Measurement and meaning of cellular thiol:disufhide redox status.
Identifieur interne : 000445 ( Main/Exploration ); précédent : 000444; suivant : 000446Measurement and meaning of cellular thiol:disufhide redox status.
Auteurs : Marcelo A. Comini [Uruguay]Source :
- Free radical research [ 1029-2470 ] ; 2016.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Bactéries (MeSH), Colorants fluorescents (MeSH), Disulfures (analyse), Disulfures (métabolisme), Eucaryotes (MeSH), Glutathion (métabolisme), Humains (MeSH), Oxydoréduction (MeSH), Protéines (métabolisme), Protéomique (méthodes), Stress oxydatif (MeSH), Techniques de chimie analytique (méthodes), Thiols (analyse), Thiols (métabolisme).
- MESH :
- analyse : Disulfures, Thiols.
- métabolisme : Disulfures, Glutathion, Protéines, Thiols.
- méthodes : Protéomique, Techniques de chimie analytique.
- Animaux, Bactéries, Colorants fluorescents, Eucaryotes, Humains, Oxydoréduction, Stress oxydatif.
English descriptors
- KwdEn :
- Animals (MeSH), Bacteria (MeSH), Chemistry Techniques, Analytical (methods), Disulfides (analysis), Disulfides (metabolism), Eukaryota (MeSH), Fluorescent Dyes (MeSH), Glutathione (metabolism), Humans (MeSH), Oxidation-Reduction (MeSH), Oxidative Stress (MeSH), Proteins (metabolism), Proteomics (methods), Sulfhydryl Compounds (analysis), Sulfhydryl Compounds (metabolism).
- MESH :
- chemical , analysis : Disulfides, Sulfhydryl Compounds.
- chemical , metabolism : Disulfides, Glutathione, Proteins, Sulfhydryl Compounds.
- methods : Chemistry Techniques, Analytical, Proteomics.
- Animals, Bacteria, Eukaryota, Fluorescent Dyes, Humans, Oxidation-Reduction, Oxidative Stress.
Abstract
The functional group of cysteine is a thiol group (SH) that, due to its chemical reactivity, is able to undergo a wide array of modifications each with the potential to confer a different property or function to the molecule harboring this residue. Most of these modifications involve the reversible oxidation of the thiol to sulfenic acid (SOH), and disulfide, including intra- and intermolecular disulfides between polypeptides and glutathione (glutathionylation). The reversibility of these oxidations allows thiol groups to serve as versatile chemical and structural transducing elements in several low molecular mass metabolites and proteins. A plethora of cellular functions such as DNA and protein synthesis, protein secretion, cytoskeleton architecture, differentiation, apoptosis, and anti-oxidant defense, are recognized to be modulated, at certain stage, by thiol-disulfide exchange mechanisms of redox active thiol groups. All organisms are equipped with enzymatic systems composed by NADPH-dependent reductases, redoxins, and peroxidases that provide kinetic control of global thiol-redox homeostasis as well as target selectivity. These redox systems are distributed in different subcellular compartments and are not in equilibrium with each other. In consequence, measuring cellular thiol-disulfide status represents a challenge for studies aimed to obtain dynamic and spatio-temporal resolution. This review provides a summary of the methods and tools available to quantify the thiol redox status of cells.
DOI: 10.3109/10715762.2015.1110241
PubMed: 26695718
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Measurement and meaning of cellular thiol:disufhide redox status.</title><author><name sortKey="Comini, Marcelo A" sort="Comini, Marcelo A" uniqKey="Comini M" first="Marcelo A" last="Comini">Marcelo A. Comini</name><affiliation wicri:level="1"><nlm:affiliation>a Laboratory Redox Biology of Trypanosomes , Institut Pasteur de Montevideo , Mataojo 2020 , Montevideo , Uruguay.</nlm:affiliation><country xml:lang="fr">Uruguay</country><wicri:regionArea>a Laboratory Redox Biology of Trypanosomes , Institut Pasteur de Montevideo , Mataojo 2020 , Montevideo </wicri:regionArea><wicri:noRegion>Montevideo </wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2016">2016</date><idno type="RBID">pubmed:26695718</idno><idno type="pmid">26695718</idno><idno type="doi">10.3109/10715762.2015.1110241</idno><idno type="wicri:Area/Main/Corpus">000473</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000473</idno><idno type="wicri:Area/Main/Curation">000473</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000473</idno><idno type="wicri:Area/Main/Exploration">000473</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Measurement and meaning of cellular thiol:disufhide redox status.</title><author><name sortKey="Comini, Marcelo A" sort="Comini, Marcelo A" uniqKey="Comini M" first="Marcelo A" last="Comini">Marcelo A. Comini</name><affiliation wicri:level="1"><nlm:affiliation>a Laboratory Redox Biology of Trypanosomes , Institut Pasteur de Montevideo , Mataojo 2020 , Montevideo , Uruguay.</nlm:affiliation><country xml:lang="fr">Uruguay</country><wicri:regionArea>a Laboratory Redox Biology of Trypanosomes , Institut Pasteur de Montevideo , Mataojo 2020 , Montevideo </wicri:regionArea><wicri:noRegion>Montevideo </wicri:noRegion></affiliation></author></analytic><series><title level="j">Free radical research</title><idno type="eISSN">1029-2470</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Bacteria (MeSH)</term><term>Chemistry Techniques, Analytical (methods)</term><term>Disulfides (analysis)</term><term>Disulfides (metabolism)</term><term>Eukaryota (MeSH)</term><term>Fluorescent Dyes (MeSH)</term><term>Glutathione (metabolism)</term><term>Humans (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidative Stress (MeSH)</term><term>Proteins (metabolism)</term><term>Proteomics (methods)</term><term>Sulfhydryl Compounds (analysis)</term><term>Sulfhydryl Compounds (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Bactéries (MeSH)</term><term>Colorants fluorescents (MeSH)</term><term>Disulfures (analyse)</term><term>Disulfures (métabolisme)</term><term>Eucaryotes (MeSH)</term><term>Glutathion (métabolisme)</term><term>Humains (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Protéines (métabolisme)</term><term>Protéomique (méthodes)</term><term>Stress oxydatif (MeSH)</term><term>Techniques de chimie analytique (méthodes)</term><term>Thiols (analyse)</term><term>Thiols (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Disulfides</term><term>Sulfhydryl Compounds</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Disulfides</term><term>Glutathione</term><term>Proteins</term><term>Sulfhydryl Compounds</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Disulfures</term><term>Thiols</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Chemistry Techniques, Analytical</term><term>Proteomics</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Disulfures</term><term>Glutathion</term><term>Protéines</term><term>Thiols</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Protéomique</term><term>Techniques de chimie analytique</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Bacteria</term><term>Eukaryota</term><term>Fluorescent Dyes</term><term>Humans</term><term>Oxidation-Reduction</term><term>Oxidative Stress</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Bactéries</term><term>Colorants fluorescents</term><term>Eucaryotes</term><term>Humains</term><term>Oxydoréduction</term><term>Stress oxydatif</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The functional group of cysteine is a thiol group (SH) that, due to its chemical reactivity, is able to undergo a wide array of modifications each with the potential to confer a different property or function to the molecule harboring this residue. Most of these modifications involve the reversible oxidation of the thiol to sulfenic acid (SOH), and disulfide, including intra- and intermolecular disulfides between polypeptides and glutathione (glutathionylation). The reversibility of these oxidations allows thiol groups to serve as versatile chemical and structural transducing elements in several low molecular mass metabolites and proteins. A plethora of cellular functions such as DNA and protein synthesis, protein secretion, cytoskeleton architecture, differentiation, apoptosis, and anti-oxidant defense, are recognized to be modulated, at certain stage, by thiol-disulfide exchange mechanisms of redox active thiol groups. All organisms are equipped with enzymatic systems composed by NADPH-dependent reductases, redoxins, and peroxidases that provide kinetic control of global thiol-redox homeostasis as well as target selectivity. These redox systems are distributed in different subcellular compartments and are not in equilibrium with each other. In consequence, measuring cellular thiol-disulfide status represents a challenge for studies aimed to obtain dynamic and spatio-temporal resolution. This review provides a summary of the methods and tools available to quantify the thiol redox status of cells. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26695718</PMID><DateCompleted><Year>2016</Year><Month>10</Month><Day>19</Day></DateCompleted><DateRevised><Year>2016</Year><Month>12</Month><Day>30</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1029-2470</ISSN><JournalIssue CitedMedium="Internet"><Volume>50</Volume><Issue>2</Issue><PubDate><Year>2016</Year></PubDate></JournalIssue><Title>Free radical research</Title><ISOAbbreviation>Free Radic Res</ISOAbbreviation></Journal><ArticleTitle>Measurement and meaning of cellular thiol:disufhide redox status.</ArticleTitle><Pagination><MedlinePgn>246-71</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.3109/10715762.2015.1110241</ELocationID><Abstract><AbstractText>The functional group of cysteine is a thiol group (SH) that, due to its chemical reactivity, is able to undergo a wide array of modifications each with the potential to confer a different property or function to the molecule harboring this residue. Most of these modifications involve the reversible oxidation of the thiol to sulfenic acid (SOH), and disulfide, including intra- and intermolecular disulfides between polypeptides and glutathione (glutathionylation). The reversibility of these oxidations allows thiol groups to serve as versatile chemical and structural transducing elements in several low molecular mass metabolites and proteins. A plethora of cellular functions such as DNA and protein synthesis, protein secretion, cytoskeleton architecture, differentiation, apoptosis, and anti-oxidant defense, are recognized to be modulated, at certain stage, by thiol-disulfide exchange mechanisms of redox active thiol groups. All organisms are equipped with enzymatic systems composed by NADPH-dependent reductases, redoxins, and peroxidases that provide kinetic control of global thiol-redox homeostasis as well as target selectivity. These redox systems are distributed in different subcellular compartments and are not in equilibrium with each other. In consequence, measuring cellular thiol-disulfide status represents a challenge for studies aimed to obtain dynamic and spatio-temporal resolution. This review provides a summary of the methods and tools available to quantify the thiol redox status of cells. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Comini</LastName><ForeName>Marcelo A</ForeName><Initials>MA</Initials><AffiliationInfo><Affiliation>a Laboratory Redox Biology of Trypanosomes , Institut Pasteur de Montevideo , Mataojo 2020 , Montevideo , Uruguay.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Free Radic Res</MedlineTA><NlmUniqueID>9423872</NlmUniqueID><ISSNLinking>1029-2470</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005456">Fluorescent Dyes</NameOfSubstance></Chemical><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="D001419" MajorTopicYN="N">Bacteria</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002623" MajorTopicYN="N">Chemistry Techniques, Analytical</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D056890" MajorTopicYN="N">Eukaryota</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005456" MajorTopicYN="N">Fluorescent Dyes</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="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D040901" MajorTopicYN="N">Proteomics</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Glutaredoxin</Keyword><Keyword MajorTopicYN="N">glutathione</Keyword><Keyword MajorTopicYN="N">redox biosensor</Keyword><Keyword MajorTopicYN="N">redox signaling</Keyword><Keyword MajorTopicYN="N">thioredoxin</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>12</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>12</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>11</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26695718</ArticleId><ArticleId IdType="doi">10.3109/10715762.2015.1110241</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Uruguay</li></country></list><tree><country name="Uruguay"><noRegion><name sortKey="Comini, Marcelo A" sort="Comini, Marcelo A" uniqKey="Comini M" first="Marcelo A" last="Comini">Marcelo A. Comini</name></noRegion></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 000445 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000445 | 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:26695718
|texte= Measurement and meaning of cellular thiol:disufhide redox status.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:26695718" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |