Glutathione, Glutaredoxins, and Iron.
Identifieur interne : 000359 ( Main/Exploration ); précédent : 000358; suivant : 000360Glutathione, Glutaredoxins, and Iron.
Auteurs : Carsten Berndt [Allemagne] ; Christopher Horst Lillig [Allemagne]Source :
- Antioxidants & redox signaling [ 1557-7716 ] ; 2017.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Glutarédoxines.
- métabolisme : Fer, Glutarédoxines, Glutathion.
- Animaux, Domaine catalytique, Homéostasie, Humains, Modèles moléculaires, Oxydoréduction.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Glutaredoxins.
- chemical , metabolism : Glutaredoxins, Glutathione, Iron.
- Animals, Catalytic Domain, Homeostasis, Humans, Models, Molecular, Oxidation-Reduction.
Abstract
SIGNIFICANCE
Glutathione (GSH) is the most abundant cellular low-molecular-weight thiol in the majority of organisms in all kingdoms of life. Therefore, functions of GSH and disturbed regulation of its concentration are associated with numerous physiological and pathological situations. Recent Advances: The function of GSH as redox buffer or antioxidant is increasingly being questioned. New functions, especially functions connected to the cellular iron homeostasis, were elucidated. Via the formation of iron complexes, GSH is an important player in all aspects of iron metabolism: sensing and regulation of iron levels, iron trafficking, and biosynthesis of iron cofactors. The variety of GSH coordinated iron complexes and their functions with a special focus on FeS-glutaredoxins are summarized in this review. Interestingly, GSH analogues that function as major low-molecular-weight thiols in organisms lacking GSH resemble the functions in iron homeostasis.
CRITICAL ISSUES
Since these iron-related functions are most likely also connected to thiol redox chemistry, it is difficult to distinguish between mechanisms related to either redox or iron metabolisms.
FUTURE DIRECTIONS
The ability of GSH to coordinate iron in different complexes with or without proteins needs further investigation. The discovery of new Fe-GSH complexes and their physiological functions will significantly advance our understanding of cellular iron homeostasis. Antioxid. Redox Signal. 27, 1235-1251.
DOI: 10.1089/ars.2017.7132
PubMed: 28537421
Affiliations:
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Lillig</name><affiliation wicri:level="1"><nlm:affiliation>2 Institute for Medical Biochemistry and Molecular Biology, University Medicine Greifswald , Greifswald, Germany .</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>2 Institute for Medical Biochemistry and Molecular Biology, University Medicine Greifswald , Greifswald</wicri:regionArea><wicri:noRegion>Greifswald</wicri:noRegion><wicri:noRegion>Greifswald</wicri:noRegion><wicri:noRegion>Greifswald</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2017">2017</date><idno type="RBID">pubmed:28537421</idno><idno type="pmid">28537421</idno><idno type="doi">10.1089/ars.2017.7132</idno><idno type="wicri:Area/Main/Corpus">000341</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000341</idno><idno type="wicri:Area/Main/Curation">000341</idno><idno type="wicri:explorRef" wicri:stream="Main" 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Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name><affiliation wicri:level="1"><nlm:affiliation>2 Institute for Medical Biochemistry and Molecular Biology, University Medicine Greifswald , Greifswald, Germany .</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>2 Institute for Medical Biochemistry and Molecular Biology, University Medicine Greifswald , Greifswald</wicri:regionArea><wicri:noRegion>Greifswald</wicri:noRegion><wicri:noRegion>Greifswald</wicri:noRegion><wicri:noRegion>Greifswald</wicri:noRegion></affiliation></author></analytic><series><title level="j">Antioxidants & redox signaling</title><idno type="eISSN">1557-7716</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Catalytic Domain (MeSH)</term><term>Glutaredoxins (chemistry)</term><term>Glutaredoxins (metabolism)</term><term>Glutathione (metabolism)</term><term>Homeostasis (MeSH)</term><term>Humans (MeSH)</term><term>Iron (metabolism)</term><term>Models, Molecular (MeSH)</term><term>Oxidation-Reduction (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Domaine catalytique (MeSH)</term><term>Fer (métabolisme)</term><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathion (métabolisme)</term><term>Homéostasie (MeSH)</term><term>Humains (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Oxydoréduction (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term><term>Glutathione</term><term>Iron</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutarédoxines</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Fer</term><term>Glutarédoxines</term><term>Glutathion</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Catalytic Domain</term><term>Homeostasis</term><term>Humans</term><term>Models, Molecular</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Domaine catalytique</term><term>Homéostasie</term><term>Humains</term><term>Modèles moléculaires</term><term>Oxydoréduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>SIGNIFICANCE</b></p><p>Glutathione (GSH) is the most abundant cellular low-molecular-weight thiol in the majority of organisms in all kingdoms of life. Therefore, functions of GSH and disturbed regulation of its concentration are associated with numerous physiological and pathological situations. Recent Advances: The function of GSH as redox buffer or antioxidant is increasingly being questioned. New functions, especially functions connected to the cellular iron homeostasis, were elucidated. Via the formation of iron complexes, GSH is an important player in all aspects of iron metabolism: sensing and regulation of iron levels, iron trafficking, and biosynthesis of iron cofactors. The variety of GSH coordinated iron complexes and their functions with a special focus on FeS-glutaredoxins are summarized in this review. Interestingly, GSH analogues that function as major low-molecular-weight thiols in organisms lacking GSH resemble the functions in iron homeostasis.</p></div><div type="abstract" xml:lang="en"><p><b>CRITICAL ISSUES</b></p><p>Since these iron-related functions are most likely also connected to thiol redox chemistry, it is difficult to distinguish between mechanisms related to either redox or iron metabolisms.</p></div><div type="abstract" xml:lang="en"><p><b>FUTURE DIRECTIONS</b></p><p>The ability of GSH to coordinate iron in different complexes with or without proteins needs further investigation. The discovery of new Fe-GSH complexes and their physiological functions will significantly advance our understanding of cellular iron homeostasis. Antioxid. Redox Signal. 27, 1235-1251.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28537421</PMID><DateCompleted><Year>2018</Year><Month>03</Month><Day>09</Day></DateCompleted><DateRevised><Year>2018</Year><Month>03</Month><Day>09</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1557-7716</ISSN><JournalIssue CitedMedium="Internet"><Volume>27</Volume><Issue>15</Issue><PubDate><Year>2017</Year><Month>Nov</Month><Day>20</Day></PubDate></JournalIssue><Title>Antioxidants & redox signaling</Title><ISOAbbreviation>Antioxid Redox Signal</ISOAbbreviation></Journal><ArticleTitle>Glutathione, Glutaredoxins, and Iron.</ArticleTitle><Pagination><MedlinePgn>1235-1251</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1089/ars.2017.7132</ELocationID><Abstract><AbstractText Label="SIGNIFICANCE" NlmCategory="CONCLUSIONS">Glutathione (GSH) is the most abundant cellular low-molecular-weight thiol in the majority of organisms in all kingdoms of life. Therefore, functions of GSH and disturbed regulation of its concentration are associated with numerous physiological and pathological situations. Recent Advances: The function of GSH as redox buffer or antioxidant is increasingly being questioned. New functions, especially functions connected to the cellular iron homeostasis, were elucidated. Via the formation of iron complexes, GSH is an important player in all aspects of iron metabolism: sensing and regulation of iron levels, iron trafficking, and biosynthesis of iron cofactors. The variety of GSH coordinated iron complexes and their functions with a special focus on FeS-glutaredoxins are summarized in this review. Interestingly, GSH analogues that function as major low-molecular-weight thiols in organisms lacking GSH resemble the functions in iron homeostasis.</AbstractText><AbstractText Label="CRITICAL ISSUES" NlmCategory="RESULTS">Since these iron-related functions are most likely also connected to thiol redox chemistry, it is difficult to distinguish between mechanisms related to either redox or iron metabolisms.</AbstractText><AbstractText Label="FUTURE DIRECTIONS" NlmCategory="CONCLUSIONS">The ability of GSH to coordinate iron in different complexes with or without proteins needs further investigation. The discovery of new Fe-GSH complexes and their physiological functions will significantly advance our understanding of cellular iron homeostasis. Antioxid. Redox Signal. 27, 1235-1251.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Berndt</LastName><ForeName>Carsten</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>1 Department of Neurology, Medical Faculty, Life Science Center , Heinrich-Heine-Universität, Düsseldorf, Germany .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lillig</LastName><ForeName>Christopher Horst</ForeName><Initials>CH</Initials><AffiliationInfo><Affiliation>2 Institute for Medical Biochemistry and Molecular Biology, University Medicine Greifswald , Greifswald, Germany .</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>06</Month><Day>26</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="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>E1UOL152H7</RegistryNumber><NameOfSubstance UI="D007501">Iron</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="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">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="D006706" MajorTopicYN="N">Homeostasis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Parkinson's disease</Keyword><Keyword MajorTopicYN="N">anemia</Keyword><Keyword MajorTopicYN="N">iron–sulfur</Keyword><Keyword MajorTopicYN="N">redox regulation</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>5</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2018</Year><Month>3</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>5</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">28537421</ArticleId><ArticleId IdType="doi">10.1089/ars.2017.7132</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country><region><li>District de Düsseldorf</li><li>Rhénanie-du-Nord-Westphalie</li></region><settlement><li>Düsseldorf</li></settlement></list><tree><country name="Allemagne"><region name="Rhénanie-du-Nord-Westphalie"><name sortKey="Berndt, Carsten" sort="Berndt, Carsten" uniqKey="Berndt C" first="Carsten" last="Berndt">Carsten Berndt</name></region><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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