Ask about this productRelated genes to: OGFOD1 antibody
- Gene:
- OGFOD1 NIH gene
- Name:
- 2-oxoglutarate and iron dependent oxygenase domain containing 1
- Previous symbol:
- -
- Synonyms:
- KIAA1612, FLJ10826, TPA1
- Chromosome:
- 16q13
- Locus Type:
- gene with protein product
- Date approved:
- 2006-02-14
- Date modifiied:
- 2016-10-05
Related products to: OGFOD1 antibody
Related articles to: OGFOD1 antibody
- 2-oxoglutarate-and iron-dependent oxygenase domain-containing protein 1(OGFOD1) is a prolyl hydroxylase that plays a pivotal role in regulating protein synthesis accuracy and efficiency. OGFOD1 is implicated in the pathogenesis of various cancers, including lung cancer, breast cancer and colonic cancer. A recent study highlights that under chemotherapy pressure, the upregulation of OGFOD1 promotes global protein synthesis via its catalytic activity, which is a key mechanism for AML chemoresistance. Deleting of OGFOD1 specifically compromises AML translation adaptability, thereby eradicating post-chemotherapy resistant cells and extending survival , while sparing normal hematopoiesis. Consequently, targeting OGFOD1 with identified inhibitors presents a promising therapeutic strategy to disrupt the translational adaptability of AML cells, potentially overcoming chemoresistance and improving patient outcomes. More importantly, there is an urgent need to develop highly selective OGFOD1-targeted agents with minimal toxicity. - Source: PubMed
Publication date: 2026/04/20
Qiu TingtingLi PeiyiTan LiquanWu ShuangLuo Qunli - Hepatic ischemia-reperfusion injury (HIRI) is a complicated pathological process impacting the prognosis of patients suffering from liver resection and transplantation surgery. 2-oxoglutarate and iron dependent oxygenase domain containing 1 (OGFOD1), a crucial factor involved in protein translation, was highly expressed during HIRI. However, its role as well as underlying mechanism is still unclear. In this study, two datasets from Gene Expression Omnibus database were analyzed and we focused on OGFOD1 which is associated with ischemia-reperfusion. Later, a HIRI rat model and a hypoxia/reoxygenation (H/R) hepatocyte model were established to explore the expression of OGFOD1 and its underlying mechanism. Furthermore, transcriptomics and proteomics were performed to analyze the downstreams of OGFOD1 in H/R hepatocytes. Our results showed that the expression of OGFOD1 in HIRI rats and H/R hepatocytes were higher than negative controls. OGFOD1 silencing ameliorated liver function, reduced hepatocellular apoptosis and mitigated oxidative stress. Later, the combined analysis of transcriptomics and proteomics showed that 5811 mRNAs and 476 proteins were modulated by OGFOD1 silencing and these factors were classified into four classes. Among these factors, secreted protein acidic and rich in cysteine (SPARC) in Class III, with decreased protein level but no-changed mRNA level, caught our eyes. Silencing OGFOD1 decreased the protein level of SPARC, but not its mRNA level. More interestingly, SPARC overexpression rescued the effects of OGFOD1 silencing on apoptosis and oxidative stress in H/R hepatocytes. Totally, OGFOD1 was a vital modulator during HIRI and its downregulation alleviated oxidative stress and apoptosis through declining SPARC protein level. - Source: PubMed
Publication date: 2026/01/18
Li ZexinWang XiaoCui YuanyuanLiu YiWei RuiWang YixinTang XiaolongLi LiangbinLi JiasaiZuo Keqiang - Acute myeloid leukemia (AML) commonly relapses after initial chemotherapy response. We assessed metabolic adaptations in chemoresistant cells in vivo before overt relapse, identifying altered branched-chain amino acid (BCAA) levels in patient-derived xenografts (PDXs) and immunophenotypically identified leukemia stem cells from AML patients. Notably, this was associated with increased BCAA transporter expression with low BCAA catabolism. Restricting BCAAs further reduced chemoresistant AML cells, but relapse still occurred. Among the persisting cells, we found an unexpected increase in protein production. This was accompanied by elevated translation of 2-oxoglutarate- and iron-dependent oxygenase 1 (OGFOD1), a known ribosomal dioxygenase that adjusts the fidelity of tRNA anticodon pairing with coding mRNA. We found that OGFOD1 upregulates protein synthesis in AML, driving disease aggressiveness. Inhibiting OGFOD1 impaired translation processing, decreased protein synthesis and improved animal survival even with chemoresistant AML while sparing normal hematopoiesis. Leukemic cells can therefore persist despite the stress of chemotherapy and nutrient deprivation through adaptive control of translation. Targeting OGFOD1 may offer a distinctive, translation-modifying means of reducing the chemopersisting cells that drive relapse. - Source: PubMed
Publication date: 2025/09/16
Mayerhofer ChristinaLi DanKristiansen TrineMayerhofer ErnstSharda AzeemSchiroli GiuliaGustafsson KarinHe LingliMazzola MichaelKeyes SamKiem AnnaCrompton EveXu YanxinKorm SovannarithDou ZhixunVidoudez CharlesMiller Peter Gvan Gastel NickGraubert Timothy AScadden David T - α-ketoglutaric acid (AKG), a tricarboxylic acid cycle metabolite central to aerobic metabolism and longevity, retains unresolved anti-aging protein targets. Here, we demonstrate that reduced isocitrate dehydrogenase 1 (IDH1) expression during senescence lowers AKG production, accelerating the aging of mesenchymal stem cells (MSCs). Exogenous AKG or IDH1 overexpression restores AKG levels, enabling 2-oxoglutarate and Fe(II)-dependent oxygenase domain-containing protein 1 (OGFOD1)-catalyzed hydroxylation of ribosomal protein S23 (RPS23) at proline 62. Mechanistically, AKG stabilizes the OGFOD1-RPS23 complex, enhancing translation accuracy to limit misfolded protein accumulation while sustaining synthesis rates, thereby balancing proteostasis. The natural flavonoid scutellarin (Scu), identified as an IDH1 agonist, elevates AKG to delay MSC senescence. In aged mice, Scu improves cognitive function, reduces osteoporosis and skin aging, and suppresses senescence-associated secretory phenotype. Our findings identify the AKG-IDH1-RPS23 axis as a regulator of stem cell senescence and we propose metabolic reprogramming strategies for anti-aging therapies. - Source: PubMed
Publication date: 2025/06/25
Cui ZhaoLi JiamengLi CaifengDeng ShiwenLiu WeiLei TongCao JunxianWang ZiyiWang XiaoxuMa ShuhuaZhu YinhuaYang HongjunChen Peng - Existing genetic studies of neuroticism have been largely limited to common variants. Here we performed a large-scale exome analysis of white British individuals from UK Biobank, revealing the role of coding variants in neuroticism. For rare variants, collapsing analysis uncovered 14 neuroticism-associated genes. Among these, 12 (PTPRE, BCL10, TRIM32, ANKRD12, ADGRB2, MON2, HIF1A, ITGB2, STK39, CAPNS2, OGFOD1 and KDM4B) were novel, and the remaining (MADD and TRPC4AP) showed convergent evidence with common variants. Heritability of rare coding variants was estimated to be up to 7.3% for neuroticism. For common variants, we identified 78 significant associations, implicating 6 unreported genes. We subsequently replicated these variants using meta-analysis across other four ancestries from UK Biobank and summary data from 23andMe sample. Furthermore, these variants had widespread impacts on neuropsychiatric disorders, cognitive abilities and brain structure. Our findings deepen the understanding of neuroticism's genetic architecture and provide potential targets for future mechanistic research. - Source: PubMed
Publication date: 2024/11/07
Wu Xin-RuiLi Ze-YuYang LiuLiu YingFei Chen-JieDeng Yue-TingLiu Wei-ShiWu Bang-ShengDong QiangFeng Jian-FengCheng WeiYu Jin-Tai