Ask about this productRelated genes to: DDX39 antibody
- Gene:
- DDX39A NIH gene
- Name:
- DExD-box helicase 39A
- Previous symbol:
- DDX39
- Synonyms:
- DDXL, BAT1L, URH49
- Chromosome:
- 19p13.12
- Locus Type:
- gene with protein product
- Date approved:
- 2002-04-19
- Date modifiied:
- 2016-09-27
Related products to: DDX39 antibody
Related articles to: DDX39 antibody
- Esophageal squamous cell carcinoma (ESCC) is an aggressive malignancy with limited treatment options. Although radiotherapy remains a cornerstone of curative treatment, intrinsic and acquired radioresistance frequently lead to locoregional recurrence and disease progression. DDX39A, a DEAD-box RNA helicase, regulates RNA metabolism in diverse cellular contexts; however, its role in ESCC pathogenesis and therapeutic resistance remains unclear. - Source: PubMed
Publication date: 2026/04/15
Hui BeinaHu WeibinChen XinWang YingLi JingSun YuchenSun XuanziRen Juan - - Source: PubMed
Zhang YanXue ZhiweiZhang NaibinZhu YuehuaWu YanZhaoLv MeilinZhang ZhihanMu FeiyuXing WenchenTang ZiyiWang ChunjieXue ZhiyiZhou WenjingLiu XiaofeiLi XingangBjerkvig RolfHuang BinHan MingzhiWang JianWang Donghai - Glioblastoma (GB) is a highly complex ecosystem characterized by numerous interactions between tumor cells and the surrounding tumor microenvironment (TME). Splicing factors play a pivotal role in processing nascent pre-mRNA and are important in the progression of cancer, making them promising molecular targets. In this study, we demonstrate that the DEAD-box helicase 39 A (DDX39A), a RNA helicase with several important roles in RNA metabolism and cellular processes, is significantly upregulated in GB and is primarily expressed in tumor cells, leading to an immunosuppressive macrophage polarization. Through in vitro and in vivo studies, we demonstrate that reducing DDX39A expression in GB results in reduced tumor growth and invasion. Mechanistically, through RNA-seq and RIP-seq, we identified WISP1 as a critical downstream effector of DDX39A. DDX39A stabilizes WISP1 pre-mRNA through alternative splicing regulation, thereby activating the AKT signaling pathway. We further demonstrate that WISP1, when secreted by tumor cells, functions as a paracrine signaling molecule that promotes the development of immunosuppressive tumor-associated macrophages (TAMs). Additionally, we demonstrate that Fluphenazine hydrochloride binds to and inhibits DDX39A, thereby suppressing GB growth, invasion, and the immunosuppressive function of macrophages. DDX39A thus represents a potential candidate for glioma-targeted therapy. - Source: PubMed
Publication date: 2026/03/02
Zhang YanXue ZhiweiZhang NaibinZhu YuehuaWu YanZhaoLv MeilinZhang ZhihanMu FeiyuXing WenchenTang ZiyiWang ChunjieXue ZhiyiZhou WenjingLiu XiaofeiLi XingangBjerkvig RolfHuang BinHan MingzhiWang JianWang Donghai - The incidence of thyroid cancer is rising worldwide, underscoring the urgent need for novel molecular targets in the management of aggressive disease. This study identifies bystin-like protein (BYSL) as a previously unrecognized oncogenic driver in thyroid carcinoma. Comprehensive analyses of clinical specimens, established cell lines, and patient-derived tumor-like clusters revealed that BYSL is significantly upregulated in thyroid malignancies and is strongly correlated with adverse patient outcomes. Functional assays demonstrated that BYSL promotes tumor cell proliferation, migration, and invasion while suppressing apoptosis. Mechanistically, BYSL interacts directly with DEAD-box helicase 49 (DDX49) to form a functional protein complex that impairs the biogenesis of the tumor suppressor miR-145-5p by inhibiting its DICER-mediated processing. Dual knockdown of BYSL and DDX49 synergistically suppressed tumor growth and induced apoptosis in patient-derived tumor-like cell clusters, with these effects reversed by inhibition of miR-145-5p. Collectively, these findings demonstrate the BYSL-DDX49 complex as a pivotal modulator of thyroid cancer progression and underscore its promise as a therapeutic intervention for restoring tumor-suppressive pathways. - Source: PubMed
Publication date: 2025/12/19
Wang YueXing XiaoxiaoZhang DongpoSun TaoZhang YurenLi JunLiao DaixiangLi Junyi - Dilated cardiomyopathy (DCM) is a progressive myocardial disorder with limited therapeutic options. Recent studies suggest that metabolic reprogramming, including lactate accumulation and protein lactylation, contributes to heart failure pathogenesis, but their roles in DCM remain poorly defined. We analyzed the global burden of cardiomyopathy and myocarditis using GBD data and performed transcriptomic profiling using GSE120895 and GSE5406 datasets. Weighted gene co-expression network analysis (WGCNA), differential gene expression, and known lactylation-related genes (LRGs) were integrated to identify key targets. LASSO regression was applied to construct a diagnostic model. Validation was conducted in an Lmna transgenic mouse model using qRT-PCR, Western blot analysis, immunofluorescence, and biochemical assays. Global analysis showed the rising age-standardized prevalence of cardiomyopathy and myocarditis by 2021. Bioinformatics revealed 1988 DEGs in DCM, 11 of which overlapped with LRGs and WGCNA modules. LASSO modeling identified DDX39A, SPR, and HNRNPC as core diagnostic biomarkers. In vivo validation confirmed upregulation of these genes in Lmna mice. Elevated lactate and protein lactylation levels were detected, alongside increased NEFA, MDA, and oxidative stress markers, implicating lactylation in metabolic dysfunction. We identify DDX39A, SPR, and HNRNPC as novel lactylation-associated biomarkers of DCM and reveal a pathophysiological link between lactate-driven protein lactylation, oxidative stress, and cardiac dysfunction. These findings offer new molecular targets for DCM diagnosis and intervention. - Source: PubMed
Liu JiaLiu ChongYu JingjiaXu Kai