Overexpression of glutaredoxin protects cardiomyocytes against nitric oxide-induced apoptosis with suppressing the S-nitrosylation of proteins and nuclear translocation of GAPDH.
Identifieur interne : 000837 ( Main/Exploration ); précédent : 000836; suivant : 000838Overexpression of glutaredoxin protects cardiomyocytes against nitric oxide-induced apoptosis with suppressing the S-nitrosylation of proteins and nuclear translocation of GAPDH.
Auteurs : Chiaki Inadomi [Japon] ; Hiroaki Murata ; Yoshito Ihara ; Shinji Goto ; Yoshishige Urata ; Junji Yodoi ; Takahito Kondo ; Koji SumikawaSource :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2012.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Apoptose (MeSH), Glutarédoxines (biosynthèse), Glutarédoxines (génétique), Glyceraldehyde 3-phosphate dehydrogenase (phosphorylating) (métabolisme), Lignée cellulaire (MeSH), Monoxyde d'azote (métabolisme), Myocytes cardiaques (cytologie), Myocytes cardiaques (physiologie), Noyau de la cellule (enzymologie), Oxydoréduction (MeSH), Rats (MeSH), Souris (MeSH), Transport nucléaire actif (MeSH).
- MESH :
- biosynthèse : Glutarédoxines.
- cytologie : Myocytes cardiaques.
- enzymologie : Noyau de la cellule.
- génétique : Glutarédoxines.
- métabolisme : Glyceraldehyde 3-phosphate dehydrogenase (phosphorylating), Monoxyde d'azote.
- physiologie : Myocytes cardiaques.
- Animaux, Apoptose, Lignée cellulaire, Oxydoréduction, Rats, Souris, Transport nucléaire actif.
English descriptors
- KwdEn :
- Active Transport, Cell Nucleus (MeSH), Animals (MeSH), Apoptosis (MeSH), Cell Line (MeSH), Cell Nucleus (enzymology), Glutaredoxins (biosynthesis), Glutaredoxins (genetics), Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) (metabolism), Mice (MeSH), Myocytes, Cardiac (cytology), Myocytes, Cardiac (physiology), Nitric Oxide (metabolism), Oxidation-Reduction (MeSH), Rats (MeSH).
- MESH :
- chemical , biosynthesis : Glutaredoxins.
- cytology : Myocytes, Cardiac.
- enzymology : Cell Nucleus.
- chemical , genetics : Glutaredoxins.
- chemical , metabolism : Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating), Nitric Oxide.
- physiology : Myocytes, Cardiac.
- Active Transport, Cell Nucleus, Animals, Apoptosis, Cell Line, Mice, Oxidation-Reduction, Rats.
Abstract
There is increasing evidence demonstrating that glutaredoxin 1 (GRX1), a cytosolic enzyme responsible for the catalysis of protein deglutathionylation, plays distinct roles in inflammation and apoptosis by inducing changes in the cellular redox system. In this study, we investigated whether and how the overexpression of GRX1 protects cardiomyocytes against nitric oxide (NO)-induced apoptosis. Cardiomyocytes (H9c2 cells) were transfected with the expression vector for mouse GRX1 cDNA, and mock-transfected cells were used as a control. Compared with the mock-transfected cells, the GRX1-transfected cells were more resistant to NO-induced apoptosis. Stimulation with NO significantly increased the nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a pro-apoptotic protein, in the mock-transfected cells, but did not change GAPDH localization in the GRX1-transfected cells. Furthermore, we found that NO stimulation clearly induced the oxidative modification of GAPDH in the mock-transfected cells, whereas less modification of GAPDH was observed in the GRX1-transfected cells. These data suggest that the overexpression of GRX1 could protect cardiomyocytes against NO-induced apoptosis, likely through the inhibition of the oxidative modification and the nuclear translocation of GAPDH.
DOI: 10.1016/j.bbrc.2012.07.118
PubMed: 22846575
Affiliations:
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Yoshito" uniqKey="Ihara Y" first="Yoshito" last="Ihara">Yoshito Ihara</name></author><author><name sortKey="Goto, Shinji" sort="Goto, Shinji" uniqKey="Goto S" first="Shinji" last="Goto">Shinji Goto</name></author><author><name sortKey="Urata, Yoshishige" sort="Urata, Yoshishige" uniqKey="Urata Y" first="Yoshishige" last="Urata">Yoshishige Urata</name></author><author><name sortKey="Yodoi, Junji" sort="Yodoi, Junji" uniqKey="Yodoi J" first="Junji" last="Yodoi">Junji Yodoi</name></author><author><name sortKey="Kondo, Takahito" sort="Kondo, Takahito" uniqKey="Kondo T" first="Takahito" last="Kondo">Takahito Kondo</name></author><author><name sortKey="Sumikawa, Koji" sort="Sumikawa, Koji" uniqKey="Sumikawa K" first="Koji" last="Sumikawa">Koji Sumikawa</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2012">2012</date><idno type="RBID">pubmed:22846575</idno><idno type="pmid">22846575</idno><idno type="doi">10.1016/j.bbrc.2012.07.118</idno><idno 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Nagasaki University School of Medicine, Nagasaki 852-8501</wicri:regionArea><wicri:noRegion>Nagasaki 852-8501</wicri:noRegion></affiliation></author><author><name sortKey="Murata, Hiroaki" sort="Murata, Hiroaki" uniqKey="Murata H" first="Hiroaki" last="Murata">Hiroaki Murata</name></author><author><name sortKey="Ihara, Yoshito" sort="Ihara, Yoshito" uniqKey="Ihara Y" first="Yoshito" last="Ihara">Yoshito Ihara</name></author><author><name sortKey="Goto, Shinji" sort="Goto, Shinji" uniqKey="Goto S" first="Shinji" last="Goto">Shinji Goto</name></author><author><name sortKey="Urata, Yoshishige" sort="Urata, Yoshishige" uniqKey="Urata Y" first="Yoshishige" last="Urata">Yoshishige Urata</name></author><author><name sortKey="Yodoi, Junji" sort="Yodoi, Junji" uniqKey="Yodoi J" first="Junji" last="Yodoi">Junji Yodoi</name></author><author><name sortKey="Kondo, Takahito" sort="Kondo, Takahito" uniqKey="Kondo T" first="Takahito" last="Kondo">Takahito Kondo</name></author><author><name sortKey="Sumikawa, Koji" sort="Sumikawa, Koji" uniqKey="Sumikawa K" first="Koji" last="Sumikawa">Koji Sumikawa</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="eISSN">1090-2104</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Active Transport, Cell Nucleus (MeSH)</term><term>Animals (MeSH)</term><term>Apoptosis (MeSH)</term><term>Cell Line (MeSH)</term><term>Cell Nucleus (enzymology)</term><term>Glutaredoxins (biosynthesis)</term><term>Glutaredoxins (genetics)</term><term>Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) (metabolism)</term><term>Mice (MeSH)</term><term>Myocytes, Cardiac (cytology)</term><term>Myocytes, Cardiac (physiology)</term><term>Nitric Oxide (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Rats (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Apoptose (MeSH)</term><term>Glutarédoxines (biosynthèse)</term><term>Glutarédoxines (génétique)</term><term>Glyceraldehyde 3-phosphate dehydrogenase (phosphorylating) (métabolisme)</term><term>Lignée cellulaire (MeSH)</term><term>Monoxyde d'azote (métabolisme)</term><term>Myocytes cardiaques (cytologie)</term><term>Myocytes cardiaques (physiologie)</term><term>Noyau de la cellule (enzymologie)</term><term>Oxydoréduction (MeSH)</term><term>Rats (MeSH)</term><term>Souris (MeSH)</term><term>Transport nucléaire actif (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Glutaredoxins</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Glutarédoxines</term></keywords><keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Myocytes cardiaques</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Myocytes, Cardiac</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Noyau de la cellule</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Cell Nucleus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glutarédoxines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)</term><term>Nitric Oxide</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glyceraldehyde 3-phosphate dehydrogenase (phosphorylating)</term><term>Monoxyde d'azote</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Myocytes cardiaques</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Myocytes, Cardiac</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Active Transport, Cell Nucleus</term><term>Animals</term><term>Apoptosis</term><term>Cell Line</term><term>Mice</term><term>Oxidation-Reduction</term><term>Rats</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Apoptose</term><term>Lignée cellulaire</term><term>Oxydoréduction</term><term>Rats</term><term>Souris</term><term>Transport nucléaire actif</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">There is increasing evidence demonstrating that glutaredoxin 1 (GRX1), a cytosolic enzyme responsible for the catalysis of protein deglutathionylation, plays distinct roles in inflammation and apoptosis by inducing changes in the cellular redox system. In this study, we investigated whether and how the overexpression of GRX1 protects cardiomyocytes against nitric oxide (NO)-induced apoptosis. Cardiomyocytes (H9c2 cells) were transfected with the expression vector for mouse GRX1 cDNA, and mock-transfected cells were used as a control. Compared with the mock-transfected cells, the GRX1-transfected cells were more resistant to NO-induced apoptosis. Stimulation with NO significantly increased the nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a pro-apoptotic protein, in the mock-transfected cells, but did not change GAPDH localization in the GRX1-transfected cells. Furthermore, we found that NO stimulation clearly induced the oxidative modification of GAPDH in the mock-transfected cells, whereas less modification of GAPDH was observed in the GRX1-transfected cells. These data suggest that the overexpression of GRX1 could protect cardiomyocytes against NO-induced apoptosis, likely through the inhibition of the oxidative modification and the nuclear translocation of GAPDH.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22846575</PMID><DateCompleted><Year>2012</Year><Month>12</Month><Day>28</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1090-2104</ISSN><JournalIssue CitedMedium="Internet"><Volume>425</Volume><Issue>3</Issue><PubDate><Year>2012</Year><Month>Aug</Month><Day>31</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Overexpression of glutaredoxin protects cardiomyocytes against nitric oxide-induced apoptosis with suppressing the S-nitrosylation of proteins and nuclear translocation of GAPDH.</ArticleTitle><Pagination><MedlinePgn>656-61</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbrc.2012.07.118</ELocationID><Abstract><AbstractText>There is increasing evidence demonstrating that glutaredoxin 1 (GRX1), a cytosolic enzyme responsible for the catalysis of protein deglutathionylation, plays distinct roles in inflammation and apoptosis by inducing changes in the cellular redox system. In this study, we investigated whether and how the overexpression of GRX1 protects cardiomyocytes against nitric oxide (NO)-induced apoptosis. Cardiomyocytes (H9c2 cells) were transfected with the expression vector for mouse GRX1 cDNA, and mock-transfected cells were used as a control. Compared with the mock-transfected cells, the GRX1-transfected cells were more resistant to NO-induced apoptosis. Stimulation with NO significantly increased the nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a pro-apoptotic protein, in the mock-transfected cells, but did not change GAPDH localization in the GRX1-transfected cells. Furthermore, we found that NO stimulation clearly induced the oxidative modification of GAPDH in the mock-transfected cells, whereas less modification of GAPDH was observed in the GRX1-transfected cells. These data suggest that the overexpression of GRX1 could protect cardiomyocytes against NO-induced apoptosis, likely through the inhibition of the oxidative modification and the nuclear translocation of GAPDH.</AbstractText><CopyrightInformation>Copyright © 2012 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Inadomi</LastName><ForeName>Chiaki</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Department of Anesthesiology, Nagasaki University School of Medicine, Nagasaki 852-8501, Japan. inadomic@nagasaki-u.ac.jp</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Murata</LastName><ForeName>Hiroaki</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Ihara</LastName><ForeName>Yoshito</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Goto</LastName><ForeName>Shinji</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Urata</LastName><ForeName>Yoshishige</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Yodoi</LastName><ForeName>Junji</ForeName><Initials>J</Initials></Author><Author 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UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>31C4KY9ESH</RegistryNumber><NameOfSubstance UI="D009569">Nitric Oxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.2.1.12</RegistryNumber><NameOfSubstance UI="D024581">Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D021581" MajorTopicYN="N">Active Transport, Cell Nucleus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017209" MajorTopicYN="Y">Apoptosis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002467" MajorTopicYN="N">Cell Nucleus</DescriptorName><QualifierName UI="Q000201" 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MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>07</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2012</Year><Month>07</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>8</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>8</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2012</Year><Month>12</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">22846575</ArticleId><ArticleId IdType="pii">S0006-291X(12)01425-8</ArticleId><ArticleId IdType="doi">10.1016/j.bbrc.2012.07.118</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country></list><tree><noCountry><name sortKey="Goto, Shinji" sort="Goto, Shinji" uniqKey="Goto S" first="Shinji" last="Goto">Shinji Goto</name><name sortKey="Ihara, Yoshito" sort="Ihara, Yoshito" uniqKey="Ihara Y" first="Yoshito" last="Ihara">Yoshito Ihara</name><name sortKey="Kondo, Takahito" sort="Kondo, Takahito" uniqKey="Kondo T" first="Takahito" last="Kondo">Takahito Kondo</name><name sortKey="Murata, Hiroaki" sort="Murata, Hiroaki" uniqKey="Murata H" first="Hiroaki" last="Murata">Hiroaki Murata</name><name sortKey="Sumikawa, Koji" sort="Sumikawa, Koji" uniqKey="Sumikawa K" first="Koji" last="Sumikawa">Koji Sumikawa</name><name sortKey="Urata, Yoshishige" sort="Urata, Yoshishige" uniqKey="Urata Y" first="Yoshishige" last="Urata">Yoshishige Urata</name><name sortKey="Yodoi, Junji" sort="Yodoi, Junji" uniqKey="Yodoi J" first="Junji" last="Yodoi">Junji Yodoi</name></noCountry><country name="Japon"><noRegion><name sortKey="Inadomi, Chiaki" sort="Inadomi, Chiaki" uniqKey="Inadomi C" first="Chiaki" last="Inadomi">Chiaki Inadomi</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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