Ask about this productRelated genes to: Arnt antibody
- Gene:
- ARNT NIH gene
- Name:
- aryl hydrocarbon receptor nuclear translocator
- Previous symbol:
- -
- Synonyms:
- HIF-1beta, bHLHe2
- Chromosome:
- 1q21.3
- Locus Type:
- gene with protein product
- Date approved:
- 1990-01-22
- Date modifiied:
- 2016-10-05
Related products to: Arnt antibody
Related articles to: Arnt antibody
- In breast cancer (BC), neoadjuvant chemotherapy (NAC) improves surgical options, and pathologic complete response (pCR) predicts better outcomes. Patients with residual disease (non-pCR) have higher recurrence risk, yet robust pretreatment biomarkers remain limited. - Source: PubMed
Publication date: 2026/08/06
Li QiangChen JinhaoYu WeiLi XunDeng Yuhua - Adipocyte depots throughout the body are physiologically and molecularly distinct. With age, adipocytes increase in and around aged thymi. Yet thymic adipocytes lack molecular characterization. We developed methods to isolate adipocyte nuclei from mouse thymi. Single-nucleus multi-omic analysis of male and female mice aged 4-9 months reveals that thymic adipocytes are heterogeneous, with two distinct populations. One subpopulation harbors a transcription and chromatin signature consistent with beige fat. Another subpopulation resembles classic white adipose tissue and expresses genes associated with epithelial-to-mesenchymal transition (EMT). Analysis of differentially open chromatin identifies binding sites for Foxn1 and HIF-1α/Arnt in the white adipose population, consistent with a thymic epithelial and/or hypoxic origin for these cells. Immunofluorescence confirmed the expression of UCP1 protein in cells in subcapsular cortical regions of the thymic parenchyma. This resource reveals a complex milieu of thymic adipocytes and identifies multiple avenues for probing their ontogeny, dynamics, and functional significance. - Source: PubMed
Publication date: 2026/08/11
Schwakopf JoonSyage Amber RFranzini AncaVarley Katherine ETantin Dean - Induction of programmed cancer cell death by selective aryl hydrocarbon receptor (AHR) ligands represents a promising strategy for developing novel anticancer therapeutics. In this study, we characterized the anticancer activity and underlying mechanism of the selective AHR ligand CGS-15943 in lung cancer cells. CGS-15943 potently inhibited the growth of lung cancer cell lines expressing high levels of AHR, whereas CRISPR-mediated knockout of AHR in H460 and H69AR cells markedly rescued cells from CGS-15943-induced cell death, demonstrating an essential role for AHR. To identify additional mediators of this response, we performed a genome-wide CRISPR knockout screen, which revealed eight enzymes involved in the heme biosynthesis pathway, three heme-containing enzymes, as well as AHR and its transcriptional partner ARNT, as critical determinants of CGS-15943-induced cell death. Transcriptomic analyses further showed that CGS-15943 induced AHR-dependent transcriptional programs enriched for oxidative stress and oxidized phospholipid response pathways. Together, these findings identify key components of the AHR signaling network that regulate a programmed heme-dependent cell death pathway and establish CGS-15943 as a promising lead compound for targeting AHR-positive lung cancers. - Source: PubMed
Publication date: 2026/08/10
Nguyen Bach DKolluri Siva K - Juvenile hormone (JH) is vital to insects. In , JH signals through a basic helix-loop-helix-PER-ARNT-SIM (bHLH-PAS) protein methoprene-tolerant (MET) and its paralog germ cell-expressed (GCE). Binding of JH to the PAS-B domain of MET or GCE triggers the assembly of a DNA-bound, transcriptionally active JH receptor (JHR) heterodimer comprising either MET or GCE and their partner taiman (TAI). Molecular mechanisms of the JHR complex activation remain unclear. Here, we use the GCE protein to address the presumably critical but as yet unexplored function of the other PAS domain (PAS-A) in JHR signaling. We show that charged amino acid residues, highly conserved within the PAS-A domain across insect and mammalian bHLH-PAS proteins, are required for JHR signaling in vitro and in vivo. Mutations at these sites do not affect the ability of GCE to bind JH to its PAS-B domain. However, they compromise the JH-induced nuclear import of GCE, its dissociation from the chaperone heat-shock protein HSP83, and dimerization with TAI, consequently preventing the DNA binding and transcriptional JHR activities. Functionality of the mutated GCE variants in developing flies is also impaired. Molecular modeling suggests that mutations of the charged GCE PAS-A residues alter the natural salt bridges critical for intra- and interdomain interactions. This in turn causes non-native configurations of both GCE PAS domains, making them incompatible with TAI dimerization and possibly augmenting GCE attachment to HSP83. These results suggest that JHR signaling critically depends on interactions between PAS-A and PAS-B domains which are allosterically coupled. - Source: PubMed
Publication date: 2026/08/06
Bittova LenkaTumova SarkaYatsenko MykolaMokhamatam Raveendra BabuTuma RomanJindra Marek - Prostate cancer (PCa) is one of the most common cancers in males, and its treatment remains challenging due to the tumor microenvironment (TME) with immunosuppressive properties and limited response to anti-PD-1 therapy. Gut microbiota-derived metabolites have recently emerged as modulators of cancer immunometabolism, however, their role in PCa progression and immunotherapy is poorly understood. Here we found that indole-3-lactic acid (ILA), a metabolite produced by Lactobacillus plantarum, exerted dual anti-tumor effects on PCa cells and the TME. Mechanistically, ILA activates the aryl hydrocarbon receptor (AHR), and the resulting AHR/ARNT heterodimer translocates into the nucleus and binds to the promoter of ASF1B. This heterodimer then recruits the HDAC1/2-NuRD complex to reduce H3K27ac levels and suppress ASF1B expression. ASF1B binds to specific residues of ENO1 via its N-terminal core domain and enhances ENO1 enzymatic activity. ILA-induced downregulation of ASF1B impairs this interaction, reduces ENO1 activity, and suppresses the PI3K/Akt pathway, thereby inhibiting the malignant phenotypes of PCa cells. Concurrently, ILA decreased CXCL8 secretion by inhibiting the PI3K/Akt/NF-κB pathway, enhancing CD8 T cell infiltration and M1 macrophage polarization, thereby remodeling the TME. Additionally, ILA synergized with anti-PD-1 therapy to more effectively suppress tumor growth. These findings reveal a novel mechanism by which gut microbiota-derived metabolites regulate PCa progression and immunometabolism, positioning ILA as a potential therapeutic agent to improve PCa treatment. - Source: PubMed
Publication date: 2026/08/06
Wang ZhengshiJia ChengyouLiu YongqiangRixiati YoulutuziayiZhang WentaoMao ShiyuChen HaotianZou LibinYe ChenShen BingYao Xudong