Oxidative regulation of the Na(+)-K(+) pump in the cardiovascular system.
Identifieur interne : 000836 ( Main/Exploration ); précédent : 000835; suivant : 000837Oxidative regulation of the Na(+)-K(+) pump in the cardiovascular system.
Auteurs : Gemma A. Figtree [Australie] ; Galougahi Keyvan Karimi [Australie] ; Chia-Chi Liu [Australie] ; Helge H. Rasmussen [Australie]Source :
- Free radical biology & medicine [ 1873-4596 ] ; 2012.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Conformation des protéines (MeSH), Défaillance cardiaque (enzymologie), Glutathion (métabolisme), Humains (MeSH), Lésion de reperfusion myocardique (enzymologie), Maturation post-traductionnelle des protéines (MeSH), Oxydoréduction (MeSH), Phosphorylation (MeSH), Sodium-Potassium-Exchanging ATPase (composition chimique), Sodium-Potassium-Exchanging ATPase (métabolisme), Stress oxydatif (MeSH), Système cardiovasculaire (enzymologie).
- MESH :
- composition chimique : Sodium-Potassium-Exchanging ATPase.
- enzymologie : Défaillance cardiaque, Lésion de reperfusion myocardique, Système cardiovasculaire.
- métabolisme : Glutathion, Sodium-Potassium-Exchanging ATPase.
- Animaux, Conformation des protéines, Humains, Maturation post-traductionnelle des protéines, Oxydoréduction, Phosphorylation, Stress oxydatif.
English descriptors
- KwdEn :
- Animals (MeSH), Cardiovascular System (enzymology), Glutathione (metabolism), Heart Failure (enzymology), Humans (MeSH), Myocardial Reperfusion Injury (enzymology), Oxidation-Reduction (MeSH), Oxidative Stress (MeSH), Phosphorylation (MeSH), Protein Conformation (MeSH), Protein Processing, Post-Translational (MeSH), Sodium-Potassium-Exchanging ATPase (chemistry), Sodium-Potassium-Exchanging ATPase (metabolism).
- MESH :
- chemical , chemistry : Sodium-Potassium-Exchanging ATPase.
- chemical , metabolism : Glutathione, Sodium-Potassium-Exchanging ATPase.
- enzymology : Cardiovascular System, Heart Failure, Myocardial Reperfusion Injury.
- Animals, Humans, Oxidation-Reduction, Oxidative Stress, Phosphorylation, Protein Conformation, Protein Processing, Post-Translational.
Abstract
The Na(+)-K(+) pump is an essential heterodimeric membrane protein, which maintains electrochemical gradients for Na(+) and K(+) across cell membranes in all tissues. We have identified glutathionylation, a reversible posttranslational redox modification, of the Na(+)-K(+) pump's β1 subunit as a regulatory mechanism of pump activity. Oxidative inhibition of the Na(+)-K(+) pump by angiotensin II- and β1-adrenergic receptor-coupled signaling via NADPH oxidase activation demonstrates the relevance of this regulatory mechanism in cardiovascular physiology and pathophysiology. This has implications for dysregulation of intracellular Na(+) and Ca(2+) as well as increased oxidative stress in heart failure, myocardial ischemia-reperfusion, and regulation of vascular tone under conditions of elevated oxidative stress. Treatment strategies that are able to reverse this oxidative inhibition of the Na(+)-K(+) pump have the potential for cardiovascular-protective effects.
DOI: 10.1016/j.freeradbiomed.2012.10.539
PubMed: 23085513
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Figtree</name><affiliation wicri:level="4"><nlm:affiliation>North Shore Heart Research Group, Kolling Institute of Medical Research, University of Sydney, St Leonards, NSW 2065, Australia; Department of Cardiology, Royal North Shore Hospital, Sydney, NSW, Australia. Electronic address: gfigtree@med.usyd.edu.au.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>North Shore Heart Research Group, Kolling Institute of Medical Research, University of Sydney, St Leonards, NSW 2065, Australia; Department of Cardiology, Royal North Shore Hospital, Sydney, NSW</wicri:regionArea><orgName type="university">Université de Sydney</orgName><placeName><settlement type="city">Sydney</settlement><region type="état">Nouvelle-Galles du Sud</region></placeName></affiliation></author><author><name sortKey="Keyvan Karimi, Galougahi" sort="Keyvan Karimi, Galougahi" uniqKey="Keyvan Karimi G" first="Galougahi" last="Keyvan Karimi">Galougahi Keyvan Karimi</name><affiliation wicri:level="4"><nlm:affiliation>North Shore Heart Research Group, Kolling Institute of Medical Research, University of Sydney, St Leonards, NSW 2065, Australia; Department of Cardiology, Royal North Shore Hospital, Sydney, NSW, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>North Shore Heart Research Group, Kolling Institute of Medical Research, University of Sydney, St Leonards, NSW 2065, Australia; Department of Cardiology, Royal North Shore Hospital, Sydney, NSW</wicri:regionArea><orgName type="university">Université de Sydney</orgName><placeName><settlement type="city">Sydney</settlement><region type="état">Nouvelle-Galles du Sud</region></placeName></affiliation></author><author><name sortKey="Liu, Chia Chi" sort="Liu, Chia Chi" uniqKey="Liu C" first="Chia-Chi" last="Liu">Chia-Chi Liu</name><affiliation wicri:level="4"><nlm:affiliation>North Shore Heart Research Group, Kolling Institute of Medical Research, University of Sydney, St Leonards, NSW 2065, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>North Shore Heart Research Group, Kolling Institute of Medical Research, University of Sydney, St Leonards, NSW 2065</wicri:regionArea><orgName type="university">Université de Sydney</orgName><placeName><settlement type="city">Sydney</settlement><region type="état">Nouvelle-Galles du Sud</region></placeName></affiliation></author><author><name sortKey="Rasmussen, Helge H" sort="Rasmussen, Helge H" uniqKey="Rasmussen H" first="Helge H" last="Rasmussen">Helge H. Rasmussen</name><affiliation wicri:level="4"><nlm:affiliation>North Shore Heart Research Group, Kolling Institute of Medical Research, University of Sydney, St Leonards, NSW 2065, Australia; Department of Cardiology, Royal North Shore Hospital, Sydney, NSW, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>North Shore Heart Research Group, Kolling Institute of Medical Research, University of Sydney, St Leonards, NSW 2065, Australia; Department of Cardiology, Royal North Shore Hospital, Sydney, NSW</wicri:regionArea><orgName type="university">Université de Sydney</orgName><placeName><settlement type="city">Sydney</settlement><region type="état">Nouvelle-Galles du Sud</region></placeName></affiliation></author></analytic><series><title level="j">Free radical biology & medicine</title><idno type="eISSN">1873-4596</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Cardiovascular System (enzymology)</term><term>Glutathione (metabolism)</term><term>Heart Failure (enzymology)</term><term>Humans (MeSH)</term><term>Myocardial Reperfusion Injury (enzymology)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidative Stress (MeSH)</term><term>Phosphorylation (MeSH)</term><term>Protein Conformation (MeSH)</term><term>Protein Processing, Post-Translational (MeSH)</term><term>Sodium-Potassium-Exchanging ATPase (chemistry)</term><term>Sodium-Potassium-Exchanging ATPase (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Défaillance cardiaque (enzymologie)</term><term>Glutathion (métabolisme)</term><term>Humains (MeSH)</term><term>Lésion de reperfusion myocardique (enzymologie)</term><term>Maturation post-traductionnelle des protéines (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Phosphorylation (MeSH)</term><term>Sodium-Potassium-Exchanging ATPase (composition chimique)</term><term>Sodium-Potassium-Exchanging ATPase (métabolisme)</term><term>Stress oxydatif (MeSH)</term><term>Système cardiovasculaire (enzymologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Sodium-Potassium-Exchanging ATPase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term><term>Sodium-Potassium-Exchanging ATPase</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Sodium-Potassium-Exchanging ATPase</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Défaillance cardiaque</term><term>Lésion de reperfusion myocardique</term><term>Système cardiovasculaire</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Cardiovascular System</term><term>Heart Failure</term><term>Myocardial Reperfusion Injury</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutathion</term><term>Sodium-Potassium-Exchanging ATPase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term><term>Oxidation-Reduction</term><term>Oxidative Stress</term><term>Phosphorylation</term><term>Protein Conformation</term><term>Protein Processing, Post-Translational</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Conformation des protéines</term><term>Humains</term><term>Maturation post-traductionnelle des protéines</term><term>Oxydoréduction</term><term>Phosphorylation</term><term>Stress oxydatif</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The Na(+)-K(+) pump is an essential heterodimeric membrane protein, which maintains electrochemical gradients for Na(+) and K(+) across cell membranes in all tissues. We have identified glutathionylation, a reversible posttranslational redox modification, of the Na(+)-K(+) pump's β1 subunit as a regulatory mechanism of pump activity. Oxidative inhibition of the Na(+)-K(+) pump by angiotensin II- and β1-adrenergic receptor-coupled signaling via NADPH oxidase activation demonstrates the relevance of this regulatory mechanism in cardiovascular physiology and pathophysiology. This has implications for dysregulation of intracellular Na(+) and Ca(2+) as well as increased oxidative stress in heart failure, myocardial ischemia-reperfusion, and regulation of vascular tone under conditions of elevated oxidative stress. Treatment strategies that are able to reverse this oxidative inhibition of the Na(+)-K(+) pump have the potential for cardiovascular-protective effects. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23085513</PMID><DateCompleted><Year>2014</Year><Month>06</Month><Day>17</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-4596</ISSN><JournalIssue CitedMedium="Internet"><Volume>53</Volume><Issue>12</Issue><PubDate><Year>2012</Year><Month>Dec</Month><Day>15</Day></PubDate></JournalIssue><Title>Free radical biology & medicine</Title><ISOAbbreviation>Free Radic Biol Med</ISOAbbreviation></Journal><ArticleTitle>Oxidative regulation of the Na(+)-K(+) pump in the cardiovascular system.</ArticleTitle><Pagination><MedlinePgn>2263-8</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.freeradbiomed.2012.10.539</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0891-5849(12)01770-4</ELocationID><Abstract><AbstractText>The Na(+)-K(+) pump is an essential heterodimeric membrane protein, which maintains electrochemical gradients for Na(+) and K(+) across cell membranes in all tissues. We have identified glutathionylation, a reversible posttranslational redox modification, of the Na(+)-K(+) pump's β1 subunit as a regulatory mechanism of pump activity. Oxidative inhibition of the Na(+)-K(+) pump by angiotensin II- and β1-adrenergic receptor-coupled signaling via NADPH oxidase activation demonstrates the relevance of this regulatory mechanism in cardiovascular physiology and pathophysiology. This has implications for dysregulation of intracellular Na(+) and Ca(2+) as well as increased oxidative stress in heart failure, myocardial ischemia-reperfusion, and regulation of vascular tone under conditions of elevated oxidative stress. Treatment strategies that are able to reverse this oxidative inhibition of the Na(+)-K(+) pump have the potential for cardiovascular-protective effects. </AbstractText><CopyrightInformation>Copyright © 2012 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Figtree</LastName><ForeName>Gemma A</ForeName><Initials>GA</Initials><AffiliationInfo><Affiliation>North Shore Heart Research Group, Kolling Institute of Medical Research, University of Sydney, St Leonards, NSW 2065, Australia; Department of Cardiology, Royal North Shore Hospital, Sydney, NSW, Australia. Electronic address: gfigtree@med.usyd.edu.au.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Keyvan Karimi</LastName><ForeName>Galougahi</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>North Shore Heart Research Group, Kolling Institute of Medical Research, University of Sydney, St Leonards, NSW 2065, Australia; Department of Cardiology, Royal North Shore Hospital, Sydney, NSW, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Chia-Chi</ForeName><Initials>CC</Initials><AffiliationInfo><Affiliation>North Shore Heart Research Group, Kolling Institute of Medical Research, University of Sydney, St Leonards, NSW 2065, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rasmussen</LastName><ForeName>Helge H</ForeName><Initials>HH</Initials><AffiliationInfo><Affiliation>North Shore Heart Research Group, Kolling Institute of Medical Research, University of Sydney, St Leonards, NSW 2065, Australia; Department of Cardiology, Royal North Shore Hospital, Sydney, NSW, Australia.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2012</Year><Month>10</Month><Day>17</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Free Radic Biol Med</MedlineTA><NlmUniqueID>8709159</NlmUniqueID><ISSNLinking>0891-5849</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>EC 7.2.2.13</RegistryNumber><NameOfSubstance UI="D000254">Sodium-Potassium-Exchanging ATPase</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002319" MajorTopicYN="N">Cardiovascular System</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006333" MajorTopicYN="N">Heart Failure</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015428" MajorTopicYN="N">Myocardial Reperfusion Injury</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011499" MajorTopicYN="N">Protein Processing, Post-Translational</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000254" MajorTopicYN="N">Sodium-Potassium-Exchanging ATPase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Free radicals</Keyword><Keyword MajorTopicYN="N">Glutaredoxin</Keyword><Keyword MajorTopicYN="N">Glutathionylation</Keyword><Keyword MajorTopicYN="N">NADPH oxidase</Keyword><Keyword MajorTopicYN="N">Na(+)–K(+) pump</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>07</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2012</Year><Month>10</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2012</Year><Month>10</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>10</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>10</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>6</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23085513</ArticleId><ArticleId IdType="pii">S0891-5849(12)01770-4</ArticleId><ArticleId IdType="doi">10.1016/j.freeradbiomed.2012.10.539</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Australie</li></country><region><li>Nouvelle-Galles du Sud</li></region><settlement><li>Sydney</li></settlement><orgName><li>Université de Sydney</li></orgName></list><tree><country name="Australie"><region name="Nouvelle-Galles du Sud"><name sortKey="Figtree, Gemma A" sort="Figtree, Gemma A" uniqKey="Figtree G" first="Gemma A" last="Figtree">Gemma A. Figtree</name></region><name sortKey="Keyvan Karimi, Galougahi" sort="Keyvan Karimi, Galougahi" uniqKey="Keyvan Karimi G" first="Galougahi" last="Keyvan Karimi">Galougahi Keyvan Karimi</name><name sortKey="Liu, Chia Chi" sort="Liu, Chia Chi" uniqKey="Liu C" first="Chia-Chi" last="Liu">Chia-Chi Liu</name><name sortKey="Rasmussen, Helge H" sort="Rasmussen, Helge H" uniqKey="Rasmussen H" first="Helge H" last="Rasmussen">Helge H. Rasmussen</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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