GlutaredoxinV1, Main, Exploration, bibRecord, 000A87

Reversible oxidative modification: a key mechanism of Na+-K+ pump regulation.

Identifieur interne : 000A87 ( Main/Exploration ); précédent : 000A86; suivant : 000A88

Reversible oxidative modification: a key mechanism of Na+-K+ pump regulation.

Auteurs : Gemma A. Figtree [Australie] ; Chia-Chi Liu ; Stephanie Bibert ; Elisha J. Hamilton ; Alvaro Garcia ; Caroline N. White ; Karin K M. Chia ; Flemming Cornelius ; Kaethi Geering ; Helge H. Rasmussen

Source :

Circulation research [ 1524-4571 ] ; 2009.

RBID : pubmed:19542013

Descripteurs français

KwdFr :
- Acide peroxynitreux (métabolisme), Adenosine triphosphatases (métabolisme), Angiotensine-II (métabolisme), Animaux (MeSH), Cinétique (MeSH), Conformation des protéines (MeSH), Cystéine (MeSH), Glutarédoxines (métabolisme), Glutathion (métabolisme), Humains (MeSH), Lapins (MeSH), Maturation post-traductionnelle des protéines (MeSH), Molécules d'adhérence cellulaire neuronale (métabolisme), Mutation (MeSH), Myocytes cardiaques (effets des médicaments et des substances chimiques), Myocytes cardiaques (enzymologie), Mâle (MeSH), NADPH oxidase (métabolisme), Ovis (MeSH), Ovocytes (MeSH), Oxydoréduction (MeSH), Paraquat (pharmacologie), Protéine kinase C (métabolisme), Rein (effets des médicaments et des substances chimiques), Rein (enzymologie), Relation structure-activité (MeSH), Sodium-Potassium-Exchanging ATPase (composition chimique), Sodium-Potassium-Exchanging ATPase (génétique), Sodium-Potassium-Exchanging ATPase (métabolisme), Suidae (MeSH), Superoxide dismutase (métabolisme), Transduction du signal (MeSH), Transporteurs de cations (métabolisme), Xenopus laevis (MeSH).
MESH :
- composition chimique : Sodium-Potassium-Exchanging ATPase.
- effets des médicaments et des substances chimiques : Myocytes cardiaques, Rein.
- enzymologie : Myocytes cardiaques, Rein.
- génétique : Sodium-Potassium-Exchanging ATPase.
- métabolisme : Acide peroxynitreux, Adenosine triphosphatases, Angiotensine-II, Glutarédoxines, Glutathion, Molécules d'adhérence cellulaire neuronale, NADPH oxidase, Protéine kinase C, Sodium-Potassium-Exchanging ATPase, Superoxide dismutase, Transporteurs de cations.
- pharmacologie : Paraquat.
- Animaux, Cinétique, Conformation des protéines, Cystéine, Humains, Lapins, Maturation post-traductionnelle des protéines, Mutation, Mâle, Ovis, Ovocytes, Oxydoréduction, Relation structure-activité, Suidae, Transduction du signal, Xenopus laevis.

English descriptors

KwdEn :
- Adenosine Triphosphatases (metabolism), Angiotensin II (metabolism), Animals (MeSH), Cation Transport Proteins (metabolism), Cell Adhesion Molecules, Neuronal (metabolism), Cysteine (MeSH), Glutaredoxins (metabolism), Glutathione (metabolism), Humans (MeSH), Kidney (drug effects), Kidney (enzymology), Kinetics (MeSH), Male (MeSH), Mutation (MeSH), Myocytes, Cardiac (drug effects), Myocytes, Cardiac (enzymology), NADPH Oxidases (metabolism), Oocytes (MeSH), Oxidation-Reduction (MeSH), Paraquat (pharmacology), Peroxynitrous Acid (metabolism), Protein Conformation (MeSH), Protein Kinase C (metabolism), Protein Processing, Post-Translational (MeSH), Rabbits (MeSH), Sheep (MeSH), Signal Transduction (MeSH), Sodium-Potassium-Exchanging ATPase (chemistry), Sodium-Potassium-Exchanging ATPase (genetics), Sodium-Potassium-Exchanging ATPase (metabolism), Structure-Activity Relationship (MeSH), Superoxide Dismutase (metabolism), Swine (MeSH), Xenopus laevis (MeSH).
MESH :
- chemical , chemistry : Sodium-Potassium-Exchanging ATPase.
- chemical , genetics : Sodium-Potassium-Exchanging ATPase.
- chemical , metabolism : Adenosine Triphosphatases, Angiotensin II, Cation Transport Proteins, Cell Adhesion Molecules, Neuronal, Glutaredoxins, Glutathione, NADPH Oxidases, Peroxynitrous Acid, Protein Kinase C, Sodium-Potassium-Exchanging ATPase, Superoxide Dismutase.
- drug effects : Kidney, Myocytes, Cardiac.
- enzymology : Kidney, Myocytes, Cardiac.
- chemical , pharmacology : Paraquat.
- Animals, Cysteine, Humans, Kinetics, Male, Mutation, Oocytes, Oxidation-Reduction, Protein Conformation, Protein Processing, Post-Translational, Rabbits, Sheep, Signal Transduction, Structure-Activity Relationship, Swine, Xenopus laevis.

Abstract

Angiotensin II (Ang II) inhibits the cardiac sarcolemmal Na(+)-K(+) pump via protein kinase (PK)C-dependent activation of NADPH oxidase. We examined whether this is mediated by oxidative modification of the pump subunits. We detected glutathionylation of beta(1), but not alpha(1), subunits in rabbit ventricular myocytes at baseline. beta(1) Subunit glutathionylation was increased by peroxynitrite (ONOO(-)), paraquat, or activation of NADPH oxidase by Ang II. Increased glutathionylation was associated with decreased alpha(1)/beta(1) subunit coimmunoprecipitation. Glutathionylation was reversed after addition of superoxide dismutase. Glutaredoxin 1, which catalyzes deglutathionylation, coimmunoprecipitated with beta(1) subunit and, when included in patch pipette solutions, abolished paraquat-induced inhibition of myocyte Na(+)-K(+) pump current (I(p)). Cysteine (Cys46) of the beta(1) subunit was the likely candidate for glutathionylation. We expressed Na(+)-K(+) pump alpha(1) subunits with wild-type or Cys46-mutated beta(1) subunits in Xenopus oocytes. ONOO(-) induced glutathionylation of beta(1) subunit and a decrease in Na(+)-K(+) pump turnover number. This was eliminated by mutation of Cys46. ONOO(-) also induced glutathionylation of the Na(+)-K(+) ATPase beta(1) subunit from pig kidney. This was associated with a approximately 2-fold decrease in the rate-limiting E(2)-->E(1) conformational change of the pump, as determined by RH421 fluorescence. We propose that kinase-dependent regulation of the Na(+)-K(+) pump occurs via glutathionylation of its beta(1) subunit at Cys46. These findings have implications for pathophysiological conditions characterized by neurohormonal dysregulation, myocardial oxidative stress and raised myocyte Na(+) levels.

DOI: 10.1161/CIRCRESAHA.109.199547
PubMed: 19542013

Affiliations:

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Le document en format XML

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<series><title level="j">Circulation research</title>
<idno type="eISSN">1524-4571</idno>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adenosine Triphosphatases (metabolism)</term>
<term>Angiotensin II (metabolism)</term>
<term>Animals (MeSH)</term>
<term>Cation Transport Proteins (metabolism)</term>
<term>Cell Adhesion Molecules, Neuronal (metabolism)</term>
<term>Cysteine (MeSH)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Glutathione (metabolism)</term>
<term>Humans (MeSH)</term>
<term>Kidney (drug effects)</term>
<term>Kidney (enzymology)</term>
<term>Kinetics (MeSH)</term>
<term>Male (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Myocytes, Cardiac (drug effects)</term>
<term>Myocytes, Cardiac (enzymology)</term>
<term>NADPH Oxidases (metabolism)</term>
<term>Oocytes (MeSH)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Paraquat (pharmacology)</term>
<term>Peroxynitrous Acid (metabolism)</term>
<term>Protein Conformation (MeSH)</term>
<term>Protein Kinase C (metabolism)</term>
<term>Protein Processing, Post-Translational (MeSH)</term>
<term>Rabbits (MeSH)</term>
<term>Sheep (MeSH)</term>
<term>Signal Transduction (MeSH)</term>
<term>Sodium-Potassium-Exchanging ATPase (chemistry)</term>
<term>Sodium-Potassium-Exchanging ATPase (genetics)</term>
<term>Sodium-Potassium-Exchanging ATPase (metabolism)</term>
<term>Structure-Activity Relationship (MeSH)</term>
<term>Superoxide Dismutase (metabolism)</term>
<term>Swine (MeSH)</term>
<term>Xenopus laevis (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Acide peroxynitreux (métabolisme)</term>
<term>Adenosine triphosphatases (métabolisme)</term>
<term>Angiotensine-II (métabolisme)</term>
<term>Animaux (MeSH)</term>
<term>Cinétique (MeSH)</term>
<term>Conformation des protéines (MeSH)</term>
<term>Cystéine (MeSH)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Glutathion (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Lapins (MeSH)</term>
<term>Maturation post-traductionnelle des protéines (MeSH)</term>
<term>Molécules d'adhérence cellulaire neuronale (métabolisme)</term>
<term>Mutation (MeSH)</term>
<term>Myocytes cardiaques (effets des médicaments et des substances chimiques)</term>
<term>Myocytes cardiaques (enzymologie)</term>
<term>Mâle (MeSH)</term>
<term>NADPH oxidase (métabolisme)</term>
<term>Ovis (MeSH)</term>
<term>Ovocytes (MeSH)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Paraquat (pharmacologie)</term>
<term>Protéine kinase C (métabolisme)</term>
<term>Rein (effets des médicaments et des substances chimiques)</term>
<term>Rein (enzymologie)</term>
<term>Relation structure-activité (MeSH)</term>
<term>Sodium-Potassium-Exchanging ATPase (composition chimique)</term>
<term>Sodium-Potassium-Exchanging ATPase (génétique)</term>
<term>Sodium-Potassium-Exchanging ATPase (métabolisme)</term>
<term>Suidae (MeSH)</term>
<term>Superoxide dismutase (métabolisme)</term>
<term>Transduction du signal (MeSH)</term>
<term>Transporteurs de cations (métabolisme)</term>
<term>Xenopus laevis (MeSH)</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="genetics" xml:lang="en"><term>Sodium-Potassium-Exchanging ATPase</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adenosine Triphosphatases</term>
<term>Angiotensin II</term>
<term>Cation Transport Proteins</term>
<term>Cell Adhesion Molecules, Neuronal</term>
<term>Glutaredoxins</term>
<term>Glutathione</term>
<term>NADPH Oxidases</term>
<term>Peroxynitrous Acid</term>
<term>Protein Kinase C</term>
<term>Sodium-Potassium-Exchanging ATPase</term>
<term>Superoxide Dismutase</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Sodium-Potassium-Exchanging ATPase</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Kidney</term>
<term>Myocytes, Cardiac</term>
</keywords>
<keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Myocytes cardiaques</term>
<term>Rein</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Myocytes cardiaques</term>
<term>Rein</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Kidney</term>
<term>Myocytes, Cardiac</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Sodium-Potassium-Exchanging ATPase</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acide peroxynitreux</term>
<term>Adenosine triphosphatases</term>
<term>Angiotensine-II</term>
<term>Glutarédoxines</term>
<term>Glutathion</term>
<term>Molécules d'adhérence cellulaire neuronale</term>
<term>NADPH oxidase</term>
<term>Protéine kinase C</term>
<term>Sodium-Potassium-Exchanging ATPase</term>
<term>Superoxide dismutase</term>
<term>Transporteurs de cations</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Paraquat</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Paraquat</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Cysteine</term>
<term>Humans</term>
<term>Kinetics</term>
<term>Male</term>
<term>Mutation</term>
<term>Oocytes</term>
<term>Oxidation-Reduction</term>
<term>Protein Conformation</term>
<term>Protein Processing, Post-Translational</term>
<term>Rabbits</term>
<term>Sheep</term>
<term>Signal Transduction</term>
<term>Structure-Activity Relationship</term>
<term>Swine</term>
<term>Xenopus laevis</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Cinétique</term>
<term>Conformation des protéines</term>
<term>Cystéine</term>
<term>Humains</term>
<term>Lapins</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Mutation</term>
<term>Mâle</term>
<term>Ovis</term>
<term>Ovocytes</term>
<term>Oxydoréduction</term>
<term>Relation structure-activité</term>
<term>Suidae</term>
<term>Transduction du signal</term>
<term>Xenopus laevis</term>
</keywords>
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<front><div type="abstract" xml:lang="en">Angiotensin II (Ang II) inhibits the cardiac sarcolemmal Na(+)-K(+) pump via protein kinase (PK)C-dependent activation of NADPH oxidase. We examined whether this is mediated by oxidative modification of the pump subunits. We detected glutathionylation of beta(1), but not alpha(1), subunits in rabbit ventricular myocytes at baseline. beta(1) Subunit glutathionylation was increased by peroxynitrite (ONOO(-)), paraquat, or activation of NADPH oxidase by Ang II. Increased glutathionylation was associated with decreased alpha(1)/beta(1) subunit coimmunoprecipitation. Glutathionylation was reversed after addition of superoxide dismutase. Glutaredoxin 1, which catalyzes deglutathionylation, coimmunoprecipitated with beta(1) subunit and, when included in patch pipette solutions, abolished paraquat-induced inhibition of myocyte Na(+)-K(+) pump current (I(p)). Cysteine (Cys46) of the beta(1) subunit was the likely candidate for glutathionylation. We expressed Na(+)-K(+) pump alpha(1) subunits with wild-type or Cys46-mutated beta(1) subunits in Xenopus oocytes. ONOO(-) induced glutathionylation of beta(1) subunit and a decrease in Na(+)-K(+) pump turnover number. This was eliminated by mutation of Cys46. ONOO(-) also induced glutathionylation of the Na(+)-K(+) ATPase beta(1) subunit from pig kidney. This was associated with a approximately 2-fold decrease in the rate-limiting E(2)-->E(1) conformational change of the pump, as determined by RH421 fluorescence. We propose that kinase-dependent regulation of the Na(+)-K(+) pump occurs via glutathionylation of its beta(1) subunit at Cys46. These findings have implications for pathophysiological conditions characterized by neurohormonal dysregulation, myocardial oxidative stress and raised myocyte Na(+) levels.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19542013</PMID>
<DateCompleted><Year>2009</Year>
<Month>08</Month>
<Day>04</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>12</Month>
<Day>10</Day>
</DateRevised>
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<JournalIssue CitedMedium="Internet"><Volume>105</Volume>
<Issue>2</Issue>
<PubDate><Year>2009</Year>
<Month>Jul</Month>
<Day>17</Day>
</PubDate>
</JournalIssue>
<Title>Circulation research</Title>
<ISOAbbreviation>Circ Res</ISOAbbreviation>
</Journal>
<ArticleTitle>Reversible oxidative modification: a key mechanism of Na+-K+ pump regulation.</ArticleTitle>
<Pagination><MedlinePgn>185-93</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1161/CIRCRESAHA.109.199547</ELocationID>
<Abstract><AbstractText>Angiotensin II (Ang II) inhibits the cardiac sarcolemmal Na(+)-K(+) pump via protein kinase (PK)C-dependent activation of NADPH oxidase. We examined whether this is mediated by oxidative modification of the pump subunits. We detected glutathionylation of beta(1), but not alpha(1), subunits in rabbit ventricular myocytes at baseline. beta(1) Subunit glutathionylation was increased by peroxynitrite (ONOO(-)), paraquat, or activation of NADPH oxidase by Ang II. Increased glutathionylation was associated with decreased alpha(1)/beta(1) subunit coimmunoprecipitation. Glutathionylation was reversed after addition of superoxide dismutase. Glutaredoxin 1, which catalyzes deglutathionylation, coimmunoprecipitated with beta(1) subunit and, when included in patch pipette solutions, abolished paraquat-induced inhibition of myocyte Na(+)-K(+) pump current (I(p)). Cysteine (Cys46) of the beta(1) subunit was the likely candidate for glutathionylation. We expressed Na(+)-K(+) pump alpha(1) subunits with wild-type or Cys46-mutated beta(1) subunits in Xenopus oocytes. ONOO(-) induced glutathionylation of beta(1) subunit and a decrease in Na(+)-K(+) pump turnover number. This was eliminated by mutation of Cys46. ONOO(-) also induced glutathionylation of the Na(+)-K(+) ATPase beta(1) subunit from pig kidney. This was associated with a approximately 2-fold decrease in the rate-limiting E(2)-->E(1) conformational change of the pump, as determined by RH421 fluorescence. We propose that kinase-dependent regulation of the Na(+)-K(+) pump occurs via glutathionylation of its beta(1) subunit at Cys46. These findings have implications for pathophysiological conditions characterized by neurohormonal dysregulation, myocardial oxidative stress and raised myocyte Na(+) levels.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Figtree</LastName>
<ForeName>Gemma A</ForeName>
<Initials>GA</Initials>
<AffiliationInfo><Affiliation>Department of Cardiology, Royal North Shore Hospital, University of Sydney, St Leonards NSW 2065, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Liu</LastName>
<ForeName>Chia-Chi</ForeName>
<Initials>CC</Initials>
</Author>
<Author ValidYN="Y"><LastName>Bibert</LastName>
<ForeName>Stephanie</ForeName>
<Initials>S</Initials>
</Author>
<Author ValidYN="Y"><LastName>Hamilton</LastName>
<ForeName>Elisha J</ForeName>
<Initials>EJ</Initials>
</Author>
<Author ValidYN="Y"><LastName>Garcia</LastName>
<ForeName>Alvaro</ForeName>
<Initials>A</Initials>
</Author>
<Author ValidYN="Y"><LastName>White</LastName>
<ForeName>Caroline N</ForeName>
<Initials>CN</Initials>
</Author>
<Author ValidYN="Y"><LastName>Chia</LastName>
<ForeName>Karin K M</ForeName>
<Initials>KK</Initials>
</Author>
<Author ValidYN="Y"><LastName>Cornelius</LastName>
<ForeName>Flemming</ForeName>
<Initials>F</Initials>
</Author>
<Author ValidYN="Y"><LastName>Geering</LastName>
<ForeName>Kaethi</ForeName>
<Initials>K</Initials>
</Author>
<Author ValidYN="Y"><LastName>Rasmussen</LastName>
<ForeName>Helge H</ForeName>
<Initials>HH</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
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<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2009</Year>
<Month>06</Month>
<Day>18</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Circ Res</MedlineTA>
<NlmUniqueID>0047103</NlmUniqueID>
<ISSNLinking>0009-7330</ISSNLinking>
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   |texte=   Reversible oxidative modification: a key mechanism of Na+-K+ pump regulation.
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	Serveur d'exploration sur la glutarédoxine
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration sur la glutarédoxine

Reversible oxidative modification: a key mechanism of Na+-K+ pump regulation.

Reversible oxidative modification: a key mechanism of Na+-K+ pump regulation.

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