Mitochondrial thiols in antioxidant protection and redox signaling: distinct roles for glutathionylation and other thiol modifications.
Identifieur interne : 000844 ( Main/Exploration ); précédent : 000843; suivant : 000845Mitochondrial thiols in antioxidant protection and redox signaling: distinct roles for glutathionylation and other thiol modifications.
Auteurs : Michael P. Murphy [Royaume-Uni]Source :
- Antioxidants & redox signaling [ 1557-7716 ] ; 2012.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Antioxydants, Mitochondries, Thiols.
- métabolisme : Antioxydants, Glutathion, Mitochondries, Thiols.
- Animaux, Humains, Oxydoréduction, Transduction du signal.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Antioxidants, Sulfhydryl Compounds.
- chemical , metabolism : Antioxidants, Glutathione, Sulfhydryl Compounds.
- chemistry : Mitochondria.
- metabolism : Mitochondria.
- Animals, Humans, Oxidation-Reduction, Signal Transduction.
Abstract
SIGNIFICANCE
The mitochondrial matrix contains much of the machinery at the heart of metabolism. This compartment is also exposed to a high and continual flux of superoxide, hydrogen peroxide, and related reactive species. To protect mitochondria from these sources of oxidative damage, there is an integrated set of thiol systems within the matrix comprising the thioredoxin/peroxiredoxin/methionine sulfoxide reductase pathways and the glutathione/glutathione peroxidase/glutathione-S-transferase/glutaredoxin pathways that in conjunction with protein thiols prevent much of this oxidative damage. In addition, the changes in the redox state of many components of these mitochondrial thiol systems may transduce and relay redox signals within and through the mitochondrial matrix to modulate the activity of biochemical processes.
RECENT ADVANCES
Here, mitochondrial thiol systems are reviewed, and areas of uncertainty are pointed out, focusing on recent developments in our understanding of their roles.
CRITICAL ISSUES
The areas of particular focus are on the multiple, overlapping roles of mitochondrial thiols and on understanding how these thiols contribute to both antioxidant defenses and redox signaling.
FUTURE DIRECTIONS
Recent technical progress in the identification and quantification of thiol modifications by redox proteomics means that many of the questions raised about the multiple roles of mitochondrial thiols can now be addressed.
DOI: 10.1089/ars.2011.4289
PubMed: 21954972
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Murphy</name><affiliation wicri:level="1"><nlm:affiliation>MRC Mitochondrial Biology Unit, Cambridge, United Kingdom. mpm@mrc-mbu.cam.ac.uk</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>MRC Mitochondrial Biology Unit, Cambridge</wicri:regionArea><wicri:noRegion>Cambridge</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2012">2012</date><idno type="RBID">pubmed:21954972</idno><idno type="pmid">21954972</idno><idno type="doi">10.1089/ars.2011.4289</idno><idno type="wicri:Area/Main/Corpus">000891</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000891</idno><idno type="wicri:Area/Main/Curation">000891</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000891</idno><idno type="wicri:Area/Main/Exploration">000891</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Mitochondrial thiols in antioxidant protection and redox signaling: distinct roles for glutathionylation and other thiol modifications.</title><author><name sortKey="Murphy, Michael P" sort="Murphy, Michael P" uniqKey="Murphy M" first="Michael P" last="Murphy">Michael P. Murphy</name><affiliation wicri:level="1"><nlm:affiliation>MRC Mitochondrial Biology Unit, Cambridge, United Kingdom. mpm@mrc-mbu.cam.ac.uk</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>MRC Mitochondrial Biology Unit, Cambridge</wicri:regionArea><wicri:noRegion>Cambridge</wicri:noRegion></affiliation></author></analytic><series><title level="j">Antioxidants & redox signaling</title><idno type="eISSN">1557-7716</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Antioxidants (chemistry)</term><term>Antioxidants (metabolism)</term><term>Glutathione (metabolism)</term><term>Humans (MeSH)</term><term>Mitochondria (chemistry)</term><term>Mitochondria (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Signal Transduction (MeSH)</term><term>Sulfhydryl Compounds (chemistry)</term><term>Sulfhydryl Compounds (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Antioxydants (composition chimique)</term><term>Antioxydants (métabolisme)</term><term>Glutathion (métabolisme)</term><term>Humains (MeSH)</term><term>Mitochondries (composition chimique)</term><term>Mitochondries (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Thiols (composition chimique)</term><term>Thiols (métabolisme)</term><term>Transduction du signal (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antioxidants</term><term>Sulfhydryl Compounds</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antioxidants</term><term>Glutathione</term><term>Sulfhydryl Compounds</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Mitochondria</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Antioxydants</term><term>Mitochondries</term><term>Thiols</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Mitochondria</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Antioxydants</term><term>Glutathion</term><term>Mitochondries</term><term>Thiols</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term><term>Oxidation-Reduction</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Humains</term><term>Oxydoréduction</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>SIGNIFICANCE</b></p><p>The mitochondrial matrix contains much of the machinery at the heart of metabolism. This compartment is also exposed to a high and continual flux of superoxide, hydrogen peroxide, and related reactive species. To protect mitochondria from these sources of oxidative damage, there is an integrated set of thiol systems within the matrix comprising the thioredoxin/peroxiredoxin/methionine sulfoxide reductase pathways and the glutathione/glutathione peroxidase/glutathione-S-transferase/glutaredoxin pathways that in conjunction with protein thiols prevent much of this oxidative damage. In addition, the changes in the redox state of many components of these mitochondrial thiol systems may transduce and relay redox signals within and through the mitochondrial matrix to modulate the activity of biochemical processes.</p></div><div type="abstract" xml:lang="en"><p><b>RECENT ADVANCES</b></p><p>Here, mitochondrial thiol systems are reviewed, and areas of uncertainty are pointed out, focusing on recent developments in our understanding of their roles.</p></div><div type="abstract" xml:lang="en"><p><b>CRITICAL ISSUES</b></p><p>The areas of particular focus are on the multiple, overlapping roles of mitochondrial thiols and on understanding how these thiols contribute to both antioxidant defenses and redox signaling.</p></div><div type="abstract" xml:lang="en"><p><b>FUTURE DIRECTIONS</b></p><p>Recent technical progress in the identification and quantification of thiol modifications by redox proteomics means that many of the questions raised about the multiple roles of mitochondrial thiols can now be addressed.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21954972</PMID><DateCompleted><Year>2012</Year><Month>09</Month><Day>17</Day></DateCompleted><DateRevised><Year>2017</Year><Month>09</Month><Day>22</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1557-7716</ISSN><JournalIssue CitedMedium="Internet"><Volume>16</Volume><Issue>6</Issue><PubDate><Year>2012</Year><Month>Mar</Month><Day>15</Day></PubDate></JournalIssue><Title>Antioxidants & redox signaling</Title><ISOAbbreviation>Antioxid Redox Signal</ISOAbbreviation></Journal><ArticleTitle>Mitochondrial thiols in antioxidant protection and redox signaling: distinct roles for glutathionylation and other thiol modifications.</ArticleTitle><Pagination><MedlinePgn>476-95</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1089/ars.2011.4289</ELocationID><Abstract><AbstractText Label="SIGNIFICANCE" NlmCategory="CONCLUSIONS">The mitochondrial matrix contains much of the machinery at the heart of metabolism. This compartment is also exposed to a high and continual flux of superoxide, hydrogen peroxide, and related reactive species. To protect mitochondria from these sources of oxidative damage, there is an integrated set of thiol systems within the matrix comprising the thioredoxin/peroxiredoxin/methionine sulfoxide reductase pathways and the glutathione/glutathione peroxidase/glutathione-S-transferase/glutaredoxin pathways that in conjunction with protein thiols prevent much of this oxidative damage. In addition, the changes in the redox state of many components of these mitochondrial thiol systems may transduce and relay redox signals within and through the mitochondrial matrix to modulate the activity of biochemical processes.</AbstractText><AbstractText Label="RECENT ADVANCES" NlmCategory="BACKGROUND">Here, mitochondrial thiol systems are reviewed, and areas of uncertainty are pointed out, focusing on recent developments in our understanding of their roles.</AbstractText><AbstractText Label="CRITICAL ISSUES" NlmCategory="RESULTS">The areas of particular focus are on the multiple, overlapping roles of mitochondrial thiols and on understanding how these thiols contribute to both antioxidant defenses and redox signaling.</AbstractText><AbstractText Label="FUTURE DIRECTIONS" NlmCategory="CONCLUSIONS">Recent technical progress in the identification and quantification of thiol modifications by redox proteomics means that many of the questions raised about the multiple roles of mitochondrial thiols can now be addressed.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Murphy</LastName><ForeName>Michael P</ForeName><Initials>MP</Initials><AffiliationInfo><Affiliation>MRC Mitochondrial Biology Unit, Cambridge, United Kingdom. mpm@mrc-mbu.cam.ac.uk</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>MC_U105663142</GrantID><Agency>Medical Research Council</Agency><Country>United Kingdom</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2011</Year><Month>12</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Antioxid Redox Signal</MedlineTA><NlmUniqueID>100888899</NlmUniqueID><ISSNLinking>1523-0864</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000975">Antioxidants</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="D000975" MajorTopicYN="N">Antioxidants</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></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="D008928" MajorTopicYN="N">Mitochondria</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="Y">Signal Transduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2011</Year><Month>9</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>10</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2012</Year><Month>9</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">21954972</ArticleId><ArticleId IdType="doi">10.1089/ars.2011.4289</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Royaume-Uni</li></country></list><tree><country name="Royaume-Uni"><noRegion><name sortKey="Murphy, Michael P" sort="Murphy, Michael P" uniqKey="Murphy M" first="Michael P" last="Murphy">Michael P. 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