Redox in redux: Emergent roles for glutathione S-transferase P (GSTP) in regulation of cell signaling and S-glutathionylation.
Identifieur interne : 000C66 ( Main/Exploration ); précédent : 000C65; suivant : 000C67Redox in redux: Emergent roles for glutathione S-transferase P (GSTP) in regulation of cell signaling and S-glutathionylation.
Auteurs : Kenneth D. Tew [États-Unis]Source :
- Biochemical pharmacology [ 0006-2952 ] ; 2007.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Glutathion, Phosphotransferases.
- physiologie : Cellules eucaryotes, Glutathione transferase, Transduction du signal.
- Animaux, Humains, Maturation post-traductionnelle des protéines, Oxydoréduction.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Glutathione, Phosphotransferases.
- physiology : Eukaryotic Cells, Glutathione Transferase, Signal Transduction.
- Animals, Humans, Oxidation-Reduction, Protein Processing, Post-Translational.
Abstract
Glutathione (GSH) provides a major source of thiol homeostasis critical to the maintenance of a reduced cellular environment that is conducive to cell survival. Mammals have accumulated a significant cadre of sulfur containing proteins, the interactive significance of which has become clear in recent times. Glutathione transferases (GST) are prevalent in eukaryotes and have been ascribed catalytic functions that involve detoxification of electrophiles through thioether bond formation with the cysteine thiol of GSH. The neutralizing impact of these reactions on products of reactive oxygen has contributed to the significant evolutionary conservation and adaptive functional redundancy of the multifaceted GSH system. Amongst the GSTs, GSTP has been implicated in tumorigenesis and in anticancer drug resistance. Emerging studies indicate that GSTP has ligand binding properties and contributes in the regulation of signaling kinases through direct protein:protein interactions. Furthermore, S-glutathionylation is a post-translational modification of low pK(a) cysteine residues in target proteins. The forward rate of the S-glutathionylation reaction can be influenced by GSTP, whereas the reverse rate is affected by a number of redox sensitive proteins including glutaredoxin, thioredoxin and sulfiredoxin. The functional importance of these reactions in governing how cells respond to oxidative or nitrosative stress exemplifies the broad importance of GSH/GST homeostasis in conditions such as cancer, ageing and neurodegenerative diseases. GSTP has also provided a platform for therapeutic drug development where some agents have completed preclinical testing and are in clinical trial for the management of cancer.
DOI: 10.1016/j.bcp.2006.09.027
PubMed: 17098212
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Redox in redux: Emergent roles for glutathione S-transferase P (GSTP) in regulation of cell signaling and S-glutathionylation.</title><author><name sortKey="Tew, Kenneth D" sort="Tew, Kenneth D" uniqKey="Tew K" first="Kenneth D" last="Tew">Kenneth D. Tew</name><affiliation wicri:level="4"><nlm:affiliation>Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, 173 Ashley Avenue, P.O. Box 250505, Charleston, SC 29425, United States. tewk@musc.edu</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, 173 Ashley Avenue, P.O. Box 250505, Charleston, SC 29425</wicri:regionArea><placeName><region type="state">Caroline du Sud</region><settlement type="city">Columbia (Caroline du Sud)</settlement></placeName><orgName type="university">Université de Caroline du Sud</orgName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17098212</idno><idno type="pmid">17098212</idno><idno type="doi">10.1016/j.bcp.2006.09.027</idno><idno type="wicri:Area/Main/Corpus">000C99</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000C99</idno><idno type="wicri:Area/Main/Curation">000C99</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000C99</idno><idno type="wicri:Area/Main/Exploration">000C99</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Redox in redux: Emergent roles for glutathione S-transferase P (GSTP) in regulation of cell signaling and S-glutathionylation.</title><author><name sortKey="Tew, Kenneth D" sort="Tew, Kenneth D" uniqKey="Tew K" first="Kenneth D" last="Tew">Kenneth D. Tew</name><affiliation wicri:level="4"><nlm:affiliation>Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, 173 Ashley Avenue, P.O. Box 250505, Charleston, SC 29425, United States. tewk@musc.edu</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, 173 Ashley Avenue, P.O. Box 250505, Charleston, SC 29425</wicri:regionArea><placeName><region type="state">Caroline du Sud</region><settlement type="city">Columbia (Caroline du Sud)</settlement></placeName><orgName type="university">Université de Caroline du Sud</orgName></affiliation></author></analytic><series><title level="j">Biochemical pharmacology</title><idno type="ISSN">0006-2952</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Eukaryotic Cells (physiology)</term><term>Glutathione (metabolism)</term><term>Glutathione Transferase (physiology)</term><term>Humans (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Phosphotransferases (metabolism)</term><term>Protein Processing, Post-Translational (MeSH)</term><term>Signal Transduction (physiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Cellules eucaryotes (physiologie)</term><term>Glutathion (métabolisme)</term><term>Glutathione transferase (physiologie)</term><term>Humains (MeSH)</term><term>Maturation post-traductionnelle des protéines (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Phosphotransferases (métabolisme)</term><term>Transduction du signal (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term><term>Phosphotransferases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutathion</term><term>Phosphotransferases</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Cellules eucaryotes</term><term>Glutathione transferase</term><term>Transduction du signal</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Eukaryotic Cells</term><term>Glutathione Transferase</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term><term>Oxidation-Reduction</term><term>Protein Processing, Post-Translational</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Humains</term><term>Maturation post-traductionnelle des protéines</term><term>Oxydoréduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutathione (GSH) provides a major source of thiol homeostasis critical to the maintenance of a reduced cellular environment that is conducive to cell survival. Mammals have accumulated a significant cadre of sulfur containing proteins, the interactive significance of which has become clear in recent times. Glutathione transferases (GST) are prevalent in eukaryotes and have been ascribed catalytic functions that involve detoxification of electrophiles through thioether bond formation with the cysteine thiol of GSH. The neutralizing impact of these reactions on products of reactive oxygen has contributed to the significant evolutionary conservation and adaptive functional redundancy of the multifaceted GSH system. Amongst the GSTs, GSTP has been implicated in tumorigenesis and in anticancer drug resistance. Emerging studies indicate that GSTP has ligand binding properties and contributes in the regulation of signaling kinases through direct protein:protein interactions. Furthermore, S-glutathionylation is a post-translational modification of low pK(a) cysteine residues in target proteins. The forward rate of the S-glutathionylation reaction can be influenced by GSTP, whereas the reverse rate is affected by a number of redox sensitive proteins including glutaredoxin, thioredoxin and sulfiredoxin. The functional importance of these reactions in governing how cells respond to oxidative or nitrosative stress exemplifies the broad importance of GSH/GST homeostasis in conditions such as cancer, ageing and neurodegenerative diseases. GSTP has also provided a platform for therapeutic drug development where some agents have completed preclinical testing and are in clinical trial for the management of cancer.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17098212</PMID><DateCompleted><Year>2007</Year><Month>05</Month><Day>17</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-2952</ISSN><JournalIssue CitedMedium="Print"><Volume>73</Volume><Issue>9</Issue><PubDate><Year>2007</Year><Month>May</Month><Day>01</Day></PubDate></JournalIssue><Title>Biochemical pharmacology</Title><ISOAbbreviation>Biochem Pharmacol</ISOAbbreviation></Journal><ArticleTitle>Redox in redux: Emergent roles for glutathione S-transferase P (GSTP) in regulation of cell signaling and S-glutathionylation.</ArticleTitle><Pagination><MedlinePgn>1257-69</MedlinePgn></Pagination><Abstract><AbstractText>Glutathione (GSH) provides a major source of thiol homeostasis critical to the maintenance of a reduced cellular environment that is conducive to cell survival. Mammals have accumulated a significant cadre of sulfur containing proteins, the interactive significance of which has become clear in recent times. Glutathione transferases (GST) are prevalent in eukaryotes and have been ascribed catalytic functions that involve detoxification of electrophiles through thioether bond formation with the cysteine thiol of GSH. The neutralizing impact of these reactions on products of reactive oxygen has contributed to the significant evolutionary conservation and adaptive functional redundancy of the multifaceted GSH system. Amongst the GSTs, GSTP has been implicated in tumorigenesis and in anticancer drug resistance. Emerging studies indicate that GSTP has ligand binding properties and contributes in the regulation of signaling kinases through direct protein:protein interactions. Furthermore, S-glutathionylation is a post-translational modification of low pK(a) cysteine residues in target proteins. The forward rate of the S-glutathionylation reaction can be influenced by GSTP, whereas the reverse rate is affected by a number of redox sensitive proteins including glutaredoxin, thioredoxin and sulfiredoxin. The functional importance of these reactions in governing how cells respond to oxidative or nitrosative stress exemplifies the broad importance of GSH/GST homeostasis in conditions such as cancer, ageing and neurodegenerative diseases. GSTP has also provided a platform for therapeutic drug development where some agents have completed preclinical testing and are in clinical trial for the management of cancer.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tew</LastName><ForeName>Kenneth D</ForeName><Initials>KD</Initials><AffiliationInfo><Affiliation>Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, 173 Ashley Avenue, P.O. Box 250505, Charleston, SC 29425, United States. tewk@musc.edu</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2006</Year><Month>10</Month><Day>04</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Biochem Pharmacol</MedlineTA><NlmUniqueID>0101032</NlmUniqueID><ISSNLinking>0006-2952</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>EC 2.5.1.18</RegistryNumber><NameOfSubstance UI="D005982">Glutathione Transferase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.-</RegistryNumber><NameOfSubstance UI="D010770">Phosphotransferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005057" MajorTopicYN="N">Eukaryotic Cells</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005982" MajorTopicYN="N">Glutathione Transferase</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010770" MajorTopicYN="N">Phosphotransferases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011499" MajorTopicYN="N">Protein Processing, Post-Translational</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2006</Year><Month>08</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2006</Year><Month>09</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2006</Year><Month>09</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>11</Month><Day>14</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>5</Month><Day>18</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>11</Month><Day>14</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17098212</ArticleId><ArticleId IdType="pii">S0006-2952(06)00620-4</ArticleId><ArticleId IdType="doi">10.1016/j.bcp.2006.09.027</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Caroline du Sud</li></region><settlement><li>Columbia (Caroline du Sud)</li></settlement><orgName><li>Université de Caroline du Sud</li></orgName></list><tree><country name="États-Unis"><region name="Caroline du Sud"><name sortKey="Tew, Kenneth D" sort="Tew, Kenneth D" uniqKey="Tew K" first="Kenneth D" last="Tew">Kenneth D. Tew</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/GlutaredoxinV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000C66 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000C66 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= GlutaredoxinV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:17098212
|texte= Redox in redux: Emergent roles for glutathione S-transferase P (GSTP) in regulation of cell signaling and S-glutathionylation.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:17098212" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |