dc.contributor.author | Yang, Mingyi | |
dc.contributor.author | Lin, Xiaolin | |
dc.contributor.author | Segers, Filip | |
dc.contributor.author | Suganthan, Rajikala | |
dc.contributor.author | Hildrestrand, Gunn Annette | |
dc.contributor.author | Rinholm, Johanne Egge | |
dc.contributor.author | Aas, Per Arne | |
dc.contributor.author | Sousa, Mirta | |
dc.contributor.author | Holm, Sverre | |
dc.contributor.author | Bolstad, Nils | |
dc.contributor.author | Warren, David | |
dc.contributor.author | Berge, Rolf Kristian | |
dc.contributor.author | Johansen, Rune Forstrøm | |
dc.contributor.author | Yndestad, Arne | |
dc.contributor.author | Kristiansen, Elise | |
dc.contributor.author | Klungland, Arne | |
dc.contributor.author | Gomez, Luisa Fernanda Luna | |
dc.contributor.author | Eide, Lars | |
dc.contributor.author | Halvorsen, Bente | |
dc.contributor.author | Aukrust, Pål | |
dc.contributor.author | Bjørås, Magnar | |
dc.date.accessioned | 2021-04-22T06:19:34Z | |
dc.date.available | 2021-04-22T06:19:34Z | |
dc.date.created | 2020-07-01T12:09:41Z | |
dc.date.issued | 2020 | |
dc.Published | Cell reports. 2020, 30 (12), 4165-4178. | |
dc.identifier.issn | 2211-1247 | |
dc.identifier.uri | https://hdl.handle.net/11250/2738985 | |
dc.description.abstract | Oxidation resistance gene 1 (OXR1) protects cells against oxidative stress. We find that male mice with brain-specific isoform A knockout (Oxr1A−/−) develop fatty liver. RNA sequencing of male Oxr1A−/− liver indicates decreased growth hormone (GH) signaling, which is known to affect liver metabolism. Indeed, Gh expression is reduced in male mice Oxr1A−/− pituitary gland and in rat Oxr1A−/− pituitary adenoma cell-line GH3. Oxr1A−/− male mice show reduced fasting-blood GH levels. Pull-down and proximity ligation assays reveal that OXR1A is associated with arginine methyl transferase PRMT5. OXR1A-depleted GH3 cells show reduced symmetrical dimethylation of histone H3 arginine 2 (H3R2me2s), a product of PRMT5 catalyzed methylation, and chromatin immunoprecipitation (ChIP) of H3R2me2s shows reduced Gh promoter enrichment. Finally, we demonstrate with purified proteins that OXR1A stimulates PRMT5/MEP50-catalyzed H3R2me2s. Our data suggest that OXR1A is a coactivator of PRMT5, regulating histone arginine methylation and thereby GH production within the pituitary gland. | en_US |
dc.language.iso | eng | en_US |
dc.publisher | Elsevier | en_US |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internasjonal | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/deed.no | * |
dc.title | OXR1A, a Coactivator of PRMT5 Regulating Histone Arginine Methylation | en_US |
dc.type | Journal article | en_US |
dc.type | Peer reviewed | en_US |
dc.description.version | publishedVersion | en_US |
dc.rights.holder | Copyright 2020 The Authors | en_US |
cristin.ispublished | true | |
cristin.fulltext | original | |
cristin.qualitycode | 1 | |
dc.identifier.doi | 10.1016/j.celrep.2020.02.063 | |
dc.identifier.cristin | 1818071 | |
dc.source.journal | Cell reports | en_US |
dc.source.40 | 30 | |
dc.source.14 | 12 | |
dc.source.pagenumber | 4165-4178 | en_US |
dc.relation.project | Norges forskningsråd: 240099/F20 | en_US |
dc.relation.project | Helse Sør-Øst RHF: 2017117 | en_US |
dc.relation.project | Helse Sør-Øst RHF: 2014092 | en_US |
dc.relation.project | Kreftforeningen: 182744-2016 | en_US |
dc.relation.project | Norges forskningsråd: 24973 | en_US |
dc.relation.project | Norges forskningsråd: 239211 | en_US |
dc.relation.project | Notur/NorStore: NN9383K | en_US |
dc.identifier.citation | Cell reports. 2020, 30, 12, 4165-4178 | en_US |
dc.source.volume | 30 | en_US |
dc.source.issue | 12 | en_US |