Protein S-glutathionylation: from current basics to targeted modifications.
Identifieur interne : 000624 ( Main/Exploration ); précédent : 000623; suivant : 000625Protein S-glutathionylation: from current basics to targeted modifications.
Auteurs : Doina Popov [Roumanie]Source :
- Archives of physiology and biochemistry [ 1744-4160 ] ; 2014.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Thiols.
- métabolisme : Glutathion, Protéines.
- Animaux, Humains, Maturation post-traductionnelle des protéines, Stress oxydatif.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Sulfhydryl Compounds.
- chemical , metabolism : Glutathione, Proteins.
- Animals, Humans, Oxidative Stress, Protein Processing, Post-Translational.
Abstract
The interaction between antioxidant glutathione and the free thiol in susceptible cysteine residues of proteins leads to reversible protein S-glutathionylation. This reaction ensures cellular homeostasis control (as a common redox-dependent post-translational modification associated with signal transduction) and intervenes in oxidative stress-related cardiovascular pathology (as initiated by redox imbalance). The purpose of this review is to evaluate the recent knowledge on protein S-glutathionylation in terms of chemistry, broad cellular intervention, specific quantification, and potential for therapeutic exploitation. The data bases searched were Medline and PubMed, from 2009 to 2014 (term: glutathionylation). Protein S-glutathionylation ensures protection of protein thiols against irreversible over-oxidation, operates as a biological redox switch in both cell survival (influencing kinases and protein phosphatases pathways) and cell death (by potentiation of apoptosis), and cross-talks with phosphorylation and with S-nitrosylation. Collectively, protein S-glutathionylation appears as a valuable biomarker for oxidative stress, with potential for translation into novel therapeutic strategies.
DOI: 10.3109/13813455.2014.944544
PubMed: 25112365
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Simionescu" of the Romanian Academy , 8, B.P. Hasdeu Street, Bucharest 050568 , Romania.</nlm:affiliation><country xml:lang="fr">Roumanie</country><wicri:regionArea>Institute of Cellular Biology and Pathology "N. Simionescu" of the Romanian Academy , 8, B.P. 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This reaction ensures cellular homeostasis control (as a common redox-dependent post-translational modification associated with signal transduction) and intervenes in oxidative stress-related cardiovascular pathology (as initiated by redox imbalance). The purpose of this review is to evaluate the recent knowledge on protein S-glutathionylation in terms of chemistry, broad cellular intervention, specific quantification, and potential for therapeutic exploitation. The data bases searched were Medline and PubMed, from 2009 to 2014 (term: glutathionylation). Protein S-glutathionylation ensures protection of protein thiols against irreversible over-oxidation, operates as a biological redox switch in both cell survival (influencing kinases and protein phosphatases pathways) and cell death (by potentiation of apoptosis), and cross-talks with phosphorylation and with S-nitrosylation. Collectively, protein S-glutathionylation appears as a valuable biomarker for oxidative stress, with potential for translation into novel therapeutic strategies.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25112365</PMID><DateCompleted><Year>2015</Year><Month>06</Month><Day>09</Day></DateCompleted><DateRevised><Year>2014</Year><Month>10</Month><Day>01</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1744-4160</ISSN><JournalIssue CitedMedium="Internet"><Volume>120</Volume><Issue>4</Issue><PubDate><Year>2014</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Archives of physiology and biochemistry</Title><ISOAbbreviation>Arch Physiol Biochem</ISOAbbreviation></Journal><ArticleTitle>Protein S-glutathionylation: from current basics to targeted modifications.</ArticleTitle><Pagination><MedlinePgn>123-30</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.3109/13813455.2014.944544</ELocationID><Abstract><AbstractText>The interaction between antioxidant glutathione and the free thiol in susceptible cysteine residues of proteins leads to reversible protein S-glutathionylation. This reaction ensures cellular homeostasis control (as a common redox-dependent post-translational modification associated with signal transduction) and intervenes in oxidative stress-related cardiovascular pathology (as initiated by redox imbalance). The purpose of this review is to evaluate the recent knowledge on protein S-glutathionylation in terms of chemistry, broad cellular intervention, specific quantification, and potential for therapeutic exploitation. The data bases searched were Medline and PubMed, from 2009 to 2014 (term: glutathionylation). Protein S-glutathionylation ensures protection of protein thiols against irreversible over-oxidation, operates as a biological redox switch in both cell survival (influencing kinases and protein phosphatases pathways) and cell death (by potentiation of apoptosis), and cross-talks with phosphorylation and with S-nitrosylation. Collectively, protein S-glutathionylation appears as a valuable biomarker for oxidative stress, with potential for translation into novel therapeutic strategies.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Popov</LastName><ForeName>Doina</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Institute of Cellular Biology and Pathology "N. Simionescu" of the Romanian Academy , 8, B.P. Hasdeu Street, Bucharest 050568 , Romania.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>08</Month><Day>12</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Arch Physiol Biochem</MedlineTA><NlmUniqueID>9510153</NlmUniqueID><ISSNLinking>1381-3455</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013438">Sulfhydryl Compounds</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="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011499" MajorTopicYN="Y">Protein Processing, Post-Translational</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Cysteine</Keyword><Keyword MajorTopicYN="N">glutaredoxin</Keyword><Keyword MajorTopicYN="N">glutathione</Keyword><Keyword MajorTopicYN="N">protein tyrosine phosphatases (PTPs)</Keyword><Keyword MajorTopicYN="N">thioredoxin</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>8</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>8</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>6</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25112365</ArticleId><ArticleId IdType="doi">10.3109/13813455.2014.944544</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Roumanie</li></country></list><tree><country name="Roumanie"><noRegion><name sortKey="Popov, Doina" sort="Popov, Doina" uniqKey="Popov D" first="Doina" last="Popov">Doina Popov</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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