Poly(ADP-ribose) glycohydrolase silencing protects against H2O2-induced cell death.
Identifieur interne : 000419 ( Ncbi/Merge ); précédent : 000418; suivant : 000420Poly(ADP-ribose) glycohydrolase silencing protects against H2O2-induced cell death.
Auteurs : Christian Blenn [Suisse] ; Felix R. Althaus ; Maria MalangaSource :
- The Biochemical journal [ 1470-8728 ] ; 2006.
Descripteurs français
- KwdFr :
- 1-Méthyl-3-nitro-1-nitroso-guanidine (pharmacologie), Animaux, Apoptose (), Cellules HeLa, Cellules cultivées, Glycosidases (génétique), Glycosidases (physiologie), Humains, Interférence par ARN, Peroxyde d'hydrogène (pharmacologie), Poly adénosine diphosphate ribose (métabolisme), Souris, Souris knockout, Survie cellulaire ().
- MESH :
- génétique : Glycosidases.
- métabolisme : Poly adénosine diphosphate ribose.
- pharmacologie : 1-Méthyl-3-nitro-1-nitroso-guanidine, Peroxyde d'hydrogène.
- physiologie : Glycosidases.
- Animaux, Apoptose, Cellules HeLa, Cellules cultivées, Humains, Interférence par ARN, Souris, Souris knockout, Survie cellulaire.
English descriptors
- KwdEn :
- Animals, Apoptosis (drug effects), Cell Survival (drug effects), Cells, Cultured, Glycoside Hydrolases (genetics), Glycoside Hydrolases (physiology), HeLa Cells, Humans, Hydrogen Peroxide (pharmacology), Methylnitronitrosoguanidine (pharmacology), Mice, Mice, Knockout, Poly Adenosine Diphosphate Ribose (metabolism), RNA Interference.
- MESH :
- chemical , genetics : Glycoside Hydrolases.
- drug effects : Apoptosis, Cell Survival.
- chemical , metabolism : Poly Adenosine Diphosphate Ribose.
- chemical , pharmacology : Hydrogen Peroxide, Methylnitronitrosoguanidine.
- chemical , physiology : Glycoside Hydrolases.
- Animals, Cells, Cultured, HeLa Cells, Humans, Mice, Mice, Knockout, RNA Interference.
Abstract
PAR [poly(ADP-ribose)] is a structural and regulatory component of multiprotein complexes in eukaryotic cells. PAR catabolism is accelerated under genotoxic stress conditions and this is largely attributable to the activity of a PARG (PAR glycohydrolase). To overcome the early embryonic lethality of parg-knockout mice and gain more insights into the biological functions of PARG, we used an RNA interference approach. We found that as little as 10% of PARG protein is sufficient to ensure basic cellular functions: PARG-silenced murine and human cells proliferated normally through several subculturing rounds and they were able to repair DNA damage induced by sublethal doses of H2O2. However, cell survival following treatment with higher concentrations of H2O2 (0.05-1 mM) was increased. In fact, PARG-silenced cells were more resistant than their wild-type counterparts to oxidant-induced apoptosis while exhibiting delayed PAR degradation and transient accumulation of ADP-ribose polymers longer than 15-mers at early stages of drug treatment. No difference was observed in response to the DNA alkylating agent N-methyl-N'-nitro-N-nitrosoguanidine, suggesting a specific involvement of PARG in the cellular response to oxidative DNA damage.
DOI: 10.1042/BJ20051696
PubMed: 16526943
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Althaus</name></author><author><name sortKey="Malanga, Maria" sort="Malanga, Maria" uniqKey="Malanga M" first="Maria" last="Malanga">Maria Malanga</name></author></analytic><series><title level="j">The Biochemical journal</title><idno type="eISSN">1470-8728</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Apoptosis (drug effects)</term><term>Cell Survival (drug effects)</term><term>Cells, Cultured</term><term>Glycoside Hydrolases (genetics)</term><term>Glycoside Hydrolases (physiology)</term><term>HeLa Cells</term><term>Humans</term><term>Hydrogen Peroxide (pharmacology)</term><term>Methylnitronitrosoguanidine (pharmacology)</term><term>Mice</term><term>Mice, Knockout</term><term>Poly Adenosine Diphosphate Ribose (metabolism)</term><term>RNA Interference</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>1-Méthyl-3-nitro-1-nitroso-guanidine (pharmacologie)</term><term>Animaux</term><term>Apoptose ()</term><term>Cellules HeLa</term><term>Cellules cultivées</term><term>Glycosidases (génétique)</term><term>Glycosidases (physiologie)</term><term>Humains</term><term>Interférence par ARN</term><term>Peroxyde d'hydrogène (pharmacologie)</term><term>Poly adénosine diphosphate ribose (métabolisme)</term><term>Souris</term><term>Souris knockout</term><term>Survie cellulaire ()</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glycoside Hydrolases</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Apoptosis</term><term>Cell Survival</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycosidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Poly Adenosine Diphosphate Ribose</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Poly adénosine diphosphate ribose</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>1-Méthyl-3-nitro-1-nitroso-guanidine</term><term>Peroxyde d'hydrogène</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Hydrogen Peroxide</term><term>Methylnitronitrosoguanidine</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Glycosidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Glycoside Hydrolases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cells, Cultured</term><term>HeLa Cells</term><term>Humans</term><term>Mice</term><term>Mice, Knockout</term><term>RNA Interference</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Apoptose</term><term>Cellules HeLa</term><term>Cellules cultivées</term><term>Humains</term><term>Interférence par ARN</term><term>Souris</term><term>Souris knockout</term><term>Survie cellulaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">PAR [poly(ADP-ribose)] is a structural and regulatory component of multiprotein complexes in eukaryotic cells. PAR catabolism is accelerated under genotoxic stress conditions and this is largely attributable to the activity of a PARG (PAR glycohydrolase). To overcome the early embryonic lethality of parg-knockout mice and gain more insights into the biological functions of PARG, we used an RNA interference approach. We found that as little as 10% of PARG protein is sufficient to ensure basic cellular functions: PARG-silenced murine and human cells proliferated normally through several subculturing rounds and they were able to repair DNA damage induced by sublethal doses of H2O2. However, cell survival following treatment with higher concentrations of H2O2 (0.05-1 mM) was increased. In fact, PARG-silenced cells were more resistant than their wild-type counterparts to oxidant-induced apoptosis while exhibiting delayed PAR degradation and transient accumulation of ADP-ribose polymers longer than 15-mers at early stages of drug treatment. No difference was observed in response to the DNA alkylating agent N-methyl-N'-nitro-N-nitrosoguanidine, suggesting a specific involvement of PARG in the cellular response to oxidative DNA damage.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16526943</PMID><DateCompleted><Year>2006</Year><Month>06</Month><Day>12</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1470-8728</ISSN><JournalIssue CitedMedium="Internet"><Volume>396</Volume><Issue>3</Issue><PubDate><Year>2006</Year><Month>Jun</Month><Day>15</Day></PubDate></JournalIssue><Title>The Biochemical journal</Title><ISOAbbreviation>Biochem. J.</ISOAbbreviation></Journal><ArticleTitle>Poly(ADP-ribose) glycohydrolase silencing protects against H2O2-induced cell death.</ArticleTitle><Pagination><MedlinePgn>419-29</MedlinePgn></Pagination><Abstract><AbstractText>PAR [poly(ADP-ribose)] is a structural and regulatory component of multiprotein complexes in eukaryotic cells. PAR catabolism is accelerated under genotoxic stress conditions and this is largely attributable to the activity of a PARG (PAR glycohydrolase). To overcome the early embryonic lethality of parg-knockout mice and gain more insights into the biological functions of PARG, we used an RNA interference approach. We found that as little as 10% of PARG protein is sufficient to ensure basic cellular functions: PARG-silenced murine and human cells proliferated normally through several subculturing rounds and they were able to repair DNA damage induced by sublethal doses of H2O2. However, cell survival following treatment with higher concentrations of H2O2 (0.05-1 mM) was increased. In fact, PARG-silenced cells were more resistant than their wild-type counterparts to oxidant-induced apoptosis while exhibiting delayed PAR degradation and transient accumulation of ADP-ribose polymers longer than 15-mers at early stages of drug treatment. 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Althaus</name><name sortKey="Malanga, Maria" sort="Malanga, Maria" uniqKey="Malanga M" first="Maria" last="Malanga">Maria Malanga</name></noCountry><country name="Suisse"><noRegion><name sortKey="Blenn, Christian" sort="Blenn, Christian" uniqKey="Blenn C" first="Christian" last="Blenn">Christian Blenn</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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