Barroso, MadalenaFlorindo, CristinaKalwa, HermannSilva, ZéliaTuranov, Anton A.Carlson, Bradley A.De Almeida, Isabel TavaresBlom, Henk J.Gladyshev, Vadim N.Hatfield, Dolph L.Michel, ThomasCastro, RitaLoscalzo, JosephHandy, Diane E.2018-06-262018-06-262014-05-300021-9258PURE: 4445823PURE UUID: 4ffdf279-ea0a-416f-a4b5-c6e86e971d80Scopus: 84901724596PubMed: 24719327WOS: 000337465400019ORCID: /0000-0001-6660-426X/work/203333196http://www.scopus.com/inward/record.url?scp=84901724596&partnerID=8YFLogxKThis work was supported, in whole or in part, by National Institutes of Health Grants HL067195, HL070819, HL048743, HL107192, and HL108630 (to J. L.); HL46457 and HL48743 (to T. M.); and GM061603 (to V. N. G.). This work was also supported by an American Heart Association postdoctoral fellowship grant (to H. K.) and by Portuguese Fundacao para a Ciencia e a Tecnologia Grants PTDC/SAU-ORG/112683/2009 (to R. C.) and SFRH/BD/73021/2010 (M. B.).Background: Methylation of tRNASec facilitates the incorporation of selenocysteine at a UGA codon during translation. Results: Accumulation of the homocysteine precursor S-adenosylhomocysteine decreases tRNASec methylation, reducing glutathione peroxidase 1 expression and increasing oxidative stress-induced inflammatory activation of endothelial cells. Conclusion: Methylation modulates the expression of selenoproteins to regulate redox-dependent inflammatory pathways. Significance: Hypomethylation stress promotes a proatherogenic endothelial cell phenotype.131330712engBiochemistryMolecular BiologyCell Biologyjournal article10.1074/jbc.M114.549782https://www.scopus.com/pages/publications/84901724596