Role of reversible, thioredoxin-sensitive oxidative protein modifications in cardiac myocytes.
Identifieur interne : 000C97 ( Main/Exploration ); précédent : 000C96; suivant : 000C98Role of reversible, thioredoxin-sensitive oxidative protein modifications in cardiac myocytes.
Auteurs : Gabriela M. Kuster [États-Unis] ; Deborah A. Siwik ; David R. Pimentel ; Wilson S. ColucciSource :
- Antioxidants & redox signaling [ 1523-0864 ]
Descripteurs français
- KwdFr :
- Animaux (MeSH), Espèces réactives de l'oxygène (métabolisme), Glutarédoxines (MeSH), Humains (MeSH), Myocytes cardiaques (effets des médicaments et des substances chimiques), Myocytes cardiaques (métabolisme), Oxidoreductases (pharmacologie), Oxydoréduction (MeSH), Protéines G monomériques (effets des médicaments et des substances chimiques), Protéines G monomériques (métabolisme), Thiorédoxines (pharmacologie), Transduction du signal (effets des médicaments et des substances chimiques), Transduction du signal (physiologie).
- MESH :
- effets des médicaments et des substances chimiques : Myocytes cardiaques, Protéines G monomériques, Transduction du signal.
- métabolisme : Espèces réactives de l'oxygène, Myocytes cardiaques, Protéines G monomériques.
- pharmacologie : Oxidoreductases, Thiorédoxines.
- physiologie : Transduction du signal.
- Animaux, Glutarédoxines, Humains, Oxydoréduction.
English descriptors
- KwdEn :
- Animals (MeSH), Glutaredoxins (MeSH), Humans (MeSH), Monomeric GTP-Binding Proteins (drug effects), Monomeric GTP-Binding Proteins (metabolism), Myocytes, Cardiac (drug effects), Myocytes, Cardiac (metabolism), Oxidation-Reduction (MeSH), Oxidoreductases (pharmacology), Reactive Oxygen Species (metabolism), Signal Transduction (drug effects), Signal Transduction (physiology), Thioredoxins (pharmacology).
- MESH :
- chemical , drug effects : Monomeric GTP-Binding Proteins.
- chemical , metabolism : Monomeric GTP-Binding Proteins, Reactive Oxygen Species.
- chemical , pharmacology : Oxidoreductases, Thioredoxins.
- chemical : Glutaredoxins.
- drug effects : Myocytes, Cardiac, Signal Transduction.
- metabolism : Myocytes, Cardiac.
- physiology : Signal Transduction.
- Animals, Humans, Oxidation-Reduction.
Abstract
Reactive oxygen species (ROS) are important mediators of myocardial remodeling. However, the precise molecular mechanisms by which ROS exert their effects are incompletely understood. ROS induce oxidative posttranslational protein modifications that can regulate the function of structural, functional, and signaling proteins. For example, oxidative modification of free reactive thiols (S-thiolation) on the small G protein Ras increases Ras activity and thereby promotes ROS-dependent hypertrophic signaling in cardiac myocytes. By reducing thiols and restoring reversible thiol modifications, thioredoxin and glutaredoxin can act as regulators of ROS-mediated protein function. Understanding the regulation and functional relevance of oxidative protein modifications in myocardial remodeling may lead to new therapeutic strategies.
DOI: 10.1089/ars.2006.8.2153
PubMed: 17034357
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Siwik</name></author><author><name sortKey="Pimentel, David R" sort="Pimentel, David R" uniqKey="Pimentel D" first="David R" last="Pimentel">David R. Pimentel</name></author><author><name sortKey="Colucci, Wilson S" sort="Colucci, Wilson S" uniqKey="Colucci W" first="Wilson S" last="Colucci">Wilson S. Colucci</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006 Nov-Dec</date><idno type="RBID">pubmed:17034357</idno><idno type="pmid">17034357</idno><idno type="doi">10.1089/ars.2006.8.2153</idno><idno type="wicri:Area/Main/Corpus">000D10</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000D10</idno><idno type="wicri:Area/Main/Curation">000D10</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000D10</idno><idno type="wicri:Area/Main/Exploration">000D10</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Role of reversible, thioredoxin-sensitive oxidative protein modifications in cardiac myocytes.</title><author><name sortKey="Kuster, Gabriela M" sort="Kuster, Gabriela M" uniqKey="Kuster G" first="Gabriela M" last="Kuster">Gabriela M. Kuster</name><affiliation wicri:level="1"><nlm:affiliation>Cardiovascular Medicine Section and the Myocardial Biology Unit, Boston University Medical Center, Boston, Massachusetts 02118, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Cardiovascular Medicine Section and the Myocardial Biology Unit, Boston University Medical Center, Boston, Massachusetts 02118</wicri:regionArea><wicri:noRegion>Massachusetts 02118</wicri:noRegion></affiliation></author><author><name sortKey="Siwik, Deborah A" sort="Siwik, Deborah A" uniqKey="Siwik D" first="Deborah A" last="Siwik">Deborah A. Siwik</name></author><author><name sortKey="Pimentel, David R" sort="Pimentel, David R" uniqKey="Pimentel D" first="David R" last="Pimentel">David R. Pimentel</name></author><author><name sortKey="Colucci, Wilson S" sort="Colucci, Wilson S" uniqKey="Colucci W" first="Wilson S" last="Colucci">Wilson S. 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However, the precise molecular mechanisms by which ROS exert their effects are incompletely understood. ROS induce oxidative posttranslational protein modifications that can regulate the function of structural, functional, and signaling proteins. For example, oxidative modification of free reactive thiols (S-thiolation) on the small G protein Ras increases Ras activity and thereby promotes ROS-dependent hypertrophic signaling in cardiac myocytes. By reducing thiols and restoring reversible thiol modifications, thioredoxin and glutaredoxin can act as regulators of ROS-mediated protein function. Understanding the regulation and functional relevance of oxidative protein modifications in myocardial remodeling may lead to new therapeutic strategies.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17034357</PMID><DateCompleted><Year>2007</Year><Month>01</Month><Day>30</Day></DateCompleted><DateRevised><Year>2007</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1523-0864</ISSN><JournalIssue CitedMedium="Print"><Volume>8</Volume><Issue>11-12</Issue><PubDate><MedlineDate>2006 Nov-Dec</MedlineDate></PubDate></JournalIssue><Title>Antioxidants & redox signaling</Title><ISOAbbreviation>Antioxid Redox Signal</ISOAbbreviation></Journal><ArticleTitle>Role of reversible, thioredoxin-sensitive oxidative protein modifications in cardiac myocytes.</ArticleTitle><Pagination><MedlinePgn>2153-9</MedlinePgn></Pagination><Abstract><AbstractText>Reactive oxygen species (ROS) are important mediators of myocardial remodeling. However, the precise molecular mechanisms by which ROS exert their effects are incompletely understood. ROS induce oxidative posttranslational protein modifications that can regulate the function of structural, functional, and signaling proteins. For example, oxidative modification of free reactive thiols (S-thiolation) on the small G protein Ras increases Ras activity and thereby promotes ROS-dependent hypertrophic signaling in cardiac myocytes. By reducing thiols and restoring reversible thiol modifications, thioredoxin and glutaredoxin can act as regulators of ROS-mediated protein function. Understanding the regulation and functional relevance of oxidative protein modifications in myocardial remodeling may lead to new therapeutic strategies.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kuster</LastName><ForeName>Gabriela M</ForeName><Initials>GM</Initials><AffiliationInfo><Affiliation>Cardiovascular Medicine Section and the Myocardial Biology Unit, Boston University Medical Center, Boston, Massachusetts 02118, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Siwik</LastName><ForeName>Deborah A</ForeName><Initials>DA</Initials></Author><Author ValidYN="Y"><LastName>Pimentel</LastName><ForeName>David R</ForeName><Initials>DR</Initials></Author><Author ValidYN="Y"><LastName>Colucci</LastName><ForeName>Wilson S</ForeName><Initials>WS</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</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="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017382">Reactive Oxygen Species</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.5.2</RegistryNumber><NameOfSubstance UI="D020559">Monomeric GTP-Binding Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020559" MajorTopicYN="N">Monomeric GTP-Binding Proteins</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032383" MajorTopicYN="N">Myocytes, Cardiac</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017382" MajorTopicYN="N">Reactive Oxygen Species</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading></MeshHeadingList><NumberOfReferences>70</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>10</Month><Day>13</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>1</Month><Day>31</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>10</Month><Day>13</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17034357</ArticleId><ArticleId IdType="doi">10.1089/ars.2006.8.2153</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Colucci, Wilson S" sort="Colucci, Wilson S" uniqKey="Colucci W" first="Wilson S" last="Colucci">Wilson S. Colucci</name><name sortKey="Pimentel, David R" sort="Pimentel, David R" uniqKey="Pimentel D" first="David R" last="Pimentel">David R. Pimentel</name><name sortKey="Siwik, Deborah A" sort="Siwik, Deborah A" uniqKey="Siwik D" first="Deborah A" last="Siwik">Deborah A. Siwik</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Kuster, Gabriela M" sort="Kuster, Gabriela M" uniqKey="Kuster G" first="Gabriela M" last="Kuster">Gabriela M. Kuster</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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