Redox modulation of tau and microtubule-associated protein-2 by the glutathione/glutaredoxin reductase system.
Identifieur interne : 000E57 ( Main/Exploration ); précédent : 000E56; suivant : 000E58Redox modulation of tau and microtubule-associated protein-2 by the glutathione/glutaredoxin reductase system.
Auteurs : Lisa M. Landino [États-Unis] ; Sarah H. Robinson ; Tabor E. Skreslet ; Diana M. CabralSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 2004.
Descripteurs français
- KwdFr :
- Acide peroxynitreux (pharmacologie), Animaux (MeSH), Chromatographie en phase liquide à haute performance (MeSH), Cystéine (composition chimique), Disulfures (composition chimique), Encéphale (métabolisme), Escherichia coli (métabolisme), Facteurs temps (MeSH), Fluorescéines (pharmacologie), Glutarédoxines (MeSH), Glutathion (composition chimique), Glutathion (métabolisme), Glutathione reductase (composition chimique), Humains (MeSH), Microtubules (métabolisme), Modèles chimiques (MeSH), NADP (MeSH), Oxidoreductases (composition chimique), Oxydants (composition chimique), Oxydoréduction (MeSH), Oxygène (composition chimique), Oxygène (métabolisme), Peroxyde d'hydrogène (composition chimique), Protéines associées aux microtubules (composition chimique), Protéines tau (composition chimique), Relation dose-effet des médicaments (MeSH), Suidae (MeSH), Thiols (MeSH).
- MESH :
- composition chimique : Cystéine, Disulfures, Glutathion, Glutathione reductase, Oxidoreductases, Oxydants, Oxygène, Peroxyde d'hydrogène, Protéines associées aux microtubules, Protéines tau.
- métabolisme : Encéphale, Escherichia coli, Glutathion, Microtubules, Oxygène.
- pharmacologie : Acide peroxynitreux, Fluorescéines.
- Animaux, Chromatographie en phase liquide à haute performance, Facteurs temps, Glutarédoxines, Humains, Modèles chimiques, NADP, Oxydoréduction, Relation dose-effet des médicaments, Suidae, Thiols.
English descriptors
- KwdEn :
- Animals (MeSH), Brain (metabolism), Chromatography, High Pressure Liquid (MeSH), Cysteine (chemistry), Disulfides (chemistry), Dose-Response Relationship, Drug (MeSH), Escherichia coli (metabolism), Fluoresceins (pharmacology), Glutaredoxins (MeSH), Glutathione (chemistry), Glutathione (metabolism), Glutathione Reductase (chemistry), Humans (MeSH), Hydrogen Peroxide (chemistry), Microtubule-Associated Proteins (chemistry), Microtubules (metabolism), Models, Chemical (MeSH), NADP (MeSH), Oxidants (chemistry), Oxidation-Reduction (MeSH), Oxidoreductases (chemistry), Oxygen (chemistry), Oxygen (metabolism), Peroxynitrous Acid (pharmacology), Sulfhydryl Compounds (MeSH), Swine (MeSH), Time Factors (MeSH), tau Proteins (chemistry).
- MESH :
- chemical , chemistry : Cysteine, Disulfides, Glutathione, Glutathione Reductase, Hydrogen Peroxide, Microtubule-Associated Proteins, Oxidants, Oxidoreductases, Oxygen, tau Proteins.
- metabolism : Brain, Escherichia coli, Glutathione, Microtubules, Oxygen.
- chemical , pharmacology : Fluoresceins, Peroxynitrous Acid.
- Animals, Chromatography, High Pressure Liquid, Dose-Response Relationship, Drug, Glutaredoxins, Humans, Models, Chemical, NADP, Oxidation-Reduction, Sulfhydryl Compounds, Swine, Time Factors.
Abstract
Alterations in the redox status of proteins have been implicated in the pathology of several neurodegenerative diseases including Alzheimer's and Parkinson's. We report that peroxynitrite and H2O2-induced disulfides in the porcine brain microtubule-associated proteins tau and microtubule-associated protein-2 are substrates for the glutaredoxin reductase system composed of glutathione reductase, human or Escherichia coli glutaredoxin, reduced glutathione, and NADPH. Oxidation and reduction of cysteines in tau and microtubule-associated protein-2 were quantitated by monitoring the incorporation of 5-iodoacetamido-fluorescein, a thiol-specific labeling reagent. Reduction of disulfide bonds in the microtubule-associated proteins by the glutaredoxin reductase system restored their ability to promote the assembly of microtubules composed of purified porcine tubulin. Thiol-disulfide exchange between oxidized glutathione and the microtubule-associated proteins was detected by monitoring protein oxidation and was quantitated by measuring reduced glutathione by HPLC.
DOI: 10.1016/j.bbrc.2004.08.065
PubMed: 15351709
Affiliations:
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Robinson</name></author><author><name sortKey="Skreslet, Tabor E" sort="Skreslet, Tabor E" uniqKey="Skreslet T" first="Tabor E" last="Skreslet">Tabor E. Skreslet</name></author><author><name sortKey="Cabral, Diana M" sort="Cabral, Diana M" uniqKey="Cabral D" first="Diana M" last="Cabral">Diana M. 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We report that peroxynitrite and H2O2-induced disulfides in the porcine brain microtubule-associated proteins tau and microtubule-associated protein-2 are substrates for the glutaredoxin reductase system composed of glutathione reductase, human or Escherichia coli glutaredoxin, reduced glutathione, and NADPH. Oxidation and reduction of cysteines in tau and microtubule-associated protein-2 were quantitated by monitoring the incorporation of 5-iodoacetamido-fluorescein, a thiol-specific labeling reagent. Reduction of disulfide bonds in the microtubule-associated proteins by the glutaredoxin reductase system restored their ability to promote the assembly of microtubules composed of purified porcine tubulin. Thiol-disulfide exchange between oxidized glutathione and the microtubule-associated proteins was detected by monitoring protein oxidation and was quantitated by measuring reduced glutathione by HPLC.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15351709</PMID><DateCompleted><Year>2004</Year><Month>11</Month><Day>23</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-291X</ISSN><JournalIssue CitedMedium="Print"><Volume>323</Volume><Issue>1</Issue><PubDate><Year>2004</Year><Month>Oct</Month><Day>08</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Redox modulation of tau and microtubule-associated protein-2 by the glutathione/glutaredoxin reductase system.</ArticleTitle><Pagination><MedlinePgn>112-7</MedlinePgn></Pagination><Abstract><AbstractText>Alterations in the redox status of proteins have been implicated in the pathology of several neurodegenerative diseases including Alzheimer's and Parkinson's. We report that peroxynitrite and H2O2-induced disulfides in the porcine brain microtubule-associated proteins tau and microtubule-associated protein-2 are substrates for the glutaredoxin reductase system composed of glutathione reductase, human or Escherichia coli glutaredoxin, reduced glutathione, and NADPH. Oxidation and reduction of cysteines in tau and microtubule-associated protein-2 were quantitated by monitoring the incorporation of 5-iodoacetamido-fluorescein, a thiol-specific labeling reagent. Reduction of disulfide bonds in the microtubule-associated proteins by the glutaredoxin reductase system restored their ability to promote the assembly of microtubules composed of purified porcine tubulin. Thiol-disulfide exchange between oxidized glutathione and the microtubule-associated proteins was detected by monitoring protein oxidation and was quantitated by measuring reduced glutathione by HPLC.</AbstractText><CopyrightInformation>Copyright 2004 Elsevier Inc.</CopyrightInformation></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>Robinson</LastName><ForeName>Sarah H</ForeName><Initials>SH</Initials></Author><Author ValidYN="Y"><LastName>Skreslet</LastName><ForeName>Tabor E</ForeName><Initials>TE</Initials></Author><Author ValidYN="Y"><LastName>Cabral</LastName><ForeName>Diana M</ForeName><Initials>DM</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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IdType="pii">S0006-291X(04)01818-2</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Virginie</li></region></list><tree><noCountry><name sortKey="Cabral, Diana M" sort="Cabral, Diana M" uniqKey="Cabral D" first="Diana M" last="Cabral">Diana M. Cabral</name><name sortKey="Robinson, Sarah H" sort="Robinson, Sarah H" uniqKey="Robinson S" first="Sarah H" last="Robinson">Sarah H. Robinson</name><name sortKey="Skreslet, Tabor E" sort="Skreslet, Tabor E" uniqKey="Skreslet T" first="Tabor E" last="Skreslet">Tabor E. Skreslet</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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