GlutaredoxinV1, Main, Exploration, bibRecord, 000361

Glutaredoxin-1 Deficiency Causes Fatty Liver and Dyslipidemia by Inhibiting Sirtuin-1.

Identifieur interne : 000361 ( Main/Exploration ); précédent : 000360; suivant : 000362

Glutaredoxin-1 Deficiency Causes Fatty Liver and Dyslipidemia by Inhibiting Sirtuin-1.

Auteurs : Di Shao [États-Unis] ; Jingyan Han [États-Unis] ; Xiuyun Hou [États-Unis] ; Jessica Fry [États-Unis] ; Jessica B. Behring [États-Unis] ; Francesca Seta [États-Unis] ; Michelle T. Long [États-Unis] ; Hemant K. Roy [États-Unis] ; Richard A. Cohen [États-Unis] ; Reiko Matsui [États-Unis] ; Markus M. Bachschmid [États-Unis]

Source :

Antioxidants & redox signaling [ 1557-7716 ] ; 2017.

RBID : pubmed:27958883

Descripteurs français

English descriptors

KwdEn :
- Acetylation (MeSH), Animals (MeSH), Disease Models, Animal (MeSH), Dyslipidemias (genetics), Dyslipidemias (metabolism), Dyslipidemias (pathology), Fatty Liver (genetics), Fatty Liver (metabolism), Fatty Liver (pathology), Gene Knockout Techniques (MeSH), Glutaredoxins (genetics), Glutathione (metabolism), Hep G2 Cells (MeSH), Humans (MeSH), Lipid Metabolism (MeSH), Mice (MeSH), Obesity (genetics), Obesity (metabolism), Sirtuin 1 (metabolism), Sterol Regulatory Element Binding Protein 1 (metabolism), Up-Regulation (MeSH).
MESH :
- chemical , genetics : Glutaredoxins.
- genetics : Dyslipidemias, Fatty Liver, Obesity.
- metabolism : Dyslipidemias, Fatty Liver, Glutathione, Obesity, Sirtuin 1, Sterol Regulatory Element Binding Protein 1.
- pathology : Dyslipidemias, Fatty Liver.
- Acetylation, Animals, Disease Models, Animal, Gene Knockout Techniques, Hep G2 Cells, Humans, Lipid Metabolism, Mice, Up-Regulation.

Abstract

AIMS

Nonalcoholic fatty liver (NAFL) is a common liver disease associated with metabolic syndrome, obesity, and diabetes that is rising in prevalence worldwide. Various molecular perturbations of key regulators and enzymes in hepatic lipid metabolism cause NAFL. However, redox regulation through glutathione (GSH) adducts in NAFL remains largely elusive. Glutaredoxin-1 (Glrx) is a small thioltransferase that removes protein GSH adducts without having direct antioxidant properties. The liver contains abundant Glrx but its metabolic function is unknown.

RESULTS

Here we report that normal diet-fed Glrx-deficient mice (Glrx

INNOVATION

These data suggest an essential role of hepatic Glrx in regulating SirT1, which controls protein glutathione adducts in the pathogenesis of hepatic steatosis.

CONCLUSION

We provide a novel redox-dependent mechanism for regulation of hepatic lipid metabolism, and propose that upregulation of hepatic Glrx may be a beneficial strategy for NAFL. Antioxid. Redox Signal. 27, 313-327.

DOI: 10.1089/ars.2016.6716
PubMed: 27958883
PubMed Central: PMC5563925

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acetylation (MeSH)</term>
<term>Animals (MeSH)</term>
<term>Disease Models, Animal (MeSH)</term>
<term>Dyslipidemias (genetics)</term>
<term>Dyslipidemias (metabolism)</term>
<term>Dyslipidemias (pathology)</term>
<term>Fatty Liver (genetics)</term>
<term>Fatty Liver (metabolism)</term>
<term>Fatty Liver (pathology)</term>
<term>Gene Knockout Techniques (MeSH)</term>
<term>Glutaredoxins (genetics)</term>
<term>Glutathione (metabolism)</term>
<term>Hep G2 Cells (MeSH)</term>
<term>Humans (MeSH)</term>
<term>Lipid Metabolism (MeSH)</term>
<term>Mice (MeSH)</term>
<term>Obesity (genetics)</term>
<term>Obesity (metabolism)</term>
<term>Sirtuin 1 (metabolism)</term>
<term>Sterol Regulatory Element Binding Protein 1 (metabolism)</term>
<term>Up-Regulation (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Acétylation (MeSH)</term>
<term>Animaux (MeSH)</term>
<term>Cellules HepG2 (MeSH)</term>
<term>Dyslipidémies (anatomopathologie)</term>
<term>Dyslipidémies (génétique)</term>
<term>Dyslipidémies (métabolisme)</term>
<term>Glutarédoxines (génétique)</term>
<term>Glutathion (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Modèles animaux de maladie humaine (MeSH)</term>
<term>Métabolisme lipidique (MeSH)</term>
<term>Obésité (génétique)</term>
<term>Obésité (métabolisme)</term>
<term>Protéine-1 de liaison à l'élément de régulation des stérols (métabolisme)</term>
<term>Régulation positive (MeSH)</term>
<term>Sirtuine-1 (métabolisme)</term>
<term>Souris (MeSH)</term>
<term>Stéatose hépatique (anatomopathologie)</term>
<term>Stéatose hépatique (génétique)</term>
<term>Stéatose hépatique (métabolisme)</term>
<term>Techniques de knock-out de gènes (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term>
</keywords>
<keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Dyslipidémies</term>
<term>Stéatose hépatique</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Dyslipidemias</term>
<term>Fatty Liver</term>
<term>Obesity</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Dyslipidémies</term>
<term>Glutarédoxines</term>
<term>Obésité</term>
<term>Stéatose hépatique</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Dyslipidemias</term>
<term>Fatty Liver</term>
<term>Glutathione</term>
<term>Obesity</term>
<term>Sirtuin 1</term>
<term>Sterol Regulatory Element Binding Protein 1</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Dyslipidémies</term>
<term>Glutathion</term>
<term>Obésité</term>
<term>Protéine-1 de liaison à l'élément de régulation des stérols</term>
<term>Sirtuine-1</term>
<term>Stéatose hépatique</term>
</keywords>
<keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Dyslipidemias</term>
<term>Fatty Liver</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Acetylation</term>
<term>Animals</term>
<term>Disease Models, Animal</term>
<term>Gene Knockout Techniques</term>
<term>Hep G2 Cells</term>
<term>Humans</term>
<term>Lipid Metabolism</term>
<term>Mice</term>
<term>Up-Regulation</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Acétylation</term>
<term>Animaux</term>
<term>Cellules HepG2</term>
<term>Humains</term>
<term>Modèles animaux de maladie humaine</term>
<term>Métabolisme lipidique</term>
<term>Régulation positive</term>
<term>Souris</term>
<term>Techniques de knock-out de gènes</term>
</keywords>
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<front><div type="abstract" xml:lang="en"><p><b>AIMS</b>
</p>
<p>Nonalcoholic fatty liver (NAFL) is a common liver disease associated with metabolic syndrome, obesity, and diabetes that is rising in prevalence worldwide. Various molecular perturbations of key regulators and enzymes in hepatic lipid metabolism cause NAFL. However, redox regulation through glutathione (GSH) adducts in NAFL remains largely elusive. Glutaredoxin-1 (Glrx) is a small thioltransferase that removes protein GSH adducts without having direct antioxidant properties. The liver contains abundant Glrx but its metabolic function is unknown.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>RESULTS</b>
</p>
<p>Here we report that normal diet-fed Glrx-deficient mice (Glrx</p>
</div>
<div type="abstract" xml:lang="en"><p><b>INNOVATION</b>
</p>
<p>These data suggest an essential role of hepatic Glrx in regulating SirT1, which controls protein glutathione adducts in the pathogenesis of hepatic steatosis.</p>
</div>
<div type="abstract" xml:lang="en"><p><b>CONCLUSION</b>
</p>
<p>We provide a novel redox-dependent mechanism for regulation of hepatic lipid metabolism, and propose that upregulation of hepatic Glrx may be a beneficial strategy for NAFL. Antioxid. Redox Signal. 27, 313-327.</p>
</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27958883</PMID>
<DateCompleted><Year>2018</Year>
<Month>02</Month>
<Day>28</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>05</Month>
<Day>08</Day>
</DateRevised>
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<JournalIssue CitedMedium="Internet"><Volume>27</Volume>
<Issue>6</Issue>
<PubDate><Year>2017</Year>
<Month>08</Month>
<Day>20</Day>
</PubDate>
</JournalIssue>
<Title>Antioxidants & redox signaling</Title>
<ISOAbbreviation>Antioxid Redox Signal</ISOAbbreviation>
</Journal>
<ArticleTitle>Glutaredoxin-1 Deficiency Causes Fatty Liver and Dyslipidemia by Inhibiting Sirtuin-1.</ArticleTitle>
<Pagination><MedlinePgn>313-327</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1089/ars.2016.6716</ELocationID>
<Abstract><AbstractText Label="AIMS">Nonalcoholic fatty liver (NAFL) is a common liver disease associated with metabolic syndrome, obesity, and diabetes that is rising in prevalence worldwide. Various molecular perturbations of key regulators and enzymes in hepatic lipid metabolism cause NAFL. However, redox regulation through glutathione (GSH) adducts in NAFL remains largely elusive. Glutaredoxin-1 (Glrx) is a small thioltransferase that removes protein GSH adducts without having direct antioxidant properties. The liver contains abundant Glrx but its metabolic function is unknown.</AbstractText>
<AbstractText Label="RESULTS">Here we report that normal diet-fed Glrx-deficient mice (Glrx<sup>-/-</sup>
) spontaneously develop obesity, hyperlipidemia, and hepatic steatosis by 8 months of age. Adenoviral Glrx repletion in the liver of Glrx<sup>-/-</sup>
 mice corrected lipid metabolism. Glrx<sup>-/-</sup>
 mice exhibited decreased sirtuin-1 (SirT1) activity that leads to hyperacetylation and activation of SREBP-1 and upregulation of key hepatic enzymes involved in lipid synthesis. We found that GSH adducts inhibited SirT1 activity in Glrx<sup>-/-</sup>
 mice. Hepatic expression of nonoxidizable cysteine mutant SirT1 corrected hepatic lipids in Glrx<sup>-/-</sup>
 mice. Wild-type mice fed high-fat diet develop metabolic syndrome, diabetes, and NAFL within several months. Glrx deficiency accelerated high-fat-induced NAFL and progression to steatohepatitis, manifested by hepatic damage and inflammation.</AbstractText>
<AbstractText Label="INNOVATION">These data suggest an essential role of hepatic Glrx in regulating SirT1, which controls protein glutathione adducts in the pathogenesis of hepatic steatosis.</AbstractText>
<AbstractText Label="CONCLUSION">We provide a novel redox-dependent mechanism for regulation of hepatic lipid metabolism, and propose that upregulation of hepatic Glrx may be a beneficial strategy for NAFL. Antioxid. Redox Signal. 27, 313-327.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shao</LastName>
<ForeName>Di</ForeName>
<Initials>D</Initials>
<AffiliationInfo><Affiliation>1 Vascular Biology Section, Whitaker Cardiovascular Institute, Boston University School of Medicine , Boston, Massachusetts.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Han</LastName>
<ForeName>Jingyan</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>1 Vascular Biology Section, Whitaker Cardiovascular Institute, Boston University School of Medicine , Boston, Massachusetts.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Hou</LastName>
<ForeName>Xiuyun</ForeName>
<Initials>X</Initials>
<AffiliationInfo><Affiliation>1 Vascular Biology Section, Whitaker Cardiovascular Institute, Boston University School of Medicine , Boston, Massachusetts.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Fry</LastName>
<ForeName>Jessica</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>1 Vascular Biology Section, Whitaker Cardiovascular Institute, Boston University School of Medicine , Boston, Massachusetts.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Behring</LastName>
<ForeName>Jessica B</ForeName>
<Initials>JB</Initials>
<AffiliationInfo><Affiliation>1 Vascular Biology Section, Whitaker Cardiovascular Institute, Boston University School of Medicine , Boston, Massachusetts.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Seta</LastName>
<ForeName>Francesca</ForeName>
<Initials>F</Initials>
<AffiliationInfo><Affiliation>1 Vascular Biology Section, Whitaker Cardiovascular Institute, Boston University School of Medicine , Boston, Massachusetts.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Long</LastName>
<ForeName>Michelle T</ForeName>
<Initials>MT</Initials>
<AffiliationInfo><Affiliation>3 Division of Gastroenterology, Boston Medical Center , Boston, Massachusetts.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Roy</LastName>
<ForeName>Hemant K</ForeName>
<Initials>HK</Initials>
<AffiliationInfo><Affiliation>3 Division of Gastroenterology, Boston Medical Center , Boston, Massachusetts.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Cohen</LastName>
<ForeName>Richard A</ForeName>
<Initials>RA</Initials>
<AffiliationInfo><Affiliation>1 Vascular Biology Section, Whitaker Cardiovascular Institute, Boston University School of Medicine , Boston, Massachusetts.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>2 Cardiovascular Proteomics Center, Boston University School of Medicine , Boston, Massachusetts.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Matsui</LastName>
<ForeName>Reiko</ForeName>
<Initials>R</Initials>
<AffiliationInfo><Affiliation>1 Vascular Biology Section, Whitaker Cardiovascular Institute, Boston University School of Medicine , Boston, Massachusetts.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Bachschmid</LastName>
<ForeName>Markus M</ForeName>
<Initials>MM</Initials>
<AffiliationInfo><Affiliation>1 Vascular Biology Section, Whitaker Cardiovascular Institute, Boston University School of Medicine , Boston, Massachusetts.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>2 Cardiovascular Proteomics Center, Boston University School of Medicine , Boston, Massachusetts.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>HHSN268201000031C</GrantID>
<Acronym>HL</Acronym>
<Agency>NHLBI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>T32 HL007024</GrantID>
<Acronym>HL</Acronym>
<Agency>NHLBI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>UL1 TR001430</GrantID>
<Acronym>TR</Acronym>
<Agency>NCATS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R37 HL104017</GrantID>
<Acronym>HL</Acronym>
<Agency>NHLBI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R01 DK076942</GrantID>
<Acronym>DK</Acronym>
<Agency>NIDDK NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R01 HL133013</GrantID>
<Acronym>HL</Acronym>
<Agency>NHLBI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>P01 HL068758</GrantID>
<Acronym>HL</Acronym>
<Agency>NHLBI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>T32 HL007501</GrantID>
<Acronym>HL</Acronym>
<Agency>NHLBI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R01 DK103750</GrantID>
<Acronym>DK</Acronym>
<Agency>NIDDK NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R01 HL115955</GrantID>
<Acronym>HL</Acronym>
<Agency>NHLBI 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="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2017</Year>
<Month>02</Month>
<Day>16</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="C516006">Glrx protein, mouse</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C497388">Srebf1 protein, mouse</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D051780">Sterol Regulatory Element Binding Protein 1</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.5.1.-</RegistryNumber>
<NameOfSubstance UI="C470545">Sirt1 protein, mouse</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.5.1.-</RegistryNumber>
<NameOfSubstance UI="D056564">Sirtuin 1</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber>
<NameOfSubstance UI="D005978">Glutathione</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000107" MajorTopicYN="N">Acetylation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004195" MajorTopicYN="N">Disease Models, Animal</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D050171" MajorTopicYN="N">Dyslipidemias</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000473" MajorTopicYN="Y">pathology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005234" MajorTopicYN="N">Fatty Liver</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000473" MajorTopicYN="Y">pathology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D055786" MajorTopicYN="N">Gene Knockout Techniques</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D056945" MajorTopicYN="N">Hep G2 Cells</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D050356" MajorTopicYN="N">Lipid Metabolism</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009765" MajorTopicYN="N">Obesity</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D056564" MajorTopicYN="N">Sirtuin 1</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051780" MajorTopicYN="N">Sterol Regulatory Element Binding Protein 1</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015854" MajorTopicYN="N">Up-Regulation</DescriptorName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">glutaredoxin</Keyword>
<Keyword MajorTopicYN="Y">glutathione</Keyword>
<Keyword MajorTopicYN="Y">lipids</Keyword>
<Keyword MajorTopicYN="Y">sirtuin</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2016</Year>
<Month>12</Month>
<Day>14</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2018</Year>
<Month>3</Month>
<Day>1</Day>
<Hour>6</Hour>
<Minute>0</Minute>
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<PubMedPubDate PubStatus="entrez"><Year>2016</Year>
<Month>12</Month>
<Day>14</Day>
<Hour>6</Hour>
<Minute>0</Minute>
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</History>
<PublicationStatus>ppublish</PublicationStatus>
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Glutaredoxin-1 Deficiency Causes Fatty Liver and Dyslipidemia by Inhibiting Sirtuin-1.

Glutaredoxin-1 Deficiency Causes Fatty Liver and Dyslipidemia by Inhibiting Sirtuin-1.

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