Elk1 (Phospho_Ser389) Antibody
- Known as:
- Elk1 (Phospho_Ser389) Antibody
- Catalog number:
- E011037-2
- Product Quantity:
- 100ug
- Category:
- Antibodies
- Supplier:
- EnoGene
- Gene target:
- Elk1 (Phospho_Ser389) Antibody
Related genes to: Elk1 (Phospho_Ser389) Antibody
- Gene:
- ELK1 NIH gene
- Name:
- ETS transcription factor ELK1
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- Xp11.23
- Locus Type:
- gene with protein product
- Date approved:
- 1989-06-30
- Date modifiied:
- 2019-01-21
Related products to: Elk1 (Phospho_Ser389) Antibody
Related articles to: Elk1 (Phospho_Ser389) Antibody
- Androgen receptor (AR)-dependent prostate cancer (PCa) cells require co-activation of ELK1 by AR to activate a critical set of cell cycle and mitosis genes, regardless of hormone - sensitivity. A small molecule antagonist (KCI807) that inhibits AR-dependent growth by selectively binding to AR and blocking its association with ELK1 is limited as a drug by auto-induced metabolism. Using structure-activity data, consistent with modeling a physically mapped KCI807 binding pocket, we developed a new class of compounds with a different core structure comprising 5-Hydroxy-2-(3-hydroxyphenyl)-1-methylquinolin-4(1H)-one (KCI830), with variable N- substituents. The compound with a N-2,2,2-trifluoroethyl substitution (KCI838) was the fastest acting and most potent inhibitor of AR-dependent cell growth and colony formation in PCa model cells, including exclusively AR splice variant-dependent and other enzalutamide-resistant cells, without affecting growth of AR-negative cell lines. Critical tests were conducted to establish that KCI838 recapitulates the previously elucidated mode of action of KCI807. KCI838 selectively inhibited ELK1-dependent vs. androgen response element (ARE)-driven promoter and gene activation by AR. KCI838 blocked AR binding to ELK1 tested by BRET assay. Increasing the total cellular AR by ∼2-fold using ectopic AR expression caused the predicted change in drug dose-response profile for growth, implicating AR as the exclusive target for the activity of KCI838. KCI838's molecular scaffold conferred reduced enzyme induction in primary human hepatocytes and weakened interactions with human UGT1A1 and CYP1A2. In mice bearing an aggressive, enzalutamide-resistant patient-derived PCa tumor xenograft characteristically overexpressing prostatic acid phosphatase, daily bolus injections of a soluble 3'phosphate monoester prodrug of KCI838 (KCI838PME) progressively inhibited tumor growth, concomitant with tumor accumulation of active hydrophobic drug, without significant toxicity. Additionally, ALZET osmotic pumps were used to establish proof-of-concept for reversible anti-tumor activity of KCI838PME administered in a low dose, controlled release mode. The results warrant investigation of KCI838PME in a controlled-release formulation, to treat PCa that is resistant to current AR-targeted therapies while obviating the need for testosterone suppression. - Source: PubMed
Publication date: 2026/05/29
Soave ClairePolin LisaDucker CharlesOng VyKim SeonghoPardy LukeLi JingBao XunHuang YanfangShaw Peter EKhupse RahulRatnam Manohar - Acute myeloid leukemia (AML) remains a heterogeneous hematologic malignancy with frequent therapeutic resistance and relapse. Although miR-2110 is upregulated in AML, its functional role and downstream mechanism remain unclear. - Source: PubMed
Publication date: 2026/05/25
Li YaChen YingHuang AoshuangZhan YunNi MingZhang FengqiXu ShaofeiLi Yanju - Bladder cancer (BC) is one of the most common malignancies of the urinary system, and chemoresistance remains a major obstacle limiting the clinical efficacy of cisplatin-based chemotherapy. Elucidating the mechanisms underlying cisplatin resistance may facilitate the identification of potential therapeutic targets and ultimately improve patient outcomes. In this study, we found that Y-box binding protein 1 (YBX1) was upregulated in bladder cancer tissues with poor chemotherapeutic response as well as in cisplatin-resistant bladder cancer cell lines, where it promoted tumor cell proliferation and invasion. Functional assays demonstrated that depletion of YBX1 significantly enhanced cisplatin sensitivity in both in vitro and in vivo. Mechanistically, elevated YBX1 expression was associated with reduced ferroptosis sensitivity in cisplatin-resistant cells. Although YBX1 induced autophagy and was accompanied by a reduction in glutathione peroxidase 4 (GPX4) protein levels, the overall enhancement of intracellular antioxidant capacity in resistant cells may partially offset the increased susceptibility to ferroptosis caused by GPX4 degradation. Furthermore, we identified the transcription factor ELK1 as an upstream regulator that transcriptionally upregulates YBX1, while YBX1 may contribute to the cisplatin-resistant phenotype through activation of the p62-NRF2-associated antioxidant pathway. Collectively, these findings highlight a critical role of YBX1 in cisplatin resistance and suggest that targeting YBX1 may represent a promising strategy for overcoming cisplatin-based chemoresistance in bladder cancer. - Source: PubMed
Publication date: 2026/06/01
Luo YaoMa JunhaiWang ChengXiong WeiZhang XingxingZhang BiaoFu YuqiangZhang XiaojunWang JienengZhang HelinZheng YanghuangLu JianzhongShang Panfeng - Brain metastasis represents an advanced complication in non-small cell lung cancer (NSCLC), characterized by therapeutic resistance and dismal survival outcomes. Although astrocytes are known to influence tumor progression within the brain microenvironment, their prognostic significance and mechanistic contributions to NSCLC brain metastasis (NSCLC-BM) remain largely unresolved. In this study, we analyze brain metastatic tumors from 66 patients with NSCLC and demonstrate that high infiltration of astrocytes is significantly associated with reduced overall survival. Functional assays reveal that astrocytes enhance the stemness of metastatic tumor cells, a phenotype that is significantly attenuated by silencing astrocytic monocarboxylate transporter 1 (MCT1), thereby blocking lactate uptake. Mechanistically, lactate reprograms astrocytes to release extracellular vesicles enriched in miR-8085, which downregulates the E3 ubiquitin ligase TRIM67 in tumor cells. This suppression stabilizes the transcription factor ELK1 through inhibition of ubiquitin-mediated degradation, promoting stemness maintenance and tumorigenic capacity. Clinically, low TRIM67 and high ELK1 expression correlate with poorer survival in patients with NSCLC-BM. Together, our findings uncover a novel lactate-induced miR-8085/TRIM67/ELK1 signaling cascade that drives brain metastasis progression and highlight potential prognostic biomarkers and therapeutic targets for patients with NSCLC involving the brain. - Source: PubMed
Publication date: 2026/05/31
Peng HaiqinTanzhu GuilongShi WenXiao GangZeng QianChen LiuWan XinJing DiDeng HaibinMarti Thomas MichaelFu JunZhou Rongrong - Premature ovarian insufficiency (POI) not only affects fertility, but also has a profound impact on women's general health, mental health and quality of life. This research was designed to explain the function and mechanism of wild-type and edited miR-483-5p in POI. Western blot analysis and RT-qPCR were utilized to evaluate gene expression. Human granulosa cell activities were assessed via CCK-8, colony formation, EdU and TUNEL assays. FSH, E2, and AMH levels were measured using ELISA. Commercially available kits were obtained to detect glucose uptake and ROS level. The targets of miRNAs were confirmed through dual-luciferase reporter assay. High editing level of miR-483-5p induced by ADAR1 enzyme was related to high FSH level and low E2, AMH levels in POI patients. Functionally, miR-483-5p restrained granulosa cell proliferation and elevated apoptosis. Interestingly, A-to-I RNA editing aggravated miR-483-5p effect on granulosa cell activity. In vivo experiment also demonstrated that edited and wild-type miR-483-5p exacerbated POI by regulating granulosa cell proliferation and apoptosis. Mechanically, A-to-I RNA editing alters the targets of miR-483-5p. And ed-miR-483-5p obtains novel target ESR2 and loses ELK1. Specifically, miR-483-5p promoted POI progression by intensifying ELK1-mediated oxidative stress. Edited miR-483-5p aggravated POI development by downregulating ESR2-mediated hormone synthesis and glycometabolism. A-to-I RNA editing reinforces the pathogenicity of miR-483-5p in POI by regulating hormone synthesis and glucose metabolic mechanism through altering its target ELK1 as ESR2. - Source: PubMed
Publication date: 2026/05/26
Ma NieyingXu KaijieLiu JuanWang Zhize