UPF1 antibody - middle region (ARP36350_P050)
- Known as:
- UPF1 (anti-) - middle region (ARP36350_P050)
- Catalog number:
- arp36350_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- UPF1 antibody - middle region (ARP36350_P050)
Related genes to: UPF1 antibody - middle region (ARP36350_P050)
- Gene:
- UPF1 NIH gene
- Name:
- UPF1 RNA helicase and ATPase
- Previous symbol:
- RENT1
- Synonyms:
- HUPF1, KIAA0221, NORF1, pNORF1, smg-2
- Chromosome:
- 19p13.11
- Locus Type:
- gene with protein product
- Date approved:
- 1997-02-11
- Date modifiied:
- 2019-01-25
Related products to: UPF1 antibody - middle region (ARP36350_P050)
Related articles to: UPF1 antibody - middle region (ARP36350_P050)
- Exosomes serve as critical mediators in driving therapeutic resistance among tumor cells by delivering bioactive molecules, including circular RNAs (circRNAs). Through bioinformatics mining of public databases, we identified circ_0097112 as a circular RNA implicated in icotinib resistance in lung adenocarcinoma (LUAD). Our subsequent experiments revealed that circ_0097112 was specifically upregulated in EGFR-TKI-resistant cells and in their secreted exosomes. To elucidate the functional role of circ_0097112 in EGFR-TKI-resistant lung cancer cells, we conducted in vitro experiments demonstrating that circ_0097112 promotes proliferation and concomitantly suppresses apoptosis in LUAD cells. Confocal microscopy revealed that drug-resistant lung cancer cells encapsulate circ_0097112 within exosomal vesicles and horizontally transfer this cargo to drug-sensitive recipient cells, thereby conferring acquired resistance. To delineate the mechanistic basis by which circ_0097112 confers drug resistance, we integrated bioinformatic prediction with experimental validation, including RNA pull-down and RNA immunoprecipitation assays. Our findings demonstrated that circ_0097112 directly interacts with UPF1 protein to assemble a functional complex, thereby suppressing decay of oncogenic NRAS. This molecular event consequently activates downstream RAF/MAPK signaling, attenuating apoptosis while promoting cellular proliferation and drug resistance. Collectively, this study reveals the pivotal involvement of the circ_0097112/UPF1/NRAS axis in driving EGFR-TKI resistance in LUAD and offers a new theoretical basis for targeting circ_0097112 to reverse EGFR-TKI resistance. - Source: PubMed
Publication date: 2026/06/06
Chen ZiyuanWang YuXu YierWang ShuaibinXu ZhiyuanTang XingpingKang BailamuZhou ChengweiMeng Xiaodan - - Source: PubMed
Publication date: 2026/05/15
Wang YixiaoSun HuiHou XiaoyaXing WenluXu ZhengguoZhang QingsongYang Bo - Ferroptosis induction is a novel strategy for treating human cancers; however, the detailed mechanisms underlying ferroptosis resistance during nasopharyngeal carcinoma (NPC) progression remain unclear. Herein, we explored the role and potential mechanism of LINC00839 in ferroptosis resistance of NPC cells. We found that the expression levels of LINC00839 and transcription factor ets-like kinase 1 (ELK1) were elevated in NPC tissues, which were associated with a poor survival of NPC patients. Overexpression of LINC00839 or ELK1 reduced the sensitivity of NPC cells to ferroptosis-inducing drugs. Mechanistically, ELK1 directly bound to LINC00839 promoter to contribute to its transcription. Subsequently, LINC00839 destabilized ring finger and CHY zinc finger domain-containing 1 (RCHY1) mRNA through recruitment of up-frameshift 1 (UPF1), and consequently inhibited ubiquitination and degradation of DJ-1 protein. LINC00839 knockdown induced NPC cell ferroptosis, which was neutralized by RCHY1 depletion or DJ-1 overexpression. Knockdown of ELK1 or LINC00839 exerted synergistic roles with Erastin or ferroptosis-inducing chemotherapeutic drug Sorafenib to enhance ferroptosis, thereby delaying tumor growth in vivo. In summary, this study reveals that ELK1-mediated transcription activation of LINC00839 promotes ferroptosis resistance of NPC cells by destabilizing RCHY1 mRNA and subsequent repressing DJ-1 ubiquitination and degradation. These findings provide potential therapeutic targets for overcoming ferroptosis resistance in NPC. - Source: PubMed
Publication date: 2026/05/14
Liu FengLi YuLiu HuaiTang LingFang ShuWenWang XiChen PanWang HuiBao MeiHuaHe BinShengGuo Zhen - RNA-binding proteins (RBP) interact with mRNA untranslated regions containing cis-regulatory elements to govern mRNA localization, stability, and translational efficiency. Among these trans-regulatory factors, RNA helicase UPF1 is a central factor which play a role in multiple mRNA decay pathways, including nonsense-mediated mRNA decay (NMD). NMD is triggered when an exon-junction complex (EJC) is located downstream of a premature termination codon. However, in some cases, NMD can be activated in an EJC-independent manner through mechanisms involving the 3'UTR. In the present study, we focused on the GABARAPL1 3'UTR, as previous studies had shown that this region plays a key role in NMD targeting, although the underlying molecular mechanism had not yet been elucidated. Unlike canonical NMD targets such as SC35, we found that the chemical inhibition of eIF4AIII helicase activity did not affect GABARAPL1 transcript levels, indicating that this transcript is regulated through its 3'UTR via an EJC-independent mechanism. We therefore investigated the potential presence of cis-regulatory element within the 3'UTR of GABARAPL1 which can regulate mRNA and protein levels in a UPF1-dependent manner. Furthermore, we identified a conserved RNA region spanning nucleotides 364-421 involved in GABARAPL1 targeting and used biochemical analysis to demonstrate the direct binding of UPF1 and eIF4AIII to this RNA region, to analyse its secondary structure in solution, and to map the protein-binding sites. By complementing these approaches with molecular modelling, we showed that this stem-loop adopts a stable global fold but a local flexibility and dynamic behaviour properties. Together, our results support the role of UPF1 and eIF4AIII as specific regulators of GABARAPL1 transcript and reveal a novel RNA regulatory element within its 3'UTR, which provides a completely unexpected binding site for these factors. - Source: PubMed
Publication date: 2026/05/08
Mercier ChloéBaudin MaëlysFiorini FrancescaHognon CéciliaDurand JulesPerez ValériePeigney AnneLebars IsabelleHervouet ÉricPeixoto PaulDelage-Mourroux RégisFraichard AnnickGuittaut MichaëlBaguet Aurélie - Diabetic foot ulcer (DFU) is a severe and debilitating complication of diabetes with limited effective therapeutic strategies, and persistent oxidative stress and inflammation are the core pathological factors leading to its impaired wound healing. RNA-binding protein UP frameshift 1 (UPF1) is implicated in modulating oxidative stress pathways, yet its regulatory role and underlying mechanism in DFU-associated oxidative stress remain largely unelucidated. This study aims to explore the function of UPF1 in oxidative stress during DFU pathogenesis and identify its related molecular regulatory axis, so as to provide novel therapeutic targets for DFU management. Human dermal fibroblasts (HDFs) were exposed to 30 mM high glucose (HG) to simulate diabetic conditions. The results showed that HG stimulation increased cytochrome P450 family 1 subfamily A member 1 (CYP1A1) and early growth response 1 (EGR1) expression, exacerbating oxidative stress and inflammation in HDFs. EGR1 knockdown or CYP1A1 inhibition attenuated these effects. Mechanistically, EGR1 transcriptionally activated CYP1A1, while UPF1 bound to and destabilized EGR1 mRNA. As expected, UPF1 upregulation rescued HG-induced inflammation and oxidative stress in HDFs, whereas concurrent EGR1 overexpression abolished this protective effect. In conclusion, UPF1 exerts a protective role in HG-stressed HDFs by degrading EGR1 mRNA, which in turn suppresses the transcriptional activation of CYP1A1 and subsequent CYP1A1-mediated oxidative stress and inflammation, thus uncovering a novel UPF1-EGR1-CYP1A1 regulatory axis in DFU pathogenesis. These core findings not only enrich the molecular understanding of oxidative stress regulation in DFU but also provide promising novel therapeutic targets for DFU management. - Source: PubMed
Publication date: 2026/05/07
Qiu Zhi-YangMa Yun-LeiZhang Yao-XueFu JiaXu Wei-ChengKuang Shao-JiaXu Jia-QinLiang Zun-Hong