Selective inactivation of glutaredoxin by sporidesmin and other epidithiopiperazinediones.
Identifieur interne : 000D13 ( Main/Exploration ); précédent : 000D12; suivant : 000D14Selective inactivation of glutaredoxin by sporidesmin and other epidithiopiperazinediones.
Auteurs : Usha Srinivasan [États-Unis] ; Aveenash Bala ; Shu-Chuan Jao ; David W. Starke ; T William Jordan ; John J. MieyalSource :
- Biochemistry [ 0006-2960 ] ; 2006.
Descripteurs français
- KwdFr :
- Disulfures (pharmacologie), Dithiothréitol (composition chimique), Gliotoxine (pharmacologie), Glutarédoxines (MeSH), Glutathion (métabolisme), Modèles chimiques (MeSH), Oxidoreductases (antagonistes et inhibiteurs), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Pipérazines (pharmacologie), Relation structure-activité (MeSH), Spectrométrie de masse MALDI (MeSH), Sporidesmines (métabolisme), Sporidesmines (pharmacologie), Substitution d'acide aminé (MeSH).
- MESH :
- antagonistes et inhibiteurs : Oxidoreductases.
- composition chimique : Dithiothréitol.
- génétique : Oxidoreductases.
- métabolisme : Glutathion, Oxidoreductases, Sporidesmines.
- pharmacologie : Disulfures, Gliotoxine, Pipérazines, Sporidesmines.
- Glutarédoxines, Modèles chimiques, Relation structure-activité, Spectrométrie de masse MALDI, Substitution d'acide aminé.
English descriptors
- KwdEn :
- Amino Acid Substitution (MeSH), Disulfides (pharmacology), Dithiothreitol (chemistry), Gliotoxin (pharmacology), Glutaredoxins (MeSH), Glutathione (metabolism), Models, Chemical (MeSH), Oxidoreductases (antagonists & inhibitors), Oxidoreductases (genetics), Oxidoreductases (metabolism), Piperazines (pharmacology), Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization (MeSH), Sporidesmins (metabolism), Sporidesmins (pharmacology), Structure-Activity Relationship (MeSH).
- MESH :
- chemical , antagonists & inhibitors : Oxidoreductases.
- chemical , chemistry : Dithiothreitol.
- chemical , genetics : Oxidoreductases.
- chemical , metabolism : Glutathione, Oxidoreductases, Sporidesmins.
- chemical , pharmacology : Disulfides, Gliotoxin, Piperazines, Sporidesmins.
- Amino Acid Substitution, Glutaredoxins, Models, Chemical, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Structure-Activity Relationship.
Abstract
Glutaredoxin (thioltransferase) is a thiol-disulfide oxidoreductase that displays efficient and specific catalysis of protein-SSG deglutathionylation and is thereby implicated in homeostatic regulation of the thiol-disulfide status of cellular proteins. Sporidesmin is an epidithiopiperazine-2,5-dione (ETP) fungal toxin that disrupts cellular functions likely via oxidative alteration of cysteine residues on key proteins. In the current study sporidesmin inactivated human glutaredoxin in a time- and concentration-dependent manner. Under comparable conditions other thiol-disulfide oxidoreductase enzymes, glutathione reductase, thioredoxin, and thioredoxin reductase, were unaffected by sporidesmin. Inactivation of glutaredoxin required the reduced (dithiol) form of the enzyme, the oxidized (intramolecular disulfide) form of sporidesmin, and molecular oxygen. The inactivated glutaredoxin could be reactivated by dithiothreitol only in the presence of urea, followed by removal of the denaturant, indicating that inactivation of the enzyme involves a conformationally inaccessible disulfide bond(s). Various cysteine-to-serine mutants of glutaredoxin were resistant to inactivation by sporidesmin, suggesting that the inactivation reaction specifically involves at least two of the five cysteine residues in human glutaredoxin. The relative ability of various epidithiopiperazine-2,5-diones to inactivate glutaredoxin indicated that at least one phenyl substituent was required in addition to the epidithiodioxopiperazine moiety for inhibitory activity. Mass spectrometry of the modified protein is consistent with formation of intermolecular disulfides, containing one adducted toxin per glutaredoxin but with elimination of two sulfur atoms from the detected product. We suggest that the initial reaction is between the toxin sulfurs and cysteine 22 in the glutaredoxin active site. This study implicates selective modification of sulfhydryls of target proteins in some of the cytotoxic effects of the ETP fungal toxins and their synthetic analogues.
DOI: 10.1021/bi060440o
PubMed: 16846241
PubMed Central: PMC3199604
Affiliations:
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Starke</name></author><author><name sortKey="Jordan, T William" sort="Jordan, T William" uniqKey="Jordan T" first="T William" last="Jordan">T William Jordan</name></author><author><name sortKey="Mieyal, John J" sort="Mieyal, John J" uniqKey="Mieyal J" first="John J" last="Mieyal">John J. Mieyal</name></author></analytic><series><title level="j">Biochemistry</title><idno type="ISSN">0006-2960</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Substitution (MeSH)</term><term>Disulfides (pharmacology)</term><term>Dithiothreitol (chemistry)</term><term>Gliotoxin (pharmacology)</term><term>Glutaredoxins (MeSH)</term><term>Glutathione (metabolism)</term><term>Models, Chemical (MeSH)</term><term>Oxidoreductases (antagonists & inhibitors)</term><term>Oxidoreductases (genetics)</term><term>Oxidoreductases (metabolism)</term><term>Piperazines (pharmacology)</term><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization (MeSH)</term><term>Sporidesmins (metabolism)</term><term>Sporidesmins (pharmacology)</term><term>Structure-Activity Relationship (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Disulfures (pharmacologie)</term><term>Dithiothréitol (composition chimique)</term><term>Gliotoxine (pharmacologie)</term><term>Glutarédoxines (MeSH)</term><term>Glutathion (métabolisme)</term><term>Modèles chimiques (MeSH)</term><term>Oxidoreductases (antagonistes et inhibiteurs)</term><term>Oxidoreductases (génétique)</term><term>Oxidoreductases (métabolisme)</term><term>Pipérazines (pharmacologie)</term><term>Relation structure-activité (MeSH)</term><term>Spectrométrie de masse MALDI (MeSH)</term><term>Sporidesmines (métabolisme)</term><term>Sporidesmines (pharmacologie)</term><term>Substitution d'acide aminé (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Dithiothreitol</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term><term>Oxidoreductases</term><term>Sporidesmins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Disulfides</term><term>Gliotoxin</term><term>Piperazines</term><term>Sporidesmins</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Dithiothréitol</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutathion</term><term>Oxidoreductases</term><term>Sporidesmines</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Disulfures</term><term>Gliotoxine</term><term>Pipérazines</term><term>Sporidesmines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Substitution</term><term>Glutaredoxins</term><term>Models, Chemical</term><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</term><term>Structure-Activity Relationship</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Glutarédoxines</term><term>Modèles chimiques</term><term>Relation structure-activité</term><term>Spectrométrie de masse MALDI</term><term>Substitution d'acide aminé</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxin (thioltransferase) is a thiol-disulfide oxidoreductase that displays efficient and specific catalysis of protein-SSG deglutathionylation and is thereby implicated in homeostatic regulation of the thiol-disulfide status of cellular proteins. Sporidesmin is an epidithiopiperazine-2,5-dione (ETP) fungal toxin that disrupts cellular functions likely via oxidative alteration of cysteine residues on key proteins. In the current study sporidesmin inactivated human glutaredoxin in a time- and concentration-dependent manner. Under comparable conditions other thiol-disulfide oxidoreductase enzymes, glutathione reductase, thioredoxin, and thioredoxin reductase, were unaffected by sporidesmin. Inactivation of glutaredoxin required the reduced (dithiol) form of the enzyme, the oxidized (intramolecular disulfide) form of sporidesmin, and molecular oxygen. The inactivated glutaredoxin could be reactivated by dithiothreitol only in the presence of urea, followed by removal of the denaturant, indicating that inactivation of the enzyme involves a conformationally inaccessible disulfide bond(s). Various cysteine-to-serine mutants of glutaredoxin were resistant to inactivation by sporidesmin, suggesting that the inactivation reaction specifically involves at least two of the five cysteine residues in human glutaredoxin. The relative ability of various epidithiopiperazine-2,5-diones to inactivate glutaredoxin indicated that at least one phenyl substituent was required in addition to the epidithiodioxopiperazine moiety for inhibitory activity. Mass spectrometry of the modified protein is consistent with formation of intermolecular disulfides, containing one adducted toxin per glutaredoxin but with elimination of two sulfur atoms from the detected product. We suggest that the initial reaction is between the toxin sulfurs and cysteine 22 in the glutaredoxin active site. This study implicates selective modification of sulfhydryls of target proteins in some of the cytotoxic effects of the ETP fungal toxins and their synthetic analogues.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16846241</PMID><DateCompleted><Year>2006</Year><Month>08</Month><Day>30</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-2960</ISSN><JournalIssue CitedMedium="Print"><Volume>45</Volume><Issue>29</Issue><PubDate><Year>2006</Year><Month>Jul</Month><Day>25</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>Selective inactivation of glutaredoxin by sporidesmin and other epidithiopiperazinediones.</ArticleTitle><Pagination><MedlinePgn>8978-87</MedlinePgn></Pagination><Abstract><AbstractText>Glutaredoxin (thioltransferase) is a thiol-disulfide oxidoreductase that displays efficient and specific catalysis of protein-SSG deglutathionylation and is thereby implicated in homeostatic regulation of the thiol-disulfide status of cellular proteins. Sporidesmin is an epidithiopiperazine-2,5-dione (ETP) fungal toxin that disrupts cellular functions likely via oxidative alteration of cysteine residues on key proteins. In the current study sporidesmin inactivated human glutaredoxin in a time- and concentration-dependent manner. Under comparable conditions other thiol-disulfide oxidoreductase enzymes, glutathione reductase, thioredoxin, and thioredoxin reductase, were unaffected by sporidesmin. Inactivation of glutaredoxin required the reduced (dithiol) form of the enzyme, the oxidized (intramolecular disulfide) form of sporidesmin, and molecular oxygen. The inactivated glutaredoxin could be reactivated by dithiothreitol only in the presence of urea, followed by removal of the denaturant, indicating that inactivation of the enzyme involves a conformationally inaccessible disulfide bond(s). Various cysteine-to-serine mutants of glutaredoxin were resistant to inactivation by sporidesmin, suggesting that the inactivation reaction specifically involves at least two of the five cysteine residues in human glutaredoxin. The relative ability of various epidithiopiperazine-2,5-diones to inactivate glutaredoxin indicated that at least one phenyl substituent was required in addition to the epidithiodioxopiperazine moiety for inhibitory activity. Mass spectrometry of the modified protein is consistent with formation of intermolecular disulfides, containing one adducted toxin per glutaredoxin but with elimination of two sulfur atoms from the detected product. We suggest that the initial reaction is between the toxin sulfurs and cysteine 22 in the glutaredoxin active site. This study implicates selective modification of sulfhydryls of target proteins in some of the cytotoxic effects of the ETP fungal toxins and their synthetic analogues.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Srinivasan</LastName><ForeName>Usha</ForeName><Initials>U</Initials><AffiliationInfo><Affiliation>Department of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106-4965, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bala</LastName><ForeName>Aveenash</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Jao</LastName><ForeName>Shu-chuan</ForeName><Initials>SC</Initials></Author><Author ValidYN="Y"><LastName>Starke</LastName><ForeName>David W</ForeName><Initials>DW</Initials></Author><Author ValidYN="Y"><LastName>Jordan</LastName><ForeName>T William</ForeName><Initials>TW</Initials></Author><Author ValidYN="Y"><LastName>Mieyal</LastName><ForeName>John J</ForeName><Initials>JJ</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>P01 AG015885</GrantID><Acronym>AG</Acronym><Agency>NIA NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01-AG 024413</GrantID><Acronym>AG</Acronym><Agency>NIA NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>A1 36219</GrantID><Agency>PHS HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>P01-AG15885</GrantID><Acronym>AG</Acronym><Agency>NIA NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 AG024413</GrantID><Acronym>AG</Acronym><Agency>NIA NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochemistry</MedlineTA><NlmUniqueID>0370623</NlmUniqueID><ISSNLinking>0006-2960</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010879">Piperazines</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013173">Sporidesmins</NameOfSubstance></Chemical><Chemical><RegistryNumber>64474-15-3</RegistryNumber><NameOfSubstance UI="C003905">3,6-bis(5-chloro-2-piperidyl)-2,5-piperazinedione</NameOfSubstance></Chemical><Chemical><RegistryNumber>67-99-2</RegistryNumber><NameOfSubstance UI="D005912">Gliotoxin</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>H70LC3H0RW</RegistryNumber><NameOfSubstance UI="C001873">sporidesmin</NameOfSubstance></Chemical><Chemical><RegistryNumber>T8ID5YZU6Y</RegistryNumber><NameOfSubstance UI="D004229">Dithiothreitol</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D019943" MajorTopicYN="N">Amino Acid Substitution</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004229" MajorTopicYN="N">Dithiothreitol</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005912" MajorTopicYN="N">Gliotoxin</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008956" MajorTopicYN="N">Models, Chemical</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010879" MajorTopicYN="N">Piperazines</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019032" MajorTopicYN="N">Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013173" MajorTopicYN="N">Sporidesmins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013329" MajorTopicYN="N">Structure-Activity Relationship</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>7</Month><Day>19</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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last="Jordan">T William Jordan</name><name sortKey="Mieyal, John J" sort="Mieyal, John J" uniqKey="Mieyal J" first="John J" last="Mieyal">John J. Mieyal</name><name sortKey="Starke, David W" sort="Starke, David W" uniqKey="Starke D" first="David W" last="Starke">David W. Starke</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Srinivasan, Usha" sort="Srinivasan, Usha" uniqKey="Srinivasan U" first="Usha" last="Srinivasan">Usha Srinivasan</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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