclear Grx (Grx2) differs from the more abundant cytosolic Grx (Grx1) by its higher affinity toward S-glutathionylated proteins and by being a substrate for thioredoxin reductase. Here, we have successfully established a method to silence the expression of Grx2 in HeLa cells by using short interfering RNA to study its role in the cell. Cells with levels of Grx2 <3% of the control were dramatically sensitized to cell death induced by doxorubicin/adriamycin and phenylarsine oxide but did not show signs of a general increase in oxidative damage with respect to carbonylation and glutathionylation. The ED(50) for doxorubicin dropped from 40 to 0.7 microM and for phenylarsine oxide from 200 to 5 nM. However, no differences were detected after treatment with cadmium, a known inhibitor of Grx1. 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IdType="pubmed">11878824</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country></list><tree><noCountry><name sortKey="Enoksson, Mari" sort="Enoksson, Mari" uniqKey="Enoksson M" first="Mari" last="Enoksson">Mari Enoksson</name><name sortKey="Fernandes, Aristi Potamitou" sort="Fernandes, Aristi Potamitou" uniqKey="Fernandes A" first="Aristi Potamitou" last="Fernandes">Aristi Potamitou Fernandes</name><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name><name sortKey="Lonn, Maria Elisabet" sort="Lonn, Maria Elisabet" uniqKey="Lonn M" first="Maria Elisabet" last="Lönn">Maria Elisabet Lönn</name></noCountry><country name="Suède"><noRegion><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst 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|texte= Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells toward doxorubicin and phenylarsine oxide.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:15328416" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |