XRCC5 antibody - C-terminal region (ARP34121_T100)
- Known as:
- XRCC5 (anti-) - C-terminal region (ARP34121_T100)
- Catalog number:
- arp34121_t100
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- XRCC5 antibody - C-terminal region (ARP34121_T100)
Related genes to: XRCC5 antibody - C-terminal region (ARP34121_T100)
- Gene:
- XRCC5 NIH gene
- Name:
- X-ray repair cross complementing 5
- Previous symbol:
- -
- Synonyms:
- KU80, KARP-1, Ku86, KUB2
- Chromosome:
- 2q35
- Locus Type:
- gene with protein product
- Date approved:
- 1992-01-22
- Date modifiied:
- 2016-06-02
Related products to: XRCC5 antibody - C-terminal region (ARP34121_T100)
Related articles to: XRCC5 antibody - C-terminal region (ARP34121_T100)
- Ribosome biogenesis (RiboSis) serves as an important foundation for the malignant progression of tumors. In this study, bioinformatics was employed to evaluate the association between RiboSis and lung adenocarcinoma (LUAD) and to preliminarily uncover potential therapeutic targets. Analysis of DepMap CRISPR/RNAi data revealed that 73% of RiboSis genes are essential for cancer cell survival. RNA-seq analysis demonstrated that RiboSis remains continuously active in multiple types of tumors and is closely related to unfavorable clinical outcomes. Through Cox and LASSO-Cox regression analyses, DDX56, XRCC5, and FAM207A were identified as risk genes associated with LUAD. We further examined their co-mutation patterns with the top 10 most frequently mutated genes in LUAD. The results revealed a significant co-occurrence phenomenon among these three genes. Enrichment analysis linked these genes to the p53 pathway, cell cycle regulation, and immune cell infiltration. The CellMiner database revealed that these three genes are associated with resistance to multiple anticancer drugs. Subsequently, LUAD cell lines with knockdown of DDX56, XRCC5, and FAM207A, respectively, were constructed. The impacts of these three risk genes on the migration and invasion abilities of tumor cells were evaluated using CCK-8, Transwell, and cell scratch assays. The results showed that the knockdown of these genes could significantly inhibit tumor migration and invasion. In summary, this study preliminarily indicates that DDX56, XRCC5, and FAM207A may be potential therapeutic targets for LUAD, providing new strategies for the clinical treatment of LUAD. - Source: PubMed
Publication date: 2026/06/09
Yin NanchangRen Hong - Epithelial-mesenchymal transition (EMT) plays a crucial role in cancer progression and is driven by EMT-inducing transcription factors (EMT-TFs). Although core EMT-TFs are well characterized, transcription factors that couple EMT to malignant phenotypes remain incompletely defined. Here, we identified C/EBPγ as a novel inducer of EMT in lung adenocarcinoma cells by examining regions of extensive histone H3 lysine 4 trimethylation occupancy that are often a hallmark of cellular identity. Ectopic expression of C/EBPγ induced mesenchymal-like morphologies and EMT-associated gene-expression profiles, whereas its RNAi knockdown attenuated EMT. Interestingly, domain mapping showed that the leucine zipper domain, but not the DNA-binding domain, was essential for C/EBPγ-mediated EMT, indicating a novel DNA-binding-independent mechanism involving critical partner proteins. Co-immunoprecipitation and mass spectrometry identified C/EBPβ and the non-homologous end joining (NHEJ) factors XRCC5 and XRCC6 as C/EBPγ-interacting proteins. C/EBPγ promotes EMT, at least in part, by antagonizing the EMT-suppressive activity of C/EBPβ. In parallel, C/EBPγ promoted XRCC6 recruitment to etoposide-induced DNA double-strand break (DSB) sites, enhanced NHEJ activity, facilitated DSB repair, and increased survival under genotoxic stress induced by anticancer drug treatment. Collectively, these findings indicate that C/EBPγ may play a role in linking EMT-associated transcriptional changes with enhanced DNA repair capacity, which could have implications for chemoresistance in lung adenocarcinoma. - Source: PubMed
Publication date: 2026/06/02
Terashima MinoruSuzuki RyusukeSuphakhong KusumaNishimura TatsunoriEerdunduleng Takino TakahisaHorike Shin-IchiNishiuchi TakumiTange ShoichiroIshimura AkihikoVoon Dominic CSashida GoroSuzuki Takeshi - Arsenic poisoning significantly elevates the risk of cancer and other chronic illnesses. The goal of this research is to identify important genes whose expression changes in response to arsenic toxicity, and the molecular pathways affected by arsenic, using computational analysis of arsenic toxicity profiles. This approach will computationally identify and analyze genes whose expression changes in response to arsenic, thereby elucidating the heightened risk of carcinogenesis in arsenic-exposed individuals. This work employed high-throughput arsenic toxicity profiles to computationally identify and analyze expressed genes (DEGs) differentially in Affymetrix microarray datasets from the Gene Expression Omnibus (GEO) database, which were screened using the GEO2R program. A protein-protein interaction (PPI) network was constructed using STRING to elucidate the functional links between these DEGs and DNA repair genes. Interactions between the seven central genes (E2F1, EXO1, EZH2, FEN1, HIST1H3A, POLA1, and TIMELESS) and the repair genes PARP1, NBN, PMS1, MSH3, XRCC5, XRCC6, MGMT, and MLH1 were discovered. We employed the DAVID and Enrichr-KG platforms to investigate the functions of these genes and their associations with cellular and molecular processes in greater detail. Two hundred eighty-one non-synonymous single-nucleotide polymorphisms (nsSNPs) in the 07 genes linked to arsenic toxicity were found using the COSMIC database. Based on our analysis, mutations in E2F1, EXO1, EZH2, FEN1, HIST1H3A, POLA1, and TIMELESS can hinder DNA repair mechanisms, ultimately leading to cancer. Our computational analysis demonstrated that these non-synonymous SNPs can affect gene function, potentially altering protein stability and activity. Furthermore, according to Metal-Protein docking and protein-protein docking, these genes and their mutations appear to affect interactions with repair proteins substantially. Specific dietary consumption may lessen the detrimental effects of arsenic poisoning on protein function. We hypothesized that the mutations might be reversed by attaching particular molecules to these mutants. The protective effects of six curcumin compounds were examined using molecular docking with AutoDock 4.2.6 to assess protein dynamics and binding interactions. Optimal complexes were selected for dynamics simulation using GROMACS, and potential strategies for long-term cancer prevention related to arsenic exposure were identified. - Source: PubMed
Parida LuckyPatel Trupti N - Radiotherapy is a mainstay of cancer treatment, yet its efficacy is still substantially restricted due to radioresistance. The mechanisms underlying radioresistance remain elusive, impeding drug development and therapeutics. Here, using a high-throughput random gene perturbation method based on piggyBac transposon, we screened and identified CABLES1, an adaptor protein, as a key regulator of tumor radioresistance. The function of CABLES1 in radioresistance was further validated in multiple human cell lines in vitro and a mouse xenograft model in vivo. High expression of CABLES1 is significantly correlated with radioresistance in cancer patients. Mechanistically, CABLES1 interacts with XRCC6/XRCC5 heterodimer and activates DNA-PKcs by promoting DNA-PK holoenzyme formation, thus facilitating the efficiency of nonhomologous end-joining (NHEJ) repair and radioresistance. Notably, YTHDF1 recognizes METTL14-deposited mA modification on CABLES1 mRNA to enhance its translation in response to ionizing radiation (IR), thereby sustaining the elevation of NHEJ repair capacity and radioresistance. Through high-throughput screening of a small molecule library, we showed that theaflavin 3,3'-digallate (TF-3) specifically disrupts the CABLES1-XRCC6 interaction, thereby sensitizing cancer cells to radiotherapy. Together, our study unveils the molecular mechanism by which CABLES1 potentiates tumor radioresistance, providing a novel synthetic lethal strategy for targeting cancer. - Source: PubMed
Publication date: 2026/05/09
Li ChangzhiTang XianchaoZeng ZimiYang LiqianCao FangZhu HaiyanZhu LiqingShen JieBian XiaocuiWang LibinLiu YangMao FengbiaoChang DeJiao PengtaoWang HaiyingLi Kailong - To investigate RNF146 expression in triple-negative breast cancer (TNBC) and its role in modulating sensitivity to the PARP inhibitor olaparib, we analyzed RNF146 expression and its association with patient survival using The Cancer Genome Atlas (TCGA) database. Functional studies were performed in 4T1 cells with stable RNF146 overexpression generated via lentiviral transduction. Cell viability and clonogenic capacity were assessed by CCK-8 and colony formation assays, respectively. An orthotopic nude mouse model was used to evaluate tumor growth and therapeutic response in vivo. Potential substrates of RNF146 were screened using the BioGRID database and validated by Western blot analysis. RNF146 expression was significantly reduced in breast cancer tissues, including TNBC, compared with normal tissues, and low RNF146 expression was associated with poor overall survival. RNF146 overexpression markedly enhanced olaparib sensitivity in vitro and significantly inhibited tumor growth while promoting apoptosis in vivo. XRCC5 was identified as a potential substrate of RNF146 and was confirmed to be downregulated by RNF146 both in vitro and in tumor tissues. These findings indicate that RNF146 enhances olaparib sensitivity in TNBC, at least in part, through downregulation of XRCC5, and suggest that RNF146 may serve as a prognostic biomarker and a potential therapeutic target for improving PARP inhibitor efficacy in TNBC. - Source: PubMed
Publication date: 2026/03/31
Chen MengTang YezhenXiao TingtingMa HongningSun HuihuiWang ZhijunZhao Wei