<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Watanabe Y</submitter><funding>American Heart Association</funding><funding>NIDDK NIH HHS</funding><funding>NHLBI NIH HHS</funding><funding>Uehara Memorial Foundation</funding><pagination>5827-5837</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8491561</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>34(4)</volume><pubmed_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)</pubmed_abstract><journal>FASEB journal : official publication of the Federation of American Societies for Experimental Biology</journal><pubmed_title>Protein S-glutathionylation stimulate adipogenesis by stabilizing C/EBPβ in 3T3L1 cells.</pubmed_title><pmcid>PMC8491561</pmcid><funding_grant_id>R01 DK103750</funding_grant_id><funding_grant_id>R01 HL133013</funding_grant_id><funding_grant_id>16GRNT27660006</funding_grant_id><pubmed_authors>Bachschmid MM</pubmed_authors><pubmed_authors>Watanabe Y</pubmed_authors><pubmed_authors>Fujioka D</pubmed_authors><pubmed_authors>Nakamura K</pubmed_authors><pubmed_authors>Kugiyama K</pubmed_authors><pubmed_authors>Watanabe K</pubmed_authors><pubmed_authors>Nakamura T</pubmed_authors><pubmed_authors>Uematsu M</pubmed_authors><pubmed_authors>Matsui R</pubmed_authors></additional><is_claimable>false</is_claimable><name>Protein S-glutathionylation stimulate adipogenesis by stabilizing C/EBPβ in 3T3L1 cells.</name><description>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)</description><dates><release>2020-01-01T00:00:00Z</release><publication>2020 Apr</publication><modification>2025-04-04T22:43:30.588Z</modification><creation>2022-02-11T11:47:17.362Z</creation></dates><accession>S-EPMC8491561</accession><cross_references><pubmed>32141127</pubmed><doi>10.1096/fj.201902575R</doi><doi>10.1096/fj.201902575r</doi></cross_references></HashMap>