Ask about this productRelated genes to: JMJD2C antibody
- Gene:
- KDM4C NIH gene
- Name:
- lysine demethylase 4C
- Previous symbol:
- JMJD2C
- Synonyms:
- GASC1, KIAA0780, TDRD14C
- Chromosome:
- 9p24.1
- Locus Type:
- gene with protein product
- Date approved:
- 2004-01-14
- Date modifiied:
- 2016-10-05
Related products to: JMJD2C antibody
Related articles to: JMJD2C antibody
- [This corrects the article on p. 491 in vol. 10, PMID: 32195022.]. - Source: PubMed
Publication date: 2026/03/25
Wu XiaoweiDeng YuZu YukunYin Jin - White adipose tissue (WAT) is a key endocrine organ regulating lipid and glucose homeostasis. Early metabolic disturbances may disrupt its endocrine function through epigenetic mechanisms; however, how DNA methylation contributes to prediabetes and its reversal remains largely unexplored. - Source: PubMed
Publication date: 2026/02/24
Dumrauf BárbaraMencucci María VictoriaLacunza EzequielAbba Martín CarlosFlores Luis EmilioMaiztegui BárbaraGagliardino Juan JoséFrancini FlavioLisi Román Carolina - This study aims to investigate structural and expression-level alterations in the histone demethylase KDM4C gene in patients with rheumatoid arthritis (RA) and elucidate its role in the disease's epigenetic basis. KDM4C sequencing was performed in RA patients, and identified variants were mapped to functional domains, including the JmjN and PHD-type2 regions. KDM4C expression was assessed by quantitative PCR in RA and control groups. Molecular findings were analyzed alongside patients' clinical characteristics and treatment histories. A rare missense mutation (c.79 C > T, R27W) located in the JmjN domain was detected in a single patient with RA. In addition, a synonymous variant was identified in the PHD-type2 domain. The R27W variant is predicted by in silico analyses to impair protein homodimerization, while the synonymous change has been hypothesized to influence translational efficiency. Neither variant has previously been linked to RA. KDM4C mRNA expression was significantly reduced in patients with RA. This reduction was particularly evident in individuals with high CRP/ESR levels, positive RF and anti-CCP status, and treatment resistance. Taken together, the molecular and clinical findings suggest a potential functional alteration of KDM4C activity. Specifically, KDM4C may have a reduced capacity to remove repressive methylation marks on histone H3, particularly H3K9me3. These findings suggest that KDM4C dysregulation may promote a closed chromatin conformation in immune cells. This state may lead to silencing of genes involved in immune regulation and increased expression of inflammatory genes, thereby contributing to the pathogenesis of RA. KDM4C appears to be an important epigenetic regulator in RA pathogenesis. The coexistence of structural variants and decreased expression underscores its potential as a diagnostic biomarker and therapeutic target. To our knowledge, this is the first study providing integrated clinical and genetic evidence linking KDM4C dysregulation to RA. - Source: PubMed
Publication date: 2026/02/13
Oner Deniz AslarToktas HasanDundar UmitAdar SevdaEyvaz Nuran - HCC predominantly develops in individuals with chronic hepatic conditions and liver cirrhosis, which is marked by high mortality. This study investigates the functional roles and molecular mechanisms by which FOXP2 modulates HCC progression through ferroptosis. After HCC and normal cells were cultured, the expression of FOXP2, RBM15B, and KDM4C was analyzed using western blot or RT-qPCR. After FOXP2 intervention, cellular metabolic activity was assessed via CCK-8 assay, while replicative capacity was quantified through EdU staining and colony formation assays; key regulators of ferroptosis were analyzed by western blot; iron content and oxidative stress levels were measured. The binding between FOXP2 and RBM15B was investigated through ChIP and dual-luciferase assays. Dual-luciferase reporter assay was used to verify the regulation of RBM15B on KDM4C via m6A modification. MeRIP was utilized to examine m6A enrichment on KDM4C mRNA. ChIP was employed to examine the enrichment of KDM4C and H3K9me3 on SLC7A11 promoters. Combined experiments investigated the role of the RBM15B/KDM4C axis in FOXP2-mediated ferroptosis and HCC cell proliferation. Xenograft models were developed in nude mice to validate the mechanism. FOXP2 expression was downregulated in HCC. FOXP2 overexpression significantly inhibited HCC cell proliferation and promoted ferroptosis. FOXP2 repressed RBM15B expression, suppressed the RBM15B-mediated m6A modification, inhibited KDM4C expression, upregulated H3K9me3 levels, and suppressed SLC7A11 expression, ultimately enhancing ferroptosis. Overexpression of RBM15B or KDM4C attenuated ferroptosis and reversed the suppression of HCC cell growth induced by FOXP2 overexpression. In conclusion, FOXP2 may promote ferroptosis and inhibit cell proliferation in HCC by decreasing SLC7A11 expression via the RBM15B/KDM4C axis in an m6A-dependent manner. - Source: PubMed
Publication date: 2026/02/09
Liu WenquanHe JiaqiZheng JingTang Qiqi - Lung cancer ranks as the leading cause of cancer-related mortality worldwide, characterised by complex molecular mechanisms and high therapeutic resistance. Ubiquitin-specific proteases, as core members of the deubiquitinating enzyme family, extensively participate in the initiation, progression, metastasis, and treatment resistance of lung cancer by regulating the stability of key proteins. Recent studies indicate that multiple Ubiquitin-Specific Proteases (USP) family members play pivotal roles in lung cancer: Ubiquitin-Specific Peptidase 7 (USP7) promotes proliferation and osimertinib resistance in non-small cell lung cancer by stabilising proteins such as ERβ, c-Abl, and KRAS; Ubiquitin-Specific Peptidase 9, X-linked (USP9X) mediates radiotherapy resistance by regulating KDM4C and REV1; USP10 influences cellular metabolism and chemotherapy sensitivity PTEN/AKT/mTOR and HDAC6 pathways; Ubiquitin-Specific Peptidase 14 (USP14) enhances tumour migration by regulating β-catenin and Acf7 stability; Ubiquitin-Specific Peptidase 22 (USP22) amplifies tumour stem cell properties and suppresses ferroptosis EGFR and BMI1 signalling; Ubiquitin-Specific Peptidase 35 (USP35) and Ubiquitin-Specific Peptidase 38 (USP38) respectively modulate apoptosis resistance and proliferation through BIRC3 and KLF5; while Ubiquitin-Specific Peptidase 39 (USP39) influences mitochondrial metabolism PDHA, thereby promoting tumour growth. This paper systematically reviews the mechanisms of action of the aforementioned USPs in multiple key signalling pathways, including KRAS, TGF-β/SMAD, ferroptosis, and DNA damage repair. It further explores the potential value of small-molecule inhibitors targeting USPs (such as P5091, IU1, and gentiopicroside) in reversing drug resistance, inducing apoptosis, and enhancing immunotherapy. Nevertheless, current research remains subject to certain limitations, including insufficient systematic and synergistic understanding of USP family members' functions, poor inhibitor selectivity and preclinical toxicity concerns, as well as unresolved functional heterogeneity across different molecular subtypes of lung cancer. This paper reviews the molecular mechanisms and targeting strategies of USPs in lung cancer based on a systematic literature search of PubMed and Web of Science databases. It further explores their potential applications in precision lung cancer therapy, providing theoretical foundations and directional guidance for future research. - Source: PubMed
Publication date: 2026/01/30
Shen XiaoyunWang RuoqiSu FeiGuo JuanjuanZhao DaYuan FangyunZhang TaoHou Xiaoming