Protein S-glutathionylation stimulate adipogenesis by stabilizing C/EBPβ in 3T3L1 cells.
Identifieur interne : 000032 ( Main/Exploration ); précédent : 000031; suivant : 000033Protein S-glutathionylation stimulate adipogenesis by stabilizing C/EBPβ in 3T3L1 cells.
Auteurs : Yosuke Watanabe [Japon] ; Kazuhiro Watanabe [Japon] ; Daisuke Fujioka [Japon] ; Kazuto Nakamura [Japon] ; Takamitsu Nakamura [Japon] ; Manabu Uematsu [Japon] ; Markus M. Bachschmid [États-Unis] ; Reiko Matsui [États-Unis] ; Kiyotaka Kugiyama [Japon]Source :
- FASEB journal : official publication of the Federation of American Societies for Experimental Biology [ 1530-6860 ] ; 2020.
Abstract
Reactive oxygen species (ROS) increase during adipogenesis and in obesity. Oxidants react with cysteine residues of proteins to form glutathione (GSH) adducts, S-glutathionylation, that are selectively removed by glutaredoxin-1 (Glrx). We have previously reported that Glrx knockout mice had increased protein S-glutathionylation and developed obesity by an unknown mechanism. In this study, we demonstrated that 3T3L1 adipocytes differentiation increased ROS and protein S-glutathionylation. Glrx ablation elevated protein S-glutathionylation and lipid content in 3T3L1 cells. Glrx replenishment decreased the lipid content of Glrx KO 3T3L1 cells. Glrx KO also increased protein expression and protein S-glutathionylation of the adipogenic transcription factor CCAAT enhancer-binding protein (C/EBP) β. Protein S-glutathionylation decreased the interaction of C/EBPβ and protein inhibitor of activated STAT (PIAS) 1, a small ubiquitin-related modifier E3 ligase that facilitates C/EBPβ degradation. Experiments with truncated mutant C/EBPβ demonstrated that PIAS1 interacted with the liver-enriched inhibitory protein (LIP) region of C/EBPβ. Furthermore, mass spectrometry analysis identified protein S-glutathionylation of Cys201 and Cys296 in the LIP region of C/EBPβ. The C201S, C296S double-mutant C/EBPβ prevented protein S-glutathionylation and preserved the interaction with PIAS1. In summary, Glrx ablation stimulated 3T3L1 cell differentiation and adipogenesis via increased protein S-glutathionylation of C/EBPβ, stabilizing and increasing C/EBPβ protein levels.
DOI: 10.1096/fj.201902575R
PubMed: 32141127
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Protein S-glutathionylation stimulate adipogenesis by stabilizing C/EBPβ in 3T3L1 cells.</title><author><name sortKey="Watanabe, Yosuke" sort="Watanabe, Yosuke" uniqKey="Watanabe Y" first="Yosuke" last="Watanabe">Yosuke Watanabe</name><affiliation wicri:level="1"><nlm:affiliation>Department of Internal Medicine II, University of Yamanashi, Chuo, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Internal Medicine II, University of Yamanashi, Chuo</wicri:regionArea><wicri:noRegion>Chuo</wicri:noRegion></affiliation></author><author><name sortKey="Watanabe, Kazuhiro" sort="Watanabe, Kazuhiro" uniqKey="Watanabe K" first="Kazuhiro" last="Watanabe">Kazuhiro Watanabe</name><affiliation wicri:level="1"><nlm:affiliation>Department of Internal Medicine II, University of Yamanashi, Chuo, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Internal Medicine II, University of Yamanashi, Chuo</wicri:regionArea><wicri:noRegion>Chuo</wicri:noRegion></affiliation></author><author><name sortKey="Fujioka, Daisuke" sort="Fujioka, Daisuke" uniqKey="Fujioka D" first="Daisuke" last="Fujioka">Daisuke Fujioka</name><affiliation wicri:level="1"><nlm:affiliation>Department of Internal Medicine II, University of Yamanashi, Chuo, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Internal Medicine II, University of Yamanashi, Chuo</wicri:regionArea><wicri:noRegion>Chuo</wicri:noRegion></affiliation></author><author><name sortKey="Nakamura, Kazuto" sort="Nakamura, Kazuto" uniqKey="Nakamura K" first="Kazuto" last="Nakamura">Kazuto Nakamura</name><affiliation wicri:level="1"><nlm:affiliation>Department of Internal Medicine II, University of Yamanashi, Chuo, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Internal Medicine II, University of Yamanashi, Chuo</wicri:regionArea><wicri:noRegion>Chuo</wicri:noRegion></affiliation></author><author><name sortKey="Nakamura, Takamitsu" sort="Nakamura, Takamitsu" uniqKey="Nakamura T" first="Takamitsu" last="Nakamura">Takamitsu Nakamura</name><affiliation wicri:level="1"><nlm:affiliation>Department of Internal Medicine II, University of Yamanashi, Chuo, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Internal Medicine II, University of Yamanashi, Chuo</wicri:regionArea><wicri:noRegion>Chuo</wicri:noRegion></affiliation></author><author><name sortKey="Uematsu, Manabu" sort="Uematsu, Manabu" uniqKey="Uematsu M" first="Manabu" last="Uematsu">Manabu Uematsu</name><affiliation wicri:level="1"><nlm:affiliation>Department of Internal Medicine II, University of Yamanashi, Chuo, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Internal Medicine II, University of Yamanashi, Chuo</wicri:regionArea><wicri:noRegion>Chuo</wicri:noRegion></affiliation></author><author><name sortKey="Bachschmid, Markus M" sort="Bachschmid, Markus M" uniqKey="Bachschmid M" first="Markus M" last="Bachschmid">Markus M. 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Watanabe</name><affiliation wicri:level="1"><nlm:affiliation>Department of Internal Medicine II, University of Yamanashi, Chuo, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Internal Medicine II, University of Yamanashi, Chuo</wicri:regionArea><wicri:noRegion>Chuo</wicri:noRegion></affiliation></author><author><name sortKey="Fujioka, Daisuke" sort="Fujioka, Daisuke" uniqKey="Fujioka D" first="Daisuke" last="Fujioka">Daisuke Fujioka</name><affiliation wicri:level="1"><nlm:affiliation>Department of Internal Medicine II, University of Yamanashi, Chuo, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Internal Medicine II, University of Yamanashi, Chuo</wicri:regionArea><wicri:noRegion>Chuo</wicri:noRegion></affiliation></author><author><name sortKey="Nakamura, Kazuto" sort="Nakamura, Kazuto" uniqKey="Nakamura K" first="Kazuto" last="Nakamura">Kazuto Nakamura</name><affiliation wicri:level="1"><nlm:affiliation>Department of Internal Medicine II, University of Yamanashi, Chuo, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Internal Medicine II, University of Yamanashi, Chuo</wicri:regionArea><wicri:noRegion>Chuo</wicri:noRegion></affiliation></author><author><name sortKey="Nakamura, Takamitsu" sort="Nakamura, Takamitsu" uniqKey="Nakamura T" first="Takamitsu" last="Nakamura">Takamitsu Nakamura</name><affiliation wicri:level="1"><nlm:affiliation>Department of Internal Medicine II, University of Yamanashi, Chuo, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Internal Medicine II, University of Yamanashi, Chuo</wicri:regionArea><wicri:noRegion>Chuo</wicri:noRegion></affiliation></author><author><name sortKey="Uematsu, Manabu" sort="Uematsu, Manabu" uniqKey="Uematsu M" first="Manabu" last="Uematsu">Manabu Uematsu</name><affiliation wicri:level="1"><nlm:affiliation>Department of Internal Medicine II, University of Yamanashi, Chuo, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Internal Medicine II, University of Yamanashi, Chuo</wicri:regionArea><wicri:noRegion>Chuo</wicri:noRegion></affiliation></author><author><name sortKey="Bachschmid, Markus M" sort="Bachschmid, Markus M" uniqKey="Bachschmid M" first="Markus M" last="Bachschmid">Markus M. Bachschmid</name><affiliation wicri:level="2"><nlm:affiliation>Department of Medicine, Vascular Biology Section, Whitaker Cardiovascular Institute, Boston University School of Medicine, Boston, MA, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Medicine, Vascular Biology Section, Whitaker Cardiovascular Institute, Boston University School of Medicine, Boston, MA</wicri:regionArea><placeName><region type="state">Massachusetts</region></placeName></affiliation></author><author><name sortKey="Matsui, Reiko" sort="Matsui, Reiko" uniqKey="Matsui R" first="Reiko" last="Matsui">Reiko Matsui</name><affiliation wicri:level="2"><nlm:affiliation>Department of Medicine, Vascular Biology Section, Whitaker Cardiovascular Institute, Boston University School of Medicine, Boston, MA, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Medicine, Vascular Biology Section, Whitaker Cardiovascular Institute, Boston University School of Medicine, Boston, MA</wicri:regionArea><placeName><region type="state">Massachusetts</region></placeName></affiliation></author><author><name sortKey="Kugiyama, Kiyotaka" sort="Kugiyama, Kiyotaka" uniqKey="Kugiyama K" first="Kiyotaka" last="Kugiyama">Kiyotaka Kugiyama</name><affiliation wicri:level="1"><nlm:affiliation>Department of Internal Medicine II, University of Yamanashi, Chuo, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Internal Medicine II, University of Yamanashi, Chuo</wicri:regionArea><wicri:noRegion>Chuo</wicri:noRegion></affiliation></author></analytic><series><title level="j">FASEB journal : official publication of the Federation of American Societies for Experimental Biology</title><idno type="eISSN">1530-6860</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Reactive oxygen species (ROS) increase during adipogenesis and in obesity. Oxidants react with cysteine residues of proteins to form glutathione (GSH) adducts, S-glutathionylation, that are selectively removed by glutaredoxin-1 (Glrx). We have previously reported that Glrx knockout mice had increased protein S-glutathionylation and developed obesity by an unknown mechanism. In this study, we demonstrated that 3T3L1 adipocytes differentiation increased ROS and protein S-glutathionylation. Glrx ablation elevated protein S-glutathionylation and lipid content in 3T3L1 cells. Glrx replenishment decreased the lipid content of Glrx KO 3T3L1 cells. Glrx KO also increased protein expression and protein S-glutathionylation of the adipogenic transcription factor CCAAT enhancer-binding protein (C/EBP) β. Protein S-glutathionylation decreased the interaction of C/EBPβ and protein inhibitor of activated STAT (PIAS) 1, a small ubiquitin-related modifier E3 ligase that facilitates C/EBPβ degradation. Experiments with truncated mutant C/EBPβ demonstrated that PIAS1 interacted with the liver-enriched inhibitory protein (LIP) region of C/EBPβ. Furthermore, mass spectrometry analysis identified protein S-glutathionylation of Cys201 and Cys296 in the LIP region of C/EBPβ. The C201S, C296S double-mutant C/EBPβ prevented protein S-glutathionylation and preserved the interaction with PIAS1. In summary, Glrx ablation stimulated 3T3L1 cell differentiation and adipogenesis via increased protein S-glutathionylation of C/EBPβ, stabilizing and increasing C/EBPβ protein levels.</div></front></TEI><pubmed><MedlineCitation Status="In-Data-Review" Owner="NLM"><PMID Version="1">32141127</PMID><DateRevised><Year>2020</Year><Month>04</Month><Day>06</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1530-6860</ISSN><JournalIssue CitedMedium="Internet"><Volume>34</Volume><Issue>4</Issue><PubDate><Year>2020</Year><Month>Apr</Month></PubDate></JournalIssue><Title>FASEB journal : official publication of the Federation of American Societies for Experimental Biology</Title><ISOAbbreviation>FASEB J</ISOAbbreviation></Journal><ArticleTitle>Protein S-glutathionylation stimulate adipogenesis by stabilizing C/EBPβ in 3T3L1 cells.</ArticleTitle><Pagination><MedlinePgn>5827-5837</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1096/fj.201902575R</ELocationID><Abstract><AbstractText>Reactive oxygen species (ROS) increase during adipogenesis and in obesity. Oxidants react with cysteine residues of proteins to form glutathione (GSH) adducts, S-glutathionylation, that are selectively removed by glutaredoxin-1 (Glrx). We have previously reported that Glrx knockout mice had increased protein S-glutathionylation and developed obesity by an unknown mechanism. In this study, we demonstrated that 3T3L1 adipocytes differentiation increased ROS and protein S-glutathionylation. Glrx ablation elevated protein S-glutathionylation and lipid content in 3T3L1 cells. Glrx replenishment decreased the lipid content of Glrx KO 3T3L1 cells. Glrx KO also increased protein expression and protein S-glutathionylation of the adipogenic transcription factor CCAAT enhancer-binding protein (C/EBP) β. Protein S-glutathionylation decreased the interaction of C/EBPβ and protein inhibitor of activated STAT (PIAS) 1, a small ubiquitin-related modifier E3 ligase that facilitates C/EBPβ degradation. Experiments with truncated mutant C/EBPβ demonstrated that PIAS1 interacted with the liver-enriched inhibitory protein (LIP) region of C/EBPβ. Furthermore, mass spectrometry analysis identified protein S-glutathionylation of Cys201 and Cys296 in the LIP region of C/EBPβ. The C201S, C296S double-mutant C/EBPβ prevented protein S-glutathionylation and preserved the interaction with PIAS1. In summary, Glrx ablation stimulated 3T3L1 cell differentiation and adipogenesis via increased protein S-glutathionylation of C/EBPβ, stabilizing and increasing C/EBPβ protein levels.</AbstractText><CopyrightInformation>© 2020 Federation of American Societies for Experimental Biology.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Watanabe</LastName><ForeName>Yosuke</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Internal Medicine II, University of Yamanashi, Chuo, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Watanabe</LastName><ForeName>Kazuhiro</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Internal Medicine II, University of Yamanashi, Chuo, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fujioka</LastName><ForeName>Daisuke</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Department of Internal Medicine II, University of Yamanashi, Chuo, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nakamura</LastName><ForeName>Kazuto</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Internal Medicine II, University of Yamanashi, Chuo, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nakamura</LastName><ForeName>Takamitsu</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Internal Medicine II, University of Yamanashi, Chuo, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Uematsu</LastName><ForeName>Manabu</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Internal Medicine II, University of Yamanashi, Chuo, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bachschmid</LastName><ForeName>Markus M</ForeName><Initials>MM</Initials><AffiliationInfo><Affiliation>Department of Medicine, Vascular Biology Section, Whitaker Cardiovascular Institute, Boston University School of Medicine, Boston, MA, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Matsui</LastName><ForeName>Reiko</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Medicine, Vascular Biology Section, Whitaker Cardiovascular Institute, Boston University School of Medicine, Boston, MA, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kugiyama</LastName><ForeName>Kiyotaka</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Internal Medicine II, University of Yamanashi, Chuo, Japan.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 DK103750</GrantID><Acronym>DK</Acronym><Agency>NIDDK NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>16GRNT27660006</GrantID><Agency>American Heart Association</Agency><Country></Country></Grant><Grant><GrantID>R01 HL133013</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 HL133013</GrantID><Acronym>HL</Acronym><Agency>NHLBI NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>03</Month><Day>05</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>FASEB J</MedlineTA><NlmUniqueID>8804484</NlmUniqueID><ISSNLinking>0892-6638</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">CCAAT enhancer-binding protein</Keyword><Keyword MajorTopicYN="N">S-glutathionylation</Keyword><Keyword MajorTopicYN="N">glutaredoxin-1</Keyword><Keyword MajorTopicYN="N">reactive oxygen species</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>10</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>02</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>02</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>3</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>3</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>3</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32141127</ArticleId><ArticleId IdType="doi">10.1096/fj.201902575R</ArticleId></ArticleIdList><ReferenceList><Title>REFERENCES</Title><Reference><Citation>Fruh SM. Obesity: risk factors, complications, and strategies for sustainable long-term weight management. J Am Assoc Nurse Pract. 2017;29:S3-S14.</Citation></Reference><Reference><Citation>Unamuno X, Gómez-Ambrosi J, Rodríguez A, Becerril S, Frühbeck G, Catalán V. Adipokine dysregulation and adipose tissue inflammation in human obesity. Eur J Clin Invest. 2018;48:e12997.</Citation></Reference><Reference><Citation>Hausman DB, DiGirolamo M, Bartness TJ, Hausman GJ, Martin RJ. The biology of white adipocyte proliferation. Obes Rev. 2001;2:239-254.</Citation></Reference><Reference><Citation>Lee H, Lee YJ, Choi H, Ko EH, Kim J-W. Reactive oxygen species facilitate adipocyte differentiation by accelerating mitotic clonal expansion. J Biol Chem. 2009;284:10601-10609.</Citation></Reference><Reference><Citation>Tormos KV, Anso E, Hamanaka RB, et al. Mitochondrial complex III ROS regulate adipocyte differentiation. Cell Metab. 2011;14:537-544.</Citation></Reference><Reference><Citation>Chang YC, Yu YH, Shew JY, et al. Deficiency of NPGPx, an oxidative stress sensor, leads to obesity in mice and human. EMBO Mol Med. 2013;5:1165-1179.</Citation></Reference><Reference><Citation>Youn J, Siu KL, Lob HE, Itani H, Harrison DG, Cai H. Role of vascular oxidative stress in obesity and metabolic syndrome. Diabetes. 2014;63:2344-2355.</Citation></Reference><Reference><Citation>Furukawa S, Fujita T, Shimabukuro M, et al. Increased oxidative stress in obesity and its impact on metabolic syndrome. J Clin Invest. 2004;114:1752-1761.</Citation></Reference><Reference><Citation>Kobayashi T, Watanabe Y, Saito Y, et al. Mice lacking the glutamate-cysteine ligase modifier subunit are susceptible to myocardial ischaemia-reperfusion injury. Cardiovasc Res. 2010;85:785-795.</Citation></Reference><Reference><Citation>Kendig EL, Chen Y, Krishan M, et al. Lipid metabolism and body composition in Gclm(-/-) mice. Toxicol Appl Pharmacol. 2011;257:338-348.</Citation></Reference><Reference><Citation>Watanabe Y, Cohen RA, Matsui R. Redox regulation of ischemic angiogenesis-another aspect of reactive oxygen species-. Circ J. 2016;80:1278-1284.</Citation></Reference><Reference><Citation>Watanabe Y, Watanabe K, Kobayashi T, et al. Chronic depletion of glutathione exacerbates ventricular remodelling and dysfunction in the pressure-overloaded heart. Cardiovasc Res. 2013;97:282-292.</Citation></Reference><Reference><Citation>Chrestensen CA, Starke DW, Mieyal JJ. Acute cadmium exposure inactivates thioltransferase (Glutaredoxin), inhibits intracellular reduction of protein-glutathionyl-mixed disulfides, and initiates apoptosis. J Biol Chem. 2000;275:26556-26565.</Citation></Reference><Reference><Citation>Shao D, Han J, Hou X, et al. Glutaredoxin-1 deficiency causes fatty liver and dyslipidemia by inhibiting Sirtuin-1. Antioxid Redox Signal. 2017;27:313-327.</Citation></Reference><Reference><Citation>Cho H, Kim KM, Han S, et al. Staufen1-mediated mRNA decay functions in adipogenesis. Mol Cell. 2012;46:495-506.</Citation></Reference><Reference><Citation>Ran FA, Hsu PD, Wright J, Agarwala V, Scott DA, Zhang F. Genome engineering using the CRISPR-Cas9 system. Nat Protoc. 2013;8:2281-2308.</Citation></Reference><Reference><Citation>Han YH, Moon HJ, You BR, Kim SZ, Kim SH, Park WH. The effects of N-acetyl cysteine on the MG132 proteasome inhibitor-treated lung cancer cells in relation to cell growth, reactive oxygen species and glutathione. Int J Mol Med. 2010;25:657-662.</Citation></Reference><Reference><Citation>Liu Y, Zhang Y-D, Guo L, et al. Protein inhibitor of activated STAT 1 (PIAS1) is identified as the SUMO E3 ligase of CCAAT/enhancer-binding protein β (C/EBPβ) during adipogenesis. Mol Cell Biol. 2013;33:4606-4617.</Citation></Reference><Reference><Citation>Luedde T, Duderstadt M, Streetz KL, et al. C/EBP β isoforms LIP and LAP modulate progression of the cell cycle in the regenerating mouse liver. Hepatology. 2004;40:356-365.</Citation></Reference><Reference><Citation>Klein EA, Thompson IM, Tangen CM, et al. Vitamin E and the risk of prostate cancer. JAMA. 2011;306:1549.</Citation></Reference><Reference><Citation>Han CY, Umemoto T, Omer M, et al. NADPH oxidase-derived reactive oxygen species increases expression of monocyte chemotactic factor genes in cultured adipocytes. J Biol Chem. 2012;287:10379-10393.</Citation></Reference><Reference><Citation>Vigilanza P, Aquilano K, Baldelli S, Rotilio G, Ciriolo MR. Modulation of intracellular glutathione affects adipogenesis in 3T3-L1 cells. J Cell Physiol. 2011;226:2016-2024.</Citation></Reference><Reference><Citation>Anathy V, Lahue KG, Chapman DG, et al. Reducing protein oxidation reverses lung fibrosis. Nat Med. 2018;24:1128-1135.</Citation></Reference><Reference><Citation>Zhang Y-Y, Li X, Qian S-W, et al. Transcriptional activation of histone H4 by C/EBPβ during the mitotic clonal expansion of 3T3-L1 adipocyte differentiation. Mol Biol Cell. 2011;22:2165-2174.</Citation></Reference><Reference><Citation>Guo L, Li X, Tang Q-Q. Transcriptional regulation of adipocyte differentiation: a central role for CCAAT/enhancer-binding protein (C/EBP) β. J Biol Chem. 2015;290:755-761.</Citation></Reference><Reference><Citation>Tanaka T, Yoshida N, Kishimoto T, Akira S. Defective adipocyte differentiation in mice lacking the C/EBPβ and/or C/EBPδ gene. EMBO J. 1997;16:7432-7443.</Citation></Reference><Reference><Citation>Millward CA, Heaney JD, Sinasac DS, et al. Mice with a deletion in the gene for CCAAT/enhancer-binding protein β are protected against diet-induced obesity. Diabetes. 2007;56:161-167.</Citation></Reference><Reference><Citation>Hershko A, Ciechanover A. The ubiquitin system. Annu Rev Biochem. 1998;67:425-479.</Citation></Reference><Reference><Citation>Herrmann J, Lerman LO, Lerman A. Ubiquitin and ubiquitin-like proteins in protein regulation. Circ Res. 2007;100:1276-1291.</Citation></Reference><Reference><Citation>Berndsen CE, Wolberger C. New insights into ubiquitin E3 ligase mechanism. Nat Struct Mol Biol. 2014;21:301-307.</Citation></Reference><Reference><Citation>Watanabe Y, Murdoch CE, Sano S, et al. Glutathione adducts induced by ischemia and deletion of glutaredoxin-1 stabilize HIF-1α and improve limb revascularization. Proc Natl Acad Sci USA. 2016;113:6011-6016.</Citation></Reference><Reference><Citation>Carvalho AN, Marques C, Guedes RC, et al. S -Glutathionylation of Keap1: a new role for glutathione S -transferase pi in neuronal protection. FEBS Lett. 2016;590:1455-1466.</Citation></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Japon</li><li>États-Unis</li></country><region><li>Massachusetts</li></region></list><tree><country name="Japon"><noRegion><name sortKey="Watanabe, Yosuke" sort="Watanabe, Yosuke" uniqKey="Watanabe Y" first="Yosuke" last="Watanabe">Yosuke Watanabe</name></noRegion><name sortKey="Fujioka, Daisuke" sort="Fujioka, Daisuke" uniqKey="Fujioka D" first="Daisuke" last="Fujioka">Daisuke Fujioka</name><name sortKey="Kugiyama, Kiyotaka" sort="Kugiyama, Kiyotaka" uniqKey="Kugiyama K" first="Kiyotaka" last="Kugiyama">Kiyotaka Kugiyama</name><name sortKey="Nakamura, Kazuto" sort="Nakamura, Kazuto" uniqKey="Nakamura K" first="Kazuto" last="Nakamura">Kazuto Nakamura</name><name sortKey="Nakamura, Takamitsu" sort="Nakamura, Takamitsu" uniqKey="Nakamura T" first="Takamitsu" last="Nakamura">Takamitsu Nakamura</name><name sortKey="Uematsu, Manabu" sort="Uematsu, Manabu" uniqKey="Uematsu M" first="Manabu" last="Uematsu">Manabu Uematsu</name><name sortKey="Watanabe, Kazuhiro" sort="Watanabe, Kazuhiro" uniqKey="Watanabe K" first="Kazuhiro" last="Watanabe">Kazuhiro Watanabe</name></country><country name="États-Unis"><region name="Massachusetts"><name sortKey="Bachschmid, Markus M" sort="Bachschmid, Markus M" uniqKey="Bachschmid M" first="Markus M" last="Bachschmid">Markus M. Bachschmid</name></region><name sortKey="Matsui, Reiko" sort="Matsui, Reiko" uniqKey="Matsui R" first="Reiko" last="Matsui">Reiko Matsui</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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