Determination of glutaredoxin enzyme activity and protein S-glutathionylation using fluorescent eosin-glutathione.
Identifieur interne : 000466 ( Main/Exploration ); précédent : 000465; suivant : 000467Determination of glutaredoxin enzyme activity and protein S-glutathionylation using fluorescent eosin-glutathione.
Auteurs : Lucia Coppo [Suède] ; Sergio J. Montano [Suède] ; Alicia C. Padilla [Espagne] ; Arne Holmgren [Suède]Source :
- Analytical biochemistry [ 1096-0309 ] ; 2016.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Bovins (MeSH), Colorants fluorescents (composition chimique), Colorants fluorescents (métabolisme), Disulfures (composition chimique), Disulfures (métabolisme), Fluorescence (MeSH), Glutarédoxines (composition chimique), Glutarédoxines (métabolisme), Glutarédoxines (sang), Glutathion (composition chimique), Glutathion (métabolisme), Humains (MeSH), Protéine S (composition chimique), Protéine S (métabolisme), Spectrométrie de fluorescence (MeSH), Structure moléculaire (MeSH), Sérumalbumine bovine (composition chimique), Sérumalbumine bovine (métabolisme), Éosine jaunâtre (composition chimique).
- MESH :
- composition chimique : Colorants fluorescents, Disulfures, Glutarédoxines, Glutathion, Protéine S, Sérumalbumine bovine, Éosine jaunâtre.
- métabolisme : Colorants fluorescents, Disulfures, Glutarédoxines, Glutathion, Protéine S, Sérumalbumine bovine.
- sang : Glutarédoxines.
- Animaux, Bovins, Fluorescence, Humains, Spectrométrie de fluorescence, Structure moléculaire.
English descriptors
- KwdEn :
- Animals (MeSH), Cattle (MeSH), Disulfides (chemistry), Disulfides (metabolism), Eosine Yellowish-(YS) (chemistry), Fluorescence (MeSH), Fluorescent Dyes (chemistry), Fluorescent Dyes (metabolism), Glutaredoxins (blood), Glutaredoxins (chemistry), Glutaredoxins (metabolism), Glutathione (chemistry), Glutathione (metabolism), Humans (MeSH), Molecular Structure (MeSH), Protein S (chemistry), Protein S (metabolism), Serum Albumin, Bovine (chemistry), Serum Albumin, Bovine (metabolism), Spectrometry, Fluorescence (MeSH).
- MESH :
- chemical , blood : Glutaredoxins.
- chemical , chemistry : Disulfides, Eosine Yellowish-(YS), Fluorescent Dyes, Glutaredoxins, Glutathione, Protein S, Serum Albumin, Bovine.
- chemical , metabolism : Disulfides, Fluorescent Dyes, Glutaredoxins, Glutathione, Protein S, Serum Albumin, Bovine.
- Animals, Cattle, Fluorescence, Humans, Molecular Structure, Spectrometry, Fluorescence.
Abstract
Glutaredoxins catalyze glutathione-dependent disulfide oxidoreductions, particularly reduction of glutathione (GSH)-protein mixed disulfides. Mammalian glutaredoxins are present in the cytosol/nucleus as Grx1 or in mitochondria as Grx2a. Here we describe di-eosin-glutathione disulfide (Di-E-GSSG) as a new tool to study glutaredoxin (Grx) activity. Di-E-GSSG has almost no fluorescence in its disulfide form due to self-quenching, whereas the reduced form (E-GSH) has a large fluorescence emission at 545 nm after excitation at 520 nm. Di-E-GSSG was a very poor substrate for glutathione reductase, but we discovered that the molecule was an excellent substrate for glutaredoxin in a coupled assay system with GSH, nicotinamide adenine dinucleotide phosphate (NADPH), and glutathione reductase or with lipoamide, NADH, and lipoamide dehydrogenase. In addition, Di-E-GSSG was used to glutathionylate the free SH group of bovine serum albumin (BSA), yielding eosin-glutathionylated BSA (E-GS-BSA) readily observed in ultraviolet (UV) light. E-GS-BSA also displayed a quenched fluorescence, and its Grx-catalyzed reduction could be followed by the formation of E-GSH by fluorescence emission using microtiter plates. This way of measuring Grx activity provided an ultrasensitive method that detected Grx1 and Grx2 at picomolar levels. Human Grx1 was readily quantified in 40 μl of plasma and determined to be 680 ± 208 pM in healthy controls.
DOI: 10.1016/j.ab.2016.01.012
PubMed: 26836485
Affiliations:
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Montano</name><affiliation wicri:level="3"><nlm:affiliation>Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-17177, Stockholm, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-17177, Stockholm</wicri:regionArea><placeName><settlement type="city">Stockholm</settlement><region nuts="2">Svealand</region></placeName></affiliation></author><author><name sortKey="Padilla, Alicia C" sort="Padilla, Alicia C" uniqKey="Padilla A" first="Alicia C" last="Padilla">Alicia C. 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Electronic address: arne.holmgren@ki.se.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-17177, Stockholm</wicri:regionArea><placeName><settlement type="city">Stockholm</settlement><region nuts="2">Svealand</region></placeName></affiliation></author></analytic><series><title level="j">Analytical biochemistry</title><idno type="eISSN">1096-0309</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Cattle (MeSH)</term><term>Disulfides (chemistry)</term><term>Disulfides (metabolism)</term><term>Eosine Yellowish-(YS) (chemistry)</term><term>Fluorescence (MeSH)</term><term>Fluorescent Dyes (chemistry)</term><term>Fluorescent Dyes (metabolism)</term><term>Glutaredoxins (blood)</term><term>Glutaredoxins (chemistry)</term><term>Glutaredoxins (metabolism)</term><term>Glutathione (chemistry)</term><term>Glutathione (metabolism)</term><term>Humans (MeSH)</term><term>Molecular Structure (MeSH)</term><term>Protein S (chemistry)</term><term>Protein S (metabolism)</term><term>Serum Albumin, Bovine (chemistry)</term><term>Serum Albumin, Bovine (metabolism)</term><term>Spectrometry, Fluorescence (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Bovins (MeSH)</term><term>Colorants fluorescents (composition chimique)</term><term>Colorants fluorescents (métabolisme)</term><term>Disulfures (composition chimique)</term><term>Disulfures (métabolisme)</term><term>Fluorescence (MeSH)</term><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (métabolisme)</term><term>Glutarédoxines (sang)</term><term>Glutathion (composition chimique)</term><term>Glutathion (métabolisme)</term><term>Humains (MeSH)</term><term>Protéine S (composition chimique)</term><term>Protéine S (métabolisme)</term><term>Spectrométrie de fluorescence (MeSH)</term><term>Structure moléculaire (MeSH)</term><term>Sérumalbumine bovine (composition chimique)</term><term>Sérumalbumine bovine (métabolisme)</term><term>Éosine jaunâtre (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="blood" xml:lang="en"><term>Glutaredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Disulfides</term><term>Eosine Yellowish-(YS)</term><term>Fluorescent Dyes</term><term>Glutaredoxins</term><term>Glutathione</term><term>Protein S</term><term>Serum Albumin, Bovine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Disulfides</term><term>Fluorescent Dyes</term><term>Glutaredoxins</term><term>Glutathione</term><term>Protein S</term><term>Serum Albumin, Bovine</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Colorants fluorescents</term><term>Disulfures</term><term>Glutarédoxines</term><term>Glutathion</term><term>Protéine S</term><term>Sérumalbumine bovine</term><term>Éosine jaunâtre</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Colorants fluorescents</term><term>Disulfures</term><term>Glutarédoxines</term><term>Glutathion</term><term>Protéine S</term><term>Sérumalbumine bovine</term></keywords><keywords scheme="MESH" qualifier="sang" xml:lang="fr"><term>Glutarédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cattle</term><term>Fluorescence</term><term>Humans</term><term>Molecular Structure</term><term>Spectrometry, Fluorescence</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Bovins</term><term>Fluorescence</term><term>Humains</term><term>Spectrométrie de fluorescence</term><term>Structure moléculaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxins catalyze glutathione-dependent disulfide oxidoreductions, particularly reduction of glutathione (GSH)-protein mixed disulfides. Mammalian glutaredoxins are present in the cytosol/nucleus as Grx1 or in mitochondria as Grx2a. Here we describe di-eosin-glutathione disulfide (Di-E-GSSG) as a new tool to study glutaredoxin (Grx) activity. Di-E-GSSG has almost no fluorescence in its disulfide form due to self-quenching, whereas the reduced form (E-GSH) has a large fluorescence emission at 545 nm after excitation at 520 nm. Di-E-GSSG was a very poor substrate for glutathione reductase, but we discovered that the molecule was an excellent substrate for glutaredoxin in a coupled assay system with GSH, nicotinamide adenine dinucleotide phosphate (NADPH), and glutathione reductase or with lipoamide, NADH, and lipoamide dehydrogenase. In addition, Di-E-GSSG was used to glutathionylate the free SH group of bovine serum albumin (BSA), yielding eosin-glutathionylated BSA (E-GS-BSA) readily observed in ultraviolet (UV) light. E-GS-BSA also displayed a quenched fluorescence, and its Grx-catalyzed reduction could be followed by the formation of E-GSH by fluorescence emission using microtiter plates. This way of measuring Grx activity provided an ultrasensitive method that detected Grx1 and Grx2 at picomolar levels. Human Grx1 was readily quantified in 40 μl of plasma and determined to be 680 ± 208 pM in healthy controls.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26836485</PMID><DateCompleted><Year>2016</Year><Month>11</Month><Day>14</Day></DateCompleted><DateRevised><Year>2017</Year><Month>11</Month><Day>16</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1096-0309</ISSN><JournalIssue CitedMedium="Internet"><Volume>499</Volume><PubDate><Year>2016</Year><Month>Apr</Month><Day>15</Day></PubDate></JournalIssue><Title>Analytical biochemistry</Title><ISOAbbreviation>Anal Biochem</ISOAbbreviation></Journal><ArticleTitle>Determination of glutaredoxin enzyme activity and protein S-glutathionylation using fluorescent eosin-glutathione.</ArticleTitle><Pagination><MedlinePgn>24-33</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0003-2697(16)00027-0</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.ab.2016.01.012</ELocationID><Abstract><AbstractText>Glutaredoxins catalyze glutathione-dependent disulfide oxidoreductions, particularly reduction of glutathione (GSH)-protein mixed disulfides. Mammalian glutaredoxins are present in the cytosol/nucleus as Grx1 or in mitochondria as Grx2a. Here we describe di-eosin-glutathione disulfide (Di-E-GSSG) as a new tool to study glutaredoxin (Grx) activity. Di-E-GSSG has almost no fluorescence in its disulfide form due to self-quenching, whereas the reduced form (E-GSH) has a large fluorescence emission at 545 nm after excitation at 520 nm. Di-E-GSSG was a very poor substrate for glutathione reductase, but we discovered that the molecule was an excellent substrate for glutaredoxin in a coupled assay system with GSH, nicotinamide adenine dinucleotide phosphate (NADPH), and glutathione reductase or with lipoamide, NADH, and lipoamide dehydrogenase. In addition, Di-E-GSSG was used to glutathionylate the free SH group of bovine serum albumin (BSA), yielding eosin-glutathionylated BSA (E-GS-BSA) readily observed in ultraviolet (UV) light. E-GS-BSA also displayed a quenched fluorescence, and its Grx-catalyzed reduction could be followed by the formation of E-GSH by fluorescence emission using microtiter plates. This way of measuring Grx activity provided an ultrasensitive method that detected Grx1 and Grx2 at picomolar levels. Human Grx1 was readily quantified in 40 μl of plasma and determined to be 680 ± 208 pM in healthy controls.</AbstractText><CopyrightInformation>Copyright © 2016 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Coppo</LastName><ForeName>Lucia</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-17177, Stockholm, Sweden. Electronic address: lucia.coppo@ki.se.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Montano</LastName><ForeName>Sergio J</ForeName><Initials>SJ</Initials><AffiliationInfo><Affiliation>Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-17177, Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Padilla</LastName><ForeName>Alicia C</ForeName><Initials>AC</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Campus de Rabanales, University of Córdoba, 14071, Córdoba, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Holmgren</LastName><ForeName>Arne</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-17177, Stockholm, Sweden. Electronic address: arne.holmgren@ki.se.</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></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>01</Month><Day>31</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Anal Biochem</MedlineTA><NlmUniqueID>0370535</NlmUniqueID><ISSNLinking>0003-2697</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005456">Fluorescent Dyes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C516005">GLRX protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017293">Protein S</NameOfSubstance></Chemical><Chemical><RegistryNumber>27432CM55Q</RegistryNumber><NameOfSubstance UI="D012710">Serum Albumin, Bovine</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>TDQ283MPCW</RegistryNumber><NameOfSubstance UI="D004801">Eosine Yellowish-(YS)</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002417" MajorTopicYN="N">Cattle</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004801" MajorTopicYN="N">Eosine Yellowish-(YS)</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005453" MajorTopicYN="Y">Fluorescence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005456" MajorTopicYN="N">Fluorescent Dyes</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000097" MajorTopicYN="N">blood</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015394" MajorTopicYN="N">Molecular Structure</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017293" MajorTopicYN="N">Protein S</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012710" MajorTopicYN="N">Serum Albumin, Bovine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013050" MajorTopicYN="N">Spectrometry, Fluorescence</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Deglutathionylation</Keyword><Keyword MajorTopicYN="N">Di-eosin-glutathione</Keyword><Keyword MajorTopicYN="N">Fluorescence assay</Keyword><Keyword MajorTopicYN="N">Glutaredoxin activity</Keyword><Keyword MajorTopicYN="N">Redox</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>10</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2016</Year><Month>01</Month><Day>21</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>01</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>2</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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sort="Montano, Sergio J" uniqKey="Montano S" first="Sergio J" last="Montano">Sergio J. Montano</name></country><country name="Espagne"><noRegion><name sortKey="Padilla, Alicia C" sort="Padilla, Alicia C" uniqKey="Padilla A" first="Alicia C" last="Padilla">Alicia C. Padilla</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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