What is the functional significance of the unique location of glutaredoxin 1 (GRx1) in the intermembrane space of mitochondria?
Identifieur interne : 000C37 ( Main/Exploration ); précédent : 000C36; suivant : 000C38What is the functional significance of the unique location of glutaredoxin 1 (GRx1) in the intermembrane space of mitochondria?
Auteurs : Harish V. Pai [États-Unis] ; David W. Starke ; Edward J. Lesnefsky ; Charles L. Hoppel ; John J. MieyalSource :
- Antioxidants & redox signaling [ 1523-0864 ] ; 2007.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Citrate (si)-synthase (métabolisme), Complexe IV de la chaîne respiratoire (métabolisme), Fractions subcellulaires (métabolisme), Glutarédoxines (métabolisme), Isoformes de protéines (génétique), Isoformes de protéines (métabolisme), Membranes mitochondriales (métabolisme), Mitochondries du foie (composition chimique), Mitochondries du foie (enzymologie), Mitochondries du myocarde (composition chimique), Mitochondries du myocarde (enzymologie), Mâle (MeSH), Phosphorylation oxydative (MeSH), Protéine Bid (métabolisme), Rat Sprague-Dawley (MeSH), Rats (MeSH), Rats de lignée F344 (MeSH).
- MESH :
- composition chimique : Mitochondries du foie, Mitochondries du myocarde.
- enzymologie : Mitochondries du foie, Mitochondries du myocarde.
- génétique : Isoformes de protéines.
- métabolisme : Citrate (si)-synthase, Complexe IV de la chaîne respiratoire, Fractions subcellulaires, Glutarédoxines, Isoformes de protéines, Membranes mitochondriales, Protéine Bid.
- Animaux, Mâle, Phosphorylation oxydative, Rat Sprague-Dawley, Rats, Rats de lignée F344.
English descriptors
- KwdEn :
- Animals (MeSH), BH3 Interacting Domain Death Agonist Protein (metabolism), Citrate (si)-Synthase (metabolism), Electron Transport Complex IV (metabolism), Glutaredoxins (metabolism), Male (MeSH), Mitochondria, Heart (chemistry), Mitochondria, Heart (enzymology), Mitochondria, Liver (chemistry), Mitochondria, Liver (enzymology), Mitochondrial Membranes (metabolism), Oxidative Phosphorylation (MeSH), Protein Isoforms (genetics), Protein Isoforms (metabolism), Rats (MeSH), Rats, Inbred F344 (MeSH), Rats, Sprague-Dawley (MeSH), Subcellular Fractions (metabolism).
- MESH :
- chemical , genetics : Protein Isoforms.
- chemical , metabolism : BH3 Interacting Domain Death Agonist Protein, Citrate (si)-Synthase, Electron Transport Complex IV, Glutaredoxins, Protein Isoforms.
- chemistry : Mitochondria, Heart, Mitochondria, Liver.
- enzymology : Mitochondria, Heart, Mitochondria, Liver.
- metabolism : Mitochondrial Membranes, Subcellular Fractions.
- Animals, Male, Oxidative Phosphorylation, Rats, Rats, Inbred F344, Rats, Sprague-Dawley.
Abstract
Glutaredoxins (GRx) catalyze reversible protein glutathionylation. They are implicated in sulfhydryl homeostasis and regulation of redox signal transduction, controlling various cellular processes like DNA synthesis, defense against oxidative stress, apoptosis signaling, and DNA-binding of transcription factors. Two isoforms of GRx are well characterized in mammals: GRx1, the "cytosolic" form, and GRx2, the "mitochondrial" form. Here we report documentation of GRx1 in mitochondria, localized exclusively in the intermembrane space and segregated from GRx2, localized exclusively in the mitochondrial matrix. We hypothesize that GRx1 and GRx2 in their unique locations regulate different functions of the mitochondria via reversible S-glutathionylation.
DOI: 10.1089/ars.2007.1642
PubMed: 17845131
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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They are implicated in sulfhydryl homeostasis and regulation of redox signal transduction, controlling various cellular processes like DNA synthesis, defense against oxidative stress, apoptosis signaling, and DNA-binding of transcription factors. Two isoforms of GRx are well characterized in mammals: GRx1, the "cytosolic" form, and GRx2, the "mitochondrial" form. Here we report documentation of GRx1 in mitochondria, localized exclusively in the intermembrane space and segregated from GRx2, localized exclusively in the mitochondrial matrix. We hypothesize that GRx1 and GRx2 in their unique locations regulate different functions of the mitochondria via reversible S-glutathionylation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17845131</PMID><DateCompleted><Year>2007</Year><Month>12</Month><Day>07</Day></DateCompleted><DateRevised><Year>2020</Year><Month>02</Month><Day>04</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1523-0864</ISSN><JournalIssue CitedMedium="Print"><Volume>9</Volume><Issue>11</Issue><PubDate><Year>2007</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Antioxidants & redox signaling</Title><ISOAbbreviation>Antioxid Redox Signal</ISOAbbreviation></Journal><ArticleTitle>What is the functional significance of the unique location of glutaredoxin 1 (GRx1) in the intermembrane space of mitochondria?</ArticleTitle><Pagination><MedlinePgn>2027-33</MedlinePgn></Pagination><Abstract><AbstractText>Glutaredoxins (GRx) catalyze reversible protein glutathionylation. They are implicated in sulfhydryl homeostasis and regulation of redox signal transduction, controlling various cellular processes like DNA synthesis, defense against oxidative stress, apoptosis signaling, and DNA-binding of transcription factors. Two isoforms of GRx are well characterized in mammals: GRx1, the "cytosolic" form, and GRx2, the "mitochondrial" form. Here we report documentation of GRx1 in mitochondria, localized exclusively in the intermembrane space and segregated from GRx2, localized exclusively in the mitochondrial matrix. We hypothesize that GRx1 and GRx2 in their unique locations regulate different functions of the mitochondria via reversible S-glutathionylation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Pai</LastName><ForeName>Harish V</ForeName><Initials>HV</Initials><AffiliationInfo><Affiliation>Department of Pharmacology, Case Western Reserve University, Cleveland, Ohio.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Starke</LastName><ForeName>David W</ForeName><Initials>DW</Initials></Author><Author ValidYN="Y"><LastName>Lesnefsky</LastName><ForeName>Edward J</ForeName><Initials>EJ</Initials></Author><Author ValidYN="Y"><LastName>Hoppel</LastName><ForeName>Charles L</ForeName><Initials>CL</Initials></Author><Author ValidYN="Y"><LastName>Mieyal</LastName><ForeName>John J</ForeName><Initials>JJ</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>1 RO1 AG024413</GrantID><Acronym>AG</Acronym><Agency>NIA NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>2 PO1 AG 15885</GrantID><Acronym>AG</Acronym><Agency>NIA NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></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="D051023">BH3 Interacting Domain Death Agonist Protein</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C516007">Glrx protein, rat</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020033">Protein Isoforms</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.9.3.1</RegistryNumber><NameOfSubstance UI="D003576">Electron Transport Complex IV</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.3.3.1</RegistryNumber><NameOfSubstance UI="D002950">Citrate (si)-Synthase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051023" MajorTopicYN="N">BH3 Interacting Domain Death Agonist Protein</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002950" MajorTopicYN="N">Citrate 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MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051336" MajorTopicYN="N">Mitochondrial Membranes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010085" MajorTopicYN="N">Oxidative Phosphorylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020033" MajorTopicYN="N">Protein Isoforms</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011916" MajorTopicYN="N">Rats, Inbred F344</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017207" MajorTopicYN="N">Rats, Sprague-Dawley</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013347" MajorTopicYN="N">Subcellular Fractions</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>9</Month><Day>12</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>12</Month><Day>8</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>9</Month><Day>12</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17845131</ArticleId><ArticleId IdType="doi">10.1089/ars.2007.1642</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Ohio</li></region></list><tree><noCountry><name sortKey="Hoppel, Charles L" sort="Hoppel, Charles L" uniqKey="Hoppel C" first="Charles L" last="Hoppel">Charles L. Hoppel</name><name sortKey="Lesnefsky, Edward J" sort="Lesnefsky, Edward J" uniqKey="Lesnefsky E" first="Edward J" last="Lesnefsky">Edward J. Lesnefsky</name><name sortKey="Mieyal, John J" sort="Mieyal, John J" uniqKey="Mieyal J" first="John J" last="Mieyal">John J. Mieyal</name><name sortKey="Starke, David W" sort="Starke, David W" uniqKey="Starke D" first="David W" last="Starke">David W. Starke</name></noCountry><country name="États-Unis"><region name="Ohio"><name sortKey="Pai, Harish V" sort="Pai, Harish V" uniqKey="Pai H" first="Harish V" last="Pai">Harish V. Pai</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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