Ask about this productRelated genes to: Jmjd8 antibody
- Gene:
- JMJD8 NIH gene
- Name:
- jumonji domain containing 8
- Previous symbol:
- C16orf20
- Synonyms:
- -
- Chromosome:
- 16p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 2000-12-21
- Date modifiied:
- 2015-08-25
Related products to: Jmjd8 antibody
Related articles to: Jmjd8 antibody
- Grass carp (Ctenopharyngodon idella) is an economically important fish species that holds a central position in freshwater aquaculture in China, and its primary disease, grass carp hemorrhagic disease (GCHD), is caused by Grass Carp Reovirus (GCRV) infection. GCHD poses serious threats to aquaculture, but traditional prevention and control methods are limited. Currently, the primary measures for preventing and controlling the disease include vaccination and cultivating disease-resistant varieties. Breeding resistant varieties is an effective strategy to improve grass carp's disease resistance. In a previous study, the role of candidate gene jmjd8 (JmjC domain-containing 8), which is related to grass carp hemorrhagic disease resistance, in the mechanism of grass carp disease resistance was identified through multi-omics association analysis. We conducted functional studies on the grass carp jmjd8 gene and cloned its open reading frame (ORF). Bioinformatics analysis revealed that the encoded protein possesses a conserved JmjC domain, which is highly homologous to those of zebrafish and carp. Tissue expression analysis showed that jmjd8 was highly expressed in the head kidney and gill of healthy grass carp, and its expression was significantly upregulated in the spleen and mesonephros after GCRV infection, suggesting that it was involved in the immune response. Subcellular localization analysis demonstrated that jmjd8 was predominantly localized in the nucleus. By establishing stable transient overexpression cell lines, we found that jmjd8 overexpression significantly inhibited GCRV replication in Ctenopharyngodon idella kidney cells (CIK), suggesting its potential to enhance antiviral immunity by regulating host epigenetic modifications. These findings indicate that jmjd8 may play a significant role in breeding disease-resistant grass carp and provide novel insights for enhancing GCRV resistance via a potential epigenetic mechanism. - Source: PubMed
Publication date: 2025/12/04
Gao XijuanZhang ChenyangTao ChendongWang YushanLiu FeiLi JialeMeng XinzhanShen Yubang - We previously identified Jumonji domain-containing 8 (JMJD8) as a regulator of lipid droplet (LD) hypertrophy in adipocytes through modulation of AMPK-dependent perilipin-2 (PLIN2) phosphorylation. Given PLIN2's established role in hepatic steatosis, we investigated whether JMJD8 also regulates lipid accumulation in the liver. Here, we report that JMJD8 expression is significantly elevated in the livers of mice fed either a high-fat diet (HFD) or the metabolic-associated fatty liver disease (MAFLD)-inducing Gubra Amylin NASH (GAN) diet. To define the metabolic role of JMJD8 in the liver, we generated liver-specific knockout () mice. Hepatic deletion of reduced triglyceride (TG) accumulation under both dietary conditions, without affecting overall body weight or adiposity. Lipidomic analyses revealed a redistribution of lipid classes in knockout livers on HFD, with decreased storage lipids and increased membrane phospholipids. mice also displayed improved insulin sensitivity and glucose tolerance under HFD but not the GAN diet. Mechanistically, although JMJD8 interacts with PLIN2, its prosteatotic effect appears to be independent of PLIN2. These findings indicate that JMJD8 promotes hepatic steatosis and metabolic dysregulation under HFD by altering lipid class distribution, highlighting its potential as a therapeutic target in obesity-associated metabolic disease. This study identifies Jumonji domain-containing 8 (JMJD8) as a previously unrecognized driver of hepatic steatosis and metabolic dysfunction in diet-induced fatty liver disease. Liver-specific deletion of protects against triglyceride accumulation and insulin resistance, redirecting hepatic lipid composition from energy storage toward membrane remodeling. These findings establish JMJD8 as a key intracellular regulator of lipid homeostasis and glucose metabolism and highlight its potential as a therapeutic target for metabolic-associated fatty liver disease. - Source: PubMed
Publication date: 2025/10/29
You DongjooRen HangjiangJung Byung ChulOh Natalie YoungjiWang LipingMaschek John AlanSummers Scott AKang Sona - Breast cancer has severe consequences due to late diagnosis and the lack of effective therapies. Currently, potential biomarkers for breast cancer have not been systematically evaluated. Research has shown that JMJD8 is associated with cGAS-STING pathway and plays a role in various tumor microenvironments, but its relationship with breast cancer remains unclear. We investigate the relationship between JMJD8 and the prognosis and immune infiltration microenvironment of breast cancer, exploring its potential as a prognostic biomarker for this type of cancer. - Source: PubMed
Publication date: 2025/07/21
Zhu ChenleiXi TianyiYang GuorongLu WenWang SentaiCao Jiwei - New research builds on previous findings that JMJD8 mediates insulin resistance by promoting adipocyte hypertrophy. We identified PLIN2 as a binding partner of JMJD8 using proteomics approaches. This study reveals a physical interaction between JMJD8 and PLIN2, which plays a crucial role in driving adipocyte hypertrophy and insulin resistance. JMJD8 suppresses fasting-induced lipophagy and reduces energy production by inhibiting PLIN2 phosphorylation. These findings highlight the importance of JMJD8 and PLIN2 in regulating lipid droplet homeostasis and suggest a potential mechanism for controlling fat mobilization during energy deprivation. - Source: PubMed
You DongjooKang Sona - The expression of Egl-9 family hypoxia-inducible factor 3 (EGLN3) is notably decreased in various malignancies, including gastric cancer (GC). While the predominant focus has been on the hydroxylase activity of EGLN3 for its antitumour effects, recent findings have suggested nonenzymatic roles for EGLN3. - Source: PubMed
Publication date: 2024/01/06
Cai FenglinYang XiudingMa GangWang PengliangZhang MengmengZhang NannanZhang RupengLiang HanNie YongzhanDong ChengDeng Jingyu