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