Modulation of the redox state of tubulin by the glutathione/glutaredoxin reductase system.
Identifieur interne : 000E71 ( Main/Exploration ); précédent : 000E70; suivant : 000E72Modulation of the redox state of tubulin by the glutathione/glutaredoxin reductase system.
Auteurs : Lisa M. Landino [États-Unis] ; Katherine L. Moynihan ; Jonathan V. Todd ; Kelly L. KennettSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 2004.
Descripteurs français
- KwdFr :
- Acide peroxynitreux (pharmacologie), Agents colorants (pharmacologie), Animaux (MeSH), Chromatographie en phase liquide à haute performance (MeSH), Concentration en ions d'hydrogène (MeSH), Cystine (composition chimique), Cystéine (composition chimique), Cystéine (métabolisme), Disulfures (composition chimique), Encéphale (métabolisme), Escherichia coli (enzymologie), Escherichia coli (métabolisme), Facteurs temps (MeSH), Fluorescéines (pharmacologie), Glutarédoxines (MeSH), Glutathion (composition chimique), Glutathion (métabolisme), Glutathione reductase (composition chimique), Humains (MeSH), Modèles chimiques (MeSH), Oxidoreductases (MeSH), Oxydoréduction (MeSH), Oxygène (métabolisme), Protéines (composition chimique), Relation dose-effet des médicaments (MeSH), Suidae (MeSH), Technique de Western (MeSH), Tubuline (composition chimique), Tubuline (métabolisme).
- MESH :
- composition chimique : Cystine, Cystéine, Disulfures, Glutathion, Glutathione reductase, Protéines, Tubuline.
- enzymologie : Escherichia coli.
- métabolisme : Cystéine, Encéphale, Escherichia coli, Glutathion, Oxygène, Tubuline.
- pharmacologie : Acide peroxynitreux, Agents colorants, Fluorescéines.
- Animaux, Chromatographie en phase liquide à haute performance, Concentration en ions d'hydrogène, Facteurs temps, Glutarédoxines, Humains, Modèles chimiques, Oxidoreductases, Oxydoréduction, Relation dose-effet des médicaments, Suidae, Technique de Western.
English descriptors
- KwdEn :
- Animals (MeSH), Blotting, Western (MeSH), Brain (metabolism), Chromatography, High Pressure Liquid (MeSH), Coloring Agents (pharmacology), Cysteine (chemistry), Cysteine (metabolism), Cystine (chemistry), Disulfides (chemistry), Dose-Response Relationship, Drug (MeSH), Escherichia coli (enzymology), Escherichia coli (metabolism), Fluoresceins (pharmacology), Glutaredoxins (MeSH), Glutathione (chemistry), Glutathione (metabolism), Glutathione Reductase (chemistry), Humans (MeSH), Hydrogen-Ion Concentration (MeSH), Models, Chemical (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (MeSH), Oxygen (metabolism), Peroxynitrous Acid (pharmacology), Proteins (chemistry), Swine (MeSH), Time Factors (MeSH), Tubulin (chemistry), Tubulin (metabolism).
- MESH :
- chemical , chemistry : Cysteine, Cystine, Disulfides, Glutathione, Glutathione Reductase, Proteins, Tubulin.
- chemical , metabolism : Cysteine, Glutathione, Oxygen, Tubulin.
- chemical , pharmacology : Coloring Agents, Fluoresceins, Peroxynitrous Acid.
- enzymology : Escherichia coli.
- metabolism : Brain, Escherichia coli.
- Animals, Blotting, Western, Chromatography, High Pressure Liquid, Dose-Response Relationship, Drug, Glutaredoxins, Humans, Hydrogen-Ion Concentration, Models, Chemical, Oxidation-Reduction, Oxidoreductases, Swine, Time Factors.
Abstract
Alterations in the redox status of proteins have been implicated in the pathology of several neurodegenerative diseases. We report that peroxynitrite-induced disulfides in porcine brain tubulin are repaired by the glutaredoxin reductase system composed of glutathione reductase, human or Escherichia coli glutaredoxin, reduced glutathione, and NADPH. Reduction of disulfide bonds between the alpha- and beta-tubulin subunits by the glutathione reductase system was assessed by Western blot. Tubulin cysteine oxidation and reduction was quantitated by monitoring the incorporation of 5-iodoacetamido-fluorescein, a thiol-specific labeling reagent. Tubulin disulfide bond reduction by the glutaredoxin reductase system restored tubulin polymerization activity that was lost following peroxynitrite addition. In support of redox modulations of tubulin by glutathione, thiol-disulfide exchange between tubulin and oxidized glutathione was detected and quantitated by HPLC. In addition, glutathionylation of tubulin was detected by dot blot using an anti-GSH antibody.
DOI: 10.1016/j.bbrc.2003.12.126
PubMed: 14733943
Affiliations:
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Box 8795, Williamsburg, VA 23187-8795, USA. lmland@wm.edu</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry, The College of William and Mary, P.O. Box 8795, Williamsburg, VA 23187-8795</wicri:regionArea><placeName><region type="state">Virginie</region></placeName></affiliation></author><author><name sortKey="Moynihan, Katherine L" sort="Moynihan, Katherine L" uniqKey="Moynihan K" first="Katherine L" last="Moynihan">Katherine L. Moynihan</name></author><author><name sortKey="Todd, Jonathan V" sort="Todd, Jonathan V" uniqKey="Todd J" first="Jonathan V" last="Todd">Jonathan V. Todd</name></author><author><name sortKey="Kennett, Kelly L" sort="Kennett, Kelly L" uniqKey="Kennett K" first="Kelly L" last="Kennett">Kelly L. 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(MeSH)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Models, Chemical (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Oxygen (metabolism)</term><term>Peroxynitrous Acid (pharmacology)</term><term>Proteins (chemistry)</term><term>Swine (MeSH)</term><term>Time Factors (MeSH)</term><term>Tubulin (chemistry)</term><term>Tubulin (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide peroxynitreux (pharmacologie)</term><term>Agents colorants (pharmacologie)</term><term>Animaux (MeSH)</term><term>Chromatographie en phase liquide à haute performance (MeSH)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Cystine (composition chimique)</term><term>Cystéine (composition chimique)</term><term>Cystéine (métabolisme)</term><term>Disulfures (composition chimique)</term><term>Encéphale (métabolisme)</term><term>Escherichia coli (enzymologie)</term><term>Escherichia coli (métabolisme)</term><term>Facteurs temps (MeSH)</term><term>Fluorescéines (pharmacologie)</term><term>Glutarédoxines (MeSH)</term><term>Glutathion (composition chimique)</term><term>Glutathion (métabolisme)</term><term>Glutathione reductase (composition chimique)</term><term>Humains (MeSH)</term><term>Modèles chimiques (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Oxygène (métabolisme)</term><term>Protéines (composition chimique)</term><term>Relation dose-effet des médicaments (MeSH)</term><term>Suidae (MeSH)</term><term>Technique de Western (MeSH)</term><term>Tubuline (composition chimique)</term><term>Tubuline (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine</term><term>Cystine</term><term>Disulfides</term><term>Glutathione</term><term>Glutathione Reductase</term><term>Proteins</term><term>Tubulin</term></keywords><keywords scheme="MESH" type="chemical" 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coli</term><term>Glutathion</term><term>Oxygène</term><term>Tubuline</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Acide peroxynitreux</term><term>Agents colorants</term><term>Fluorescéines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Blotting, Western</term><term>Chromatography, High Pressure Liquid</term><term>Dose-Response Relationship, Drug</term><term>Glutaredoxins</term><term>Humans</term><term>Hydrogen-Ion Concentration</term><term>Models, Chemical</term><term>Oxidation-Reduction</term><term>Oxidoreductases</term><term>Swine</term><term>Time Factors</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Chromatographie en phase liquide à haute performance</term><term>Concentration en ions d'hydrogène</term><term>Facteurs temps</term><term>Glutarédoxines</term><term>Humains</term><term>Modèles chimiques</term><term>Oxidoreductases</term><term>Oxydoréduction</term><term>Relation dose-effet des médicaments</term><term>Suidae</term><term>Technique de Western</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Alterations in the redox status of proteins have been implicated in the pathology of several neurodegenerative diseases. We report that peroxynitrite-induced disulfides in porcine brain tubulin are repaired by the glutaredoxin reductase system composed of glutathione reductase, human or Escherichia coli glutaredoxin, reduced glutathione, and NADPH. Reduction of disulfide bonds between the alpha- and beta-tubulin subunits by the glutathione reductase system was assessed by Western blot. Tubulin cysteine oxidation and reduction was quantitated by monitoring the incorporation of 5-iodoacetamido-fluorescein, a thiol-specific labeling reagent. Tubulin disulfide bond reduction by the glutaredoxin reductase system restored tubulin polymerization activity that was lost following peroxynitrite addition. In support of redox modulations of tubulin by glutathione, thiol-disulfide exchange between tubulin and oxidized glutathione was detected and quantitated by HPLC. In addition, glutathionylation of tubulin was detected by dot blot using an anti-GSH antibody.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">14733943</PMID><DateCompleted><Year>2004</Year><Month>03</Month><Day>05</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>12</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-291X</ISSN><JournalIssue CitedMedium="Print"><Volume>314</Volume><Issue>2</Issue><PubDate><Year>2004</Year><Month>Feb</Month><Day>06</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Modulation of the redox state of tubulin by the glutathione/glutaredoxin reductase system.</ArticleTitle><Pagination><MedlinePgn>555-60</MedlinePgn></Pagination><Abstract><AbstractText>Alterations in the redox status of proteins have been implicated in the pathology of several neurodegenerative diseases. We report that peroxynitrite-induced disulfides in porcine brain tubulin are repaired by the glutaredoxin reductase system composed of glutathione reductase, human or Escherichia coli glutaredoxin, reduced glutathione, and NADPH. Reduction of disulfide bonds between the alpha- and beta-tubulin subunits by the glutathione reductase system was assessed by Western blot. Tubulin cysteine oxidation and reduction was quantitated by monitoring the incorporation of 5-iodoacetamido-fluorescein, a thiol-specific labeling reagent. Tubulin disulfide bond reduction by the glutaredoxin reductase system restored tubulin polymerization activity that was lost following peroxynitrite addition. In support of redox modulations of tubulin by glutathione, thiol-disulfide exchange between tubulin and oxidized glutathione was detected and quantitated by HPLC. In addition, glutathionylation of tubulin was detected by dot blot using an anti-GSH antibody.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Landino</LastName><ForeName>Lisa M</ForeName><Initials>LM</Initials><AffiliationInfo><Affiliation>Department of Chemistry, The College of William and Mary, P.O. Box 8795, Williamsburg, VA 23187-8795, USA. lmland@wm.edu</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Moynihan</LastName><ForeName>Katherine L</ForeName><Initials>KL</Initials></Author><Author ValidYN="Y"><LastName>Todd</LastName><ForeName>Jonathan V</ForeName><Initials>JV</Initials></Author><Author ValidYN="Y"><LastName>Kennett</LastName><ForeName>Kelly L</ForeName><Initials>KL</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R15-NS38885</GrantID><Acronym>NS</Acronym><Agency>NINDS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochem Biophys Res 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Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>48TCX9A1VT</RegistryNumber><NameOfSubstance UI="D003553">Cystine</NameOfSubstance></Chemical><Chemical><RegistryNumber>63368-54-7</RegistryNumber><NameOfSubstance UI="C015296">5-iodoacetamidofluorescein</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.7</RegistryNumber><NameOfSubstance UI="D005980">Glutathione Reductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical><Chemical><RegistryNumber>S88TT14065</RegistryNumber><NameOfSubstance UI="D010100">Oxygen</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015153" MajorTopicYN="N">Blotting, Western</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001921" MajorTopicYN="N">Brain</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002851" MajorTopicYN="N">Chromatography, High Pressure Liquid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004396" MajorTopicYN="N">Coloring Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003553" MajorTopicYN="N">Cystine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004305" MajorTopicYN="N">Dose-Response Relationship, Drug</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005452" MajorTopicYN="N">Fluoresceins</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" 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MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010100" MajorTopicYN="N">Oxygen</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D030421" MajorTopicYN="N">Peroxynitrous Acid</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013552" MajorTopicYN="N">Swine</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013997" MajorTopicYN="N">Time Factors</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014404" MajorTopicYN="N">Tubulin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2004</Year><Month>1</Month><Day>22</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2004</Year><Month>3</Month><Day>6</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2004</Year><Month>1</Month><Day>22</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">14733943</ArticleId><ArticleId IdType="pii">S0006291X03027529</ArticleId><ArticleId IdType="doi">10.1016/j.bbrc.2003.12.126</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Virginie</li></region></list><tree><noCountry><name sortKey="Kennett, Kelly L" sort="Kennett, Kelly L" uniqKey="Kennett K" first="Kelly L" last="Kennett">Kelly L. Kennett</name><name sortKey="Moynihan, Katherine L" sort="Moynihan, Katherine L" uniqKey="Moynihan K" first="Katherine L" last="Moynihan">Katherine L. Moynihan</name><name sortKey="Todd, Jonathan V" sort="Todd, Jonathan V" uniqKey="Todd J" first="Jonathan V" last="Todd">Jonathan V. Todd</name></noCountry><country name="États-Unis"><region name="Virginie"><name sortKey="Landino, Lisa M" sort="Landino, Lisa M" uniqKey="Landino L" first="Lisa M" last="Landino">Lisa M. Landino</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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