Regulation of annexin A2 by reversible glutathionylation.
Identifieur interne : 000E54 ( Main/Exploration ); précédent : 000E53; suivant : 000E55Regulation of annexin A2 by reversible glutathionylation.
Auteurs : Jennifer F. Caplan [Canada] ; Nolan R. Filipenko ; Sandra L. Fitzpatrick ; David M. WaismanSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2004.
Descripteurs français
- KwdFr :
- Actines (métabolisme), Animaux (MeSH), Annexine A2 (composition chimique), Annexine A2 (métabolisme), Biotinylation (MeSH), Bovins (MeSH), Cystéine (composition chimique), Dithiothréitol (pharmacologie), Facteur de nécrose tumorale alpha (pharmacologie), Glutarédoxines (MeSH), Glutathion (composition chimique), Homéostasie (MeSH), Liposomes (métabolisme), Oxidoreductases (MeSH), Oxydants (composition chimique), Oxydants (pharmacologie), Oxydoréduction (MeSH), Peroxyde d'hydrogène (pharmacologie), Phospholipides (métabolisme), Protéines (métabolisme), Relation structure-activité (MeSH), Spectrométrie de masse (MeSH), Stress oxydatif (MeSH), Tétraméthyl-diazènedicarboxamide (composition chimique), Tétraméthyl-diazènedicarboxamide (pharmacologie).
- MESH :
- composition chimique : Annexine A2, Cystéine, Glutathion, Oxydants, Tétraméthyl-diazènedicarboxamide.
- métabolisme : Actines, Annexine A2, Liposomes, Phospholipides, Protéines.
- pharmacologie : Dithiothréitol, Facteur de nécrose tumorale alpha, Oxydants, Peroxyde d'hydrogène, Tétraméthyl-diazènedicarboxamide.
- Animaux, Biotinylation, Bovins, Glutarédoxines, Homéostasie, Oxidoreductases, Oxydoréduction, Relation structure-activité, Spectrométrie de masse, Stress oxydatif.
English descriptors
- KwdEn :
- Actins (metabolism), Animals (MeSH), Annexin A2 (chemistry), Annexin A2 (metabolism), Biotinylation (MeSH), Cattle (MeSH), Cysteine (chemistry), Diamide (chemistry), Diamide (pharmacology), Dithiothreitol (pharmacology), Glutaredoxins (MeSH), Glutathione (chemistry), Homeostasis (MeSH), Hydrogen Peroxide (pharmacology), Liposomes (metabolism), Mass Spectrometry (MeSH), Oxidants (chemistry), Oxidants (pharmacology), Oxidation-Reduction (MeSH), Oxidative Stress (MeSH), Oxidoreductases (MeSH), Phospholipids (metabolism), Proteins (metabolism), Structure-Activity Relationship (MeSH), Tumor Necrosis Factor-alpha (pharmacology).
- MESH :
- chemical , chemistry : Annexin A2, Cysteine, Diamide, Glutathione, Oxidants.
- chemical , metabolism : Actins, Annexin A2, Liposomes, Phospholipids, Proteins.
- chemical , pharmacology : Diamide, Dithiothreitol, Hydrogen Peroxide, Oxidants, Tumor Necrosis Factor-alpha.
- Animals, Biotinylation, Cattle, Glutaredoxins, Homeostasis, Mass Spectrometry, Oxidation-Reduction, Oxidative Stress, Oxidoreductases, Structure-Activity Relationship.
Abstract
The annexin A2-S100A10 heterotetramer (AIIt) is a multifunctional Ca(2+)-dependent, phospholipid-binding, and F-actin-binding phosphoprotein composed of two annexin A2 subunits and two S100A10 subunits. It was reported previously that oxidative stress from exogenous hydrogen peroxide or generated in response to tumor necrosis factor-alpha results in the glutathionylation of Cys(8) of annexin A2. In this study, we demonstrate that AIIt is an oxidatively labile protein whose level of activity is regulated by the redox status of its sulfhydryl groups. Oxidation of AIIt by diamide resulted in a time- and concentration-dependent loss of the ability of AIIt to interact with phospholipid liposomes and F-actin. The inhibitory effect of diamide on the activity of AIIt was partially reversed by dithiothreitol. In addition, incubation of AIIt with diamide and GSH resulted in the glutathionylation of AIIt in vitro. Mass spectrometry established the incorporation of 2 mol of GSH/mol of annexin A2 subunit at Cys(8) and Cys(132). Glutathionylation potentiated the inhibitory effects of diamide on the activity of AIIt. Furthermore, AIIt could be deglutathionylated by glutaredoxin (thiol transferase). Thus, we show for the first time that AIIt can undergo functional reactivation by glutaredoxin, therefore establishing that AIIt is regulated by reversible glutathionylation.
DOI: 10.1074/jbc.M313049200
PubMed: 14668336
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Waisman</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2004">2004</date><idno type="RBID">pubmed:14668336</idno><idno type="pmid">14668336</idno><idno type="doi">10.1074/jbc.M313049200</idno><idno type="wicri:Area/Main/Corpus">000E98</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000E98</idno><idno type="wicri:Area/Main/Curation">000E98</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000E98</idno><idno type="wicri:Area/Main/Exploration">000E98</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Regulation of annexin A2 by reversible glutathionylation.</title><author><name sortKey="Caplan, Jennifer F" sort="Caplan, Jennifer F" uniqKey="Caplan J" first="Jennifer F" last="Caplan">Jennifer F. Caplan</name><affiliation wicri:level="4"><nlm:affiliation>Cancer Biology Research Group, Department of Biochemistry, University of Calgary, Calgary, Alberta T2N 4N1, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Cancer Biology Research Group, Department of Biochemistry, University of Calgary, Calgary, Alberta T2N 4N1</wicri:regionArea><orgName type="university">Université de Calgary</orgName><placeName><settlement type="city">Calgary</settlement><region type="state">Alberta</region></placeName></affiliation></author><author><name sortKey="Filipenko, Nolan R" sort="Filipenko, Nolan R" uniqKey="Filipenko N" first="Nolan R" last="Filipenko">Nolan R. Filipenko</name></author><author><name sortKey="Fitzpatrick, Sandra L" sort="Fitzpatrick, Sandra L" uniqKey="Fitzpatrick S" first="Sandra L" last="Fitzpatrick">Sandra L. Fitzpatrick</name></author><author><name sortKey="Waisman, David M" sort="Waisman, David M" uniqKey="Waisman D" first="David M" last="Waisman">David M. Waisman</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Actins (metabolism)</term><term>Animals (MeSH)</term><term>Annexin A2 (chemistry)</term><term>Annexin A2 (metabolism)</term><term>Biotinylation (MeSH)</term><term>Cattle (MeSH)</term><term>Cysteine (chemistry)</term><term>Diamide (chemistry)</term><term>Diamide (pharmacology)</term><term>Dithiothreitol (pharmacology)</term><term>Glutaredoxins (MeSH)</term><term>Glutathione (chemistry)</term><term>Homeostasis (MeSH)</term><term>Hydrogen Peroxide (pharmacology)</term><term>Liposomes (metabolism)</term><term>Mass Spectrometry (MeSH)</term><term>Oxidants (chemistry)</term><term>Oxidants (pharmacology)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidative Stress (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Phospholipids (metabolism)</term><term>Proteins (metabolism)</term><term>Structure-Activity Relationship (MeSH)</term><term>Tumor Necrosis Factor-alpha (pharmacology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Actines (métabolisme)</term><term>Animaux (MeSH)</term><term>Annexine A2 (composition chimique)</term><term>Annexine A2 (métabolisme)</term><term>Biotinylation (MeSH)</term><term>Bovins (MeSH)</term><term>Cystéine (composition chimique)</term><term>Dithiothréitol (pharmacologie)</term><term>Facteur de nécrose tumorale alpha (pharmacologie)</term><term>Glutarédoxines (MeSH)</term><term>Glutathion (composition chimique)</term><term>Homéostasie (MeSH)</term><term>Liposomes (métabolisme)</term><term>Oxidoreductases (MeSH)</term><term>Oxydants (composition chimique)</term><term>Oxydants (pharmacologie)</term><term>Oxydoréduction (MeSH)</term><term>Peroxyde d'hydrogène (pharmacologie)</term><term>Phospholipides (métabolisme)</term><term>Protéines (métabolisme)</term><term>Relation structure-activité (MeSH)</term><term>Spectrométrie de masse (MeSH)</term><term>Stress oxydatif (MeSH)</term><term>Tétraméthyl-diazènedicarboxamide (composition chimique)</term><term>Tétraméthyl-diazènedicarboxamide (pharmacologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Annexin A2</term><term>Cysteine</term><term>Diamide</term><term>Glutathione</term><term>Oxidants</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Actins</term><term>Annexin A2</term><term>Liposomes</term><term>Phospholipids</term><term>Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Diamide</term><term>Dithiothreitol</term><term>Hydrogen Peroxide</term><term>Oxidants</term><term>Tumor Necrosis Factor-alpha</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Annexine A2</term><term>Cystéine</term><term>Glutathion</term><term>Oxydants</term><term>Tétraméthyl-diazènedicarboxamide</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Actines</term><term>Annexine A2</term><term>Liposomes</term><term>Phospholipides</term><term>Protéines</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Dithiothréitol</term><term>Facteur de nécrose tumorale alpha</term><term>Oxydants</term><term>Peroxyde d'hydrogène</term><term>Tétraméthyl-diazènedicarboxamide</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Biotinylation</term><term>Cattle</term><term>Glutaredoxins</term><term>Homeostasis</term><term>Mass Spectrometry</term><term>Oxidation-Reduction</term><term>Oxidative Stress</term><term>Oxidoreductases</term><term>Structure-Activity Relationship</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Biotinylation</term><term>Bovins</term><term>Glutarédoxines</term><term>Homéostasie</term><term>Oxidoreductases</term><term>Oxydoréduction</term><term>Relation structure-activité</term><term>Spectrométrie de masse</term><term>Stress oxydatif</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The annexin A2-S100A10 heterotetramer (AIIt) is a multifunctional Ca(2+)-dependent, phospholipid-binding, and F-actin-binding phosphoprotein composed of two annexin A2 subunits and two S100A10 subunits. It was reported previously that oxidative stress from exogenous hydrogen peroxide or generated in response to tumor necrosis factor-alpha results in the glutathionylation of Cys(8) of annexin A2. In this study, we demonstrate that AIIt is an oxidatively labile protein whose level of activity is regulated by the redox status of its sulfhydryl groups. Oxidation of AIIt by diamide resulted in a time- and concentration-dependent loss of the ability of AIIt to interact with phospholipid liposomes and F-actin. The inhibitory effect of diamide on the activity of AIIt was partially reversed by dithiothreitol. In addition, incubation of AIIt with diamide and GSH resulted in the glutathionylation of AIIt in vitro. Mass spectrometry established the incorporation of 2 mol of GSH/mol of annexin A2 subunit at Cys(8) and Cys(132). Glutathionylation potentiated the inhibitory effects of diamide on the activity of AIIt. Furthermore, AIIt could be deglutathionylated by glutaredoxin (thiol transferase). Thus, we show for the first time that AIIt can undergo functional reactivation by glutaredoxin, therefore establishing that AIIt is regulated by reversible glutathionylation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">14668336</PMID><DateCompleted><Year>2004</Year><Month>05</Month><Day>03</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>279</Volume><Issue>9</Issue><PubDate><Year>2004</Year><Month>Feb</Month><Day>27</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Regulation of annexin A2 by reversible glutathionylation.</ArticleTitle><Pagination><MedlinePgn>7740-50</MedlinePgn></Pagination><Abstract><AbstractText>The annexin A2-S100A10 heterotetramer (AIIt) is a multifunctional Ca(2+)-dependent, phospholipid-binding, and F-actin-binding phosphoprotein composed of two annexin A2 subunits and two S100A10 subunits. It was reported previously that oxidative stress from exogenous hydrogen peroxide or generated in response to tumor necrosis factor-alpha results in the glutathionylation of Cys(8) of annexin A2. In this study, we demonstrate that AIIt is an oxidatively labile protein whose level of activity is regulated by the redox status of its sulfhydryl groups. Oxidation of AIIt by diamide resulted in a time- and concentration-dependent loss of the ability of AIIt to interact with phospholipid liposomes and F-actin. The inhibitory effect of diamide on the activity of AIIt was partially reversed by dithiothreitol. In addition, incubation of AIIt with diamide and GSH resulted in the glutathionylation of AIIt in vitro. Mass spectrometry established the incorporation of 2 mol of GSH/mol of annexin A2 subunit at Cys(8) and Cys(132). Glutathionylation potentiated the inhibitory effects of diamide on the activity of AIIt. Furthermore, AIIt could be deglutathionylated by glutaredoxin (thiol transferase). Thus, we show for the first time that AIIt can undergo functional reactivation by glutaredoxin, therefore establishing that AIIt is regulated by reversible glutathionylation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Caplan</LastName><ForeName>Jennifer F</ForeName><Initials>JF</Initials><AffiliationInfo><Affiliation>Cancer Biology Research Group, Department of Biochemistry, University of Calgary, Calgary, Alberta T2N 4N1, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Filipenko</LastName><ForeName>Nolan R</ForeName><Initials>NR</Initials></Author><Author ValidYN="Y"><LastName>Fitzpatrick</LastName><ForeName>Sandra L</ForeName><Initials>SL</Initials></Author><Author ValidYN="Y"><LastName>Waisman</LastName><ForeName>David M</ForeName><Initials>DM</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2003</Year><Month>12</Month><Day>10</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000199">Actins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017306">Annexin A2</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008081">Liposomes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016877">Oxidants</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010743">Phospholipids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014409">Tumor Necrosis Factor-alpha</NameOfSubstance></Chemical><Chemical><RegistryNumber>10465-78-8</RegistryNumber><NameOfSubstance UI="D003958">Diamide</NameOfSubstance></Chemical><Chemical><RegistryNumber>BBX060AN9V</RegistryNumber><NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical><Chemical><RegistryNumber>T8ID5YZU6Y</RegistryNumber><NameOfSubstance UI="D004229">Dithiothreitol</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000199" MajorTopicYN="N">Actins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017306" MajorTopicYN="N">Annexin A2</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019921" MajorTopicYN="N">Biotinylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002417" MajorTopicYN="N">Cattle</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003958" MajorTopicYN="N">Diamide</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004229" MajorTopicYN="N">Dithiothreitol</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006706" MajorTopicYN="N">Homeostasis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008081" MajorTopicYN="N">Liposomes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013058" MajorTopicYN="N">Mass Spectrometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016877" MajorTopicYN="N">Oxidants</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</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="D010088" MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010743" 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PubStatus="entrez"><Year>2003</Year><Month>12</Month><Day>12</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">14668336</ArticleId><ArticleId IdType="doi">10.1074/jbc.M313049200</ArticleId><ArticleId IdType="pii">M313049200</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Canada</li></country><region><li>Alberta</li></region><settlement><li>Calgary</li></settlement><orgName><li>Université de Calgary</li></orgName></list><tree><noCountry><name sortKey="Filipenko, Nolan R" sort="Filipenko, Nolan R" uniqKey="Filipenko N" first="Nolan R" last="Filipenko">Nolan R. Filipenko</name><name sortKey="Fitzpatrick, Sandra L" sort="Fitzpatrick, Sandra L" uniqKey="Fitzpatrick S" first="Sandra L" last="Fitzpatrick">Sandra L. Fitzpatrick</name><name sortKey="Waisman, David M" sort="Waisman, David M" uniqKey="Waisman D" first="David M" last="Waisman">David M. Waisman</name></noCountry><country name="Canada"><region name="Alberta"><name sortKey="Caplan, Jennifer F" sort="Caplan, Jennifer F" uniqKey="Caplan J" first="Jennifer F" last="Caplan">Jennifer F. Caplan</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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