Ask about this productRelated genes to: HNRPH1 antibody
- Gene:
- HNRNPH1 NIH gene
- Name:
- heterogeneous nuclear ribonucleoprotein H1
- Previous symbol:
- HNRPH1
- Synonyms:
- hnRNPH
- Chromosome:
- 5q35.3
- Locus Type:
- gene with protein product
- Date approved:
- 1997-08-28
- Date modifiied:
- 2017-01-12
Related products to: HNRPH1 antibody
Related articles to: HNRPH1 antibody
- Hypertension is a major risk factor for cardiovascular diseases. RNA N6-methyladenosine (mA) modification is closely linked to hypertension pathogenesis, but key mA-related factors that regulate blood pressure remain unclear. This study aims to identify these regulators and evaluate their therapeutic potential. - Source: PubMed
Publication date: 2026/08/25
Chen ZhenzhenZhang HaizengYang QiaoxiFan LuyunDong XilanLing QianhuiGuo XinruYue FengkaiCui JiaruiTang YanGeng BinCai Jun - Chemotherapy resistance remains a significant challenge in colorectal cancer (CRC) treatment, with disrupted redox balance playing a central role. Here we identify CHTOP as a key regulator of oxidative stress and chemoresistance in CRC. Mechanistically, CHTOP promotes NRF2 transcriptional activity by recruiting the SENP3-containing 5FMC complex to deSUMOylate NRF2, thereby sustaining HO-1 expression and redox balance. Notably, CHTOP expression itself is tightly controlled by a feedback mechanism. The p52 isoform of PSIP1 inhibits CHTOP expression by interfering with HNRNPH1-mediated splicing, leading to CHTOP degradation via nonsense-mediated decay (NMD). Conversely, elevated oxidative stress stabilizes SENP3, which promotes deSUMOylation and degradation of p52, thereby relieving p52-mediated suppression of CHTOP expression. This establishes an oxidative stress-SENP3-p52-CHTOP feedback loop that fine-tunes CHTOP levels. In 5-FU-resistant CRC cells, CHTOP downregulation shifts cells into an elevated oxidative stress state, which correlates with reduced 5-FU sensitivity. Notably, either restoring CHTOP expression or further depleting CHTOP disrupts this redox balance and resensitizes resistant cells to 5-FU. These findings suggest that modulating CHTOP expression may offer a therapeutic strategy to overcome chemoresistance in CRC through redox regulation. - Source: PubMed
Publication date: 2026/08/15
Li JingLi XiaopengZhao ChenyeWu PeiwenHu WeibinZhao XuMa YuanDong ZepengYuan HangChen ShihuiChen ZiluLu JingWang WeiSun XuejunZhang QinMu Mingchao - Lung adenocarcinoma (LUAD) remains a leading cause of cancer-related death, underscoring the need for an improved molecular understanding. This study investigated the regulatory mechanism of the long non-coding RNA deoxyguanosine kinase antisense RNA 1 (DGUOK-AS1) in LUAD. DGUOK-AS1 was significantly upregulated in LUAD cells and serum samples, and its elevated expression showed a preliminary association with LUAD. Functional experiments demonstrated that DGUOK-AS1 promoted LUAD proliferation and migration both and , partly by acting as a competing endogenous RNA for miR-2467-5p to modulate PRMT5 expression. Mechanistically, RNA-binding motif protein 15 (RBM15) enhanced DGUOK-AS1 stability through m6A modification, which in turn enabled heterogeneous nuclear ribonucleoprotein H1 (HNRNPH1) binding in an m6A-dependent manner via its RNA recognition motif 3 (RRM3) domain, promoting degradation. RBM15 knockdown attenuated the malignant phenotype through the miR-2467-5p/PRMT5 axis. These findings reveal an m6A-dependent mechanism governing DGUOK-AS1 stability and provide insights into its contribution to LUAD progression. - Source: PubMed
Publication date: 2026/08/07
Yang MenghaoWu JiaenLi YoujieLi HuiZhang HongrongLiang YanWang QinWang PingyuYu YuanSun GuangbinFeng JiankaiLiu WenwenXie ShuyangSun Hongfang - NK cells are promising candidates for adoptive cell therapy; however, their proliferative capacity and functional persistence may be limited. Genetic modification with hTERT enhances their proliferative potential, while co-expression of the iCASP9 suicide gene provides a safety mechanism based on late-stage apoptosis induction by chemical dimerizer (CID). Whether hTERT overexpression interferes with iCasp9-mediated cell death remains unclear, and the non-canonical functions of telomerase in this context are poorly understood. This study served a dual purpose: to assess the efficacy of the iCasp9 "suicide switch" in NK cells, and to investigate a non-canonical role of telomerase in NK cell-mediated evasion from cell death. Here, we demonstrate that hTERT-modified NK cells exhibit significant resistance to CID-induced apoptosis, an effect independent of telomerase catalytic activity, as confirmed using a dominant-negative hTERT (DN-hTERT) mutant. Transcriptomic profiling revealed that both CID-resistant iCasp9-NK cells and hTERT-iCasp9-NK cells share common gene expression signatures: upregulation of cell cycle-associated genes and downregulation of splicing-related factors, including HNRNPH1 and SNRPD3, accompanied by shared patterns of alternative splicing. Among apoptosis-related transcripts, BIRC3, which encodes c-IAP-2, a direct inhibitor of caspase 9, was consistently elevated in both "resistant" and "survived" NK cells. However, shRNA-mediated knockdown of BIRC3 failed to restore sensitivity to CID, indicating that BIRC3 upregulation is not the unique determinant of resistance and suggesting involvement of additional compensatory pathways. Overall, our findings define specific transcriptional signatures associated with evasion of NK cells from iCasp9-mediated apoptosis, implying the contribution of cell cycle progression, enhanced anti-apoptotic signaling, and alterations in splicing regulation, and highlighting the complex role of non-canonical hTERT functions in these adaptations. In the rational design of next-generation gene-modified NK cell therapies with improved safety and persistence, the uncovered insights should be considered. - Source: PubMed
Publication date: 2026/06/12
Palamarchuk Anastasia IUstiuzhanina Maria OVelichinskii Rodion AVavilova Julia DGrechikhina Maria VKovalenko Elena IStreltsova Maria A - Acute kidney injury (AKI) lacks disease-modifying therapies, partly because cell type-specific injury programs remain incompletely resolved and tissue mechanisms are not readily translated into clinically accessible biomarkers. We constructed a cross-scale, multi-omics atlas to prioritize candidate regulator linking renal injury circuitry with urine-detectable signals. Human single-cell, bulk, and spatial transcriptomics were integrated with mouse renal ischemia-reperfusion injury (RIRI) kidney proteomics and clinical urine proteomics. Overlap of differentially expressed genes and differentially abundant proteins nominated candidates, which were ranked by a random forest model. Immune remodeling was assessed by deconvolution and pathway enrichment, with spatial localization supported by reference-based deconvolution. Therapeutic tractability was explored by structure-based virtual screening, molecular docking, molecular dynamics simulation, and cellular thermal shift assay (CETSA). TRIM28 was evaluated in HK-2 hypoxia/reoxygenation (H/R) and mouse RIRI models using genetic perturbation, expression validation, and in vitro pharmacologic evaluation. Integration converged on five genes (TRIM28, HNRNPH1, ARHGEF10L, C1RL, and UCHL3), with TRIM28 showing the highest feature importance and links to inflammatory, immune, metabolic, and proliferative programs. AKI exhibited intensified intercellular communication and an innate-skewed immune landscape. TRIM28 was robustly upregulated in HK-2 H/R and mouse RIRI kidneys and was also directly detected in the human urine proteome. In HK-2 cells, TRIM28 knockdown dampened, whereas overexpression amplified, IL-17-linked inflammatory signaling and apoptotic responses. Docking-prioritized HY-N10592 improved viability, reduced H/R-associated TRIM28 induction, IL-17-linked output, and apoptotic marker activation, and showed CETSA-supported cellular engagement of TRIM28. This integrative framework prioritizes TRIM28 as a candidate regulator linking tubular injury mechanisms with clinically relevant urinary signals and nominates HY-N10592 as a candidate chemical tool with CETSA-supported cellular target engagement for further mechanistic and in vivo evaluation in AKI. - Source: PubMed
Publication date: 2026/06/10
Wang KangyuWang HaoZhang YalongZhang ZijianXu ChanghongZhao HongMa JiaxuanMan JiangweiYang Li