GlutaredoxinV1, Main, Exploration, bibRecord, 000371

Effect of Reduction of Redox Modifications of Cys-Residues in the Na,K-ATPase α1-Subunit on Its Activity.

Identifieur interne : 000371 ( Main/Exploration ); précédent : 000370; suivant : 000372

Effect of Reduction of Redox Modifications of Cys-Residues in the Na,K-ATPase α1-Subunit on Its Activity.

Auteurs : Elena A. Dergousova [Russie] ; Irina Yu Petrushanko [Russie] ; Elizaveta A. Klimanova [Russie] ; Vladimir A. Mitkevich [Russie] ; Rustam H. Ziganshin [Russie] ; Olga D. Lopina [Russie] ; Alexander A. Makarov [Russie]

Source :

Biomolecules [ 2218-273X ] ; 2017.

RBID : pubmed:28230807

Descripteurs français

KwdFr :
- Animaux (MeSH), Canards (MeSH), Cystéine (métabolisme), Dénaturation des protéines (MeSH), Glutathion (métabolisme), Oxydoréduction (MeSH), Peptides (métabolisme), Sodium-Potassium-Exchanging ATPase (métabolisme), Sous-unités de protéines (métabolisme).
MESH :
- métabolisme : Cystéine, Glutathion, Peptides, Sodium-Potassium-Exchanging ATPase, Sous-unités de protéines.
- Animaux, Canards, Dénaturation des protéines, Oxydoréduction.

English descriptors

KwdEn :
- Animals (MeSH), Cysteine (metabolism), Ducks (MeSH), Glutathione (metabolism), Oxidation-Reduction (MeSH), Peptides (metabolism), Protein Denaturation (MeSH), Protein Subunits (metabolism), Sodium-Potassium-Exchanging ATPase (metabolism).
MESH :
- chemical , metabolism : Cysteine, Glutathione, Peptides, Protein Subunits, Sodium-Potassium-Exchanging ATPase.
- Animals, Ducks, Oxidation-Reduction, Protein Denaturation.

Abstract

Sodium-potassium adenosine triphosphatase (Na,K-ATPase) creates a gradient of sodium and potassium ions necessary for the viability of animal cells, and it is extremely sensitive to intracellular redox status. Earlier we found that regulatory glutathionylation determines Na,K-ATPase redox sensitivity but the role of basal glutathionylation and other redox modifications of cysteine residues is not clear. The purpose of this study was to detect oxidized, nitrosylated, or glutathionylated cysteine residues in Na,K-ATPase, evaluate the possibility of removing these modifications and assess their influence on the enzyme activity. To this aim, we have detected such modifications in the Na,K-ATPase α1-subunit purified from duck salt glands and tried to eliminate them by chemical reducing agents and the glutaredoxin1/glutathione reductase enzyme system. Detection of cysteine modifications was performed using mass spectrometry and Western blot analysis. We have found that purified Na,K-ATPase α1-subunit contains glutathionylated, nitrosylated, and oxidized cysteines. Chemical reducing agents partially eliminate these modifications that leads to the slight increase of the enzyme activity. Enzyme system glutaredoxin/glutathione reductase, unlike chemical reducing agents, produces significant increase of the enzyme activity. At the same time, the enzyme system deglutathionylates native Na,K-ATPase to a lesser degree than chemical reducing agents. This suggests that the enzymatic reducing system glutaredoxin/glutathione reductase specifically affects glutathionylation of the regulatory cysteine residues of Na,K-ATPase α1-subunit.

DOI: 10.3390/biom7010018
PubMed: 28230807
PubMed Central: PMC5372730

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<series><title level="j">Biomolecules</title>
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<term>Cysteine (metabolism)</term>
<term>Ducks (MeSH)</term>
<term>Glutathione (metabolism)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Peptides (metabolism)</term>
<term>Protein Denaturation (MeSH)</term>
<term>Protein Subunits (metabolism)</term>
<term>Sodium-Potassium-Exchanging ATPase (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term>
<term>Canards (MeSH)</term>
<term>Cystéine (métabolisme)</term>
<term>Dénaturation des protéines (MeSH)</term>
<term>Glutathion (métabolisme)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Peptides (métabolisme)</term>
<term>Sodium-Potassium-Exchanging ATPase (métabolisme)</term>
<term>Sous-unités de protéines (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine</term>
<term>Glutathione</term>
<term>Peptides</term>
<term>Protein Subunits</term>
<term>Sodium-Potassium-Exchanging ATPase</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cystéine</term>
<term>Glutathion</term>
<term>Peptides</term>
<term>Sodium-Potassium-Exchanging ATPase</term>
<term>Sous-unités de protéines</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Ducks</term>
<term>Oxidation-Reduction</term>
<term>Protein Denaturation</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Canards</term>
<term>Dénaturation des protéines</term>
<term>Oxydoréduction</term>
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<front><div type="abstract" xml:lang="en">Sodium-potassium adenosine triphosphatase (Na,K-ATPase) creates a gradient of sodium and potassium ions necessary for the viability of animal cells, and it is extremely sensitive to intracellular redox status. Earlier we found that regulatory glutathionylation determines Na,K-ATPase redox sensitivity but the role of basal glutathionylation and other redox modifications of cysteine residues is not clear. The purpose of this study was to detect oxidized, nitrosylated, or glutathionylated cysteine residues in Na,K-ATPase, evaluate the possibility of removing these modifications and assess their influence on the enzyme activity. To this aim, we have detected such modifications in the Na,K-ATPase α1-subunit purified from duck salt glands and tried to eliminate them by chemical reducing agents and the glutaredoxin1/glutathione reductase enzyme system. Detection of cysteine modifications was performed using mass spectrometry and Western blot analysis. We have found that purified Na,K-ATPase α1-subunit contains glutathionylated, nitrosylated, and oxidized cysteines. Chemical reducing agents partially eliminate these modifications that leads to the slight increase of the enzyme activity. Enzyme system glutaredoxin/glutathione reductase, unlike chemical reducing agents, produces significant increase of the enzyme activity. At the same time, the enzyme system deglutathionylates native Na,K-ATPase to a lesser degree than chemical reducing agents. This suggests that the enzymatic reducing system glutaredoxin/glutathione reductase specifically affects glutathionylation of the regulatory cysteine residues of Na,K-ATPase α1-subunit.</div>
</front>
</TEI>
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<DateCompleted><Year>2017</Year>
<Month>11</Month>
<Day>21</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>12</Month>
<Day>10</Day>
</DateRevised>
<Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2218-273X</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>7</Volume>
<Issue>1</Issue>
<PubDate><Year>2017</Year>
<Month>02</Month>
<Day>21</Day>
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<Title>Biomolecules</Title>
<ISOAbbreviation>Biomolecules</ISOAbbreviation>
</Journal>
<ArticleTitle>Effect of Reduction of Redox Modifications of Cys-Residues in the Na,K-ATPase α1-Subunit on Its Activity.</ArticleTitle>
<ELocationID EIdType="pii" ValidYN="Y">E18</ELocationID>
<ELocationID EIdType="doi" ValidYN="Y">10.3390/biom7010018</ELocationID>
<Abstract><AbstractText>Sodium-potassium adenosine triphosphatase (Na,K-ATPase) creates a gradient of sodium and potassium ions necessary for the viability of animal cells, and it is extremely sensitive to intracellular redox status. Earlier we found that regulatory glutathionylation determines Na,K-ATPase redox sensitivity but the role of basal glutathionylation and other redox modifications of cysteine residues is not clear. The purpose of this study was to detect oxidized, nitrosylated, or glutathionylated cysteine residues in Na,K-ATPase, evaluate the possibility of removing these modifications and assess their influence on the enzyme activity. To this aim, we have detected such modifications in the Na,K-ATPase α1-subunit purified from duck salt glands and tried to eliminate them by chemical reducing agents and the glutaredoxin1/glutathione reductase enzyme system. Detection of cysteine modifications was performed using mass spectrometry and Western blot analysis. We have found that purified Na,K-ATPase α1-subunit contains glutathionylated, nitrosylated, and oxidized cysteines. Chemical reducing agents partially eliminate these modifications that leads to the slight increase of the enzyme activity. Enzyme system glutaredoxin/glutathione reductase, unlike chemical reducing agents, produces significant increase of the enzyme activity. At the same time, the enzyme system deglutathionylates native Na,K-ATPase to a lesser degree than chemical reducing agents. This suggests that the enzymatic reducing system glutaredoxin/glutathione reductase specifically affects glutathionylation of the regulatory cysteine residues of Na,K-ATPase α1-subunit.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Dergousova</LastName>
<ForeName>Elena A</ForeName>
<Initials>EA</Initials>
<AffiliationInfo><Affiliation>Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov St, 32, Moscow 119991, Russia. dergousova90@list.ru.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Faculty of Biology, Lomonosov Moscow State University, Leninskie Gory, 1/12, Moscow 119234, Russia. dergousova90@list.ru.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Petrushanko</LastName>
<ForeName>Irina Yu</ForeName>
<Initials>IY</Initials>
<AffiliationInfo><Affiliation>Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov St, 32, Moscow 119991, Russia. irina-pva@mail.ru.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Klimanova</LastName>
<ForeName>Elizaveta A</ForeName>
<Initials>EA</Initials>
<AffiliationInfo><Affiliation>Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov St, 32, Moscow 119991, Russia. klimanova.ea@yandex.ru.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Faculty of Biology, Lomonosov Moscow State University, Leninskie Gory, 1/12, Moscow 119234, Russia. klimanova.ea@yandex.ru.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Mitkevich</LastName>
<ForeName>Vladimir A</ForeName>
<Initials>VA</Initials>
<AffiliationInfo><Affiliation>Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov St, 32, Moscow 119991, Russia. mitkevich@gmail.com.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ziganshin</LastName>
<ForeName>Rustam H</ForeName>
<Initials>RH</Initials>
<AffiliationInfo><Affiliation>Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya str., 16/10, Moscow 117997, Russia. ziganshin@mail.ru.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lopina</LastName>
<ForeName>Olga D</ForeName>
<Initials>OD</Initials>
<AffiliationInfo><Affiliation>Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov St, 32, Moscow 119991, Russia. od_lopina@mail.ru.</Affiliation>
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Effect of Reduction of Redox Modifications of Cys-Residues in the Na,K-ATPase α1-Subunit on Its Activity.

Effect of Reduction of Redox Modifications of Cys-Residues in the Na,K-ATPase α1-Subunit on Its Activity.

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