Ask about this productRelated genes to: EphA2 antibody
- Gene:
- EPHA2 NIH gene
- Name:
- EPH receptor A2
- Previous symbol:
- ECK
- Synonyms:
- -
- Chromosome:
- 1p36.13
- Locus Type:
- gene with protein product
- Date approved:
- 1991-08-07
- Date modifiied:
- 2016-10-05
Related products to: EphA2 antibody
Related articles to: EphA2 antibody
- Targeting the Transforming Growth Factor-β (TGF-β) pathway to reverse the immunologically "cold" tumor microenvironment (TME) of pancreatic ductal adenocarcinoma (PDAC) remains clinically unsuccessful, warranting novel therapeutic strategies. - Source: PubMed
Publication date: 2026/05/01
Bansod Sapana PHung-Po Chen TimothySomani Vikas KLi LinGeng YutongWang YuBulle AshenafiModekurty SuneetaKnolhoff Brett LFields Ryan CRuzinova Marianna BDeNardo David GLim Kian-Huat - Tyrosine kinase inhibitors (TKIs), such as sorafenib, lenvatinib, and regorafenib, serve as the mainstay targeted therapies for advanced hepatocellular carcinoma (HCC), yet resistance severely limits their clinical benefits. This study aimed to elucidate the role of CXCR4 in promoting vasculogenic mimicry (VM) to drive TKI resistance and to explore the natural chalcone flavokawain A (FKA) as a novel CXCR4-targeting agent to overcome this challenge. Utilizing comprehensive experimental approaches-including transcriptome sequencing, MTT, transwell and 3D-tubule formation assays, western blotting, molecular docking, cellular thermal shift assay (CETSA), and a subcutaneous xenograft model-we confirmed that sorafenib (0-8 μM) elevated CXCR4, consistent with our prior reports, and first revealed a similar upregulation occurred following exposure to lenvatinib (0-10 μM) and regorafenib (0-2 μM), with CXCR4 further enriched in TKI-resistant cells. CXCR4 overexpression promoted VM formation and reduced TKI sensitivity, while its knockdown suppressed VM and restored TKI responsiveness. Mechanistically, CXCR4 facilitated VM through the Snail/E-cadherin/Vimentin and VE-cadherin/EphA2/MMP-14/MMP-2/Laminin5γ2 pathways. TKI-resistant cells with upregulated CXCR4 exhibited a pronounced VM phenotype, including enhanced proliferation, migration, invasion, and VM. CXCR4 depletion attenuated these VM hallmarks and resensitized resistant cells to TKIs. FKA disrupted the VM phenotype by directly targeting CXCR4, and synergized with TKI to inhibit HCC growth in vitro and in vivo, with its efficacy being CXCR4-dependent. Collectively, our findings suggest that CXCR4 promotes VM to drive TKI resistance and reveal that FKA, as a potential CXCR4 inhibitor, represents a promising therapeutic strategy in combination with TKIs to overcome resistance in HCC. - Source: PubMed
Publication date: 2026/04/29
Zheng NingChen YanLuo ShijieLuo JialinBahediyaer AyixuwakeSu ShizhenWu LixianWang Jichuang - The MYC oncoprotein is a key driver of various cancers and is particularly relevant in triple-negative breast cancer (TNBC), where its dysregulated activation promotes aggressive tumor growth, metastasis, and resistance to treatment. Despite its central role in cancer development, directly targeting MYC proves challenging due to its disordered structure and lack of druggable pockets. Synthetic lethality, a strategy that exploits secondary vulnerabilities in MYC-driven cancer cells, offers a promising therapeutic approach. In this study, we establish a chemogenetic screening platform to identify compounds that selectively target MYC-driven cancer cells. We screen a library of approximately 600 kinase inhibitors and identify ALW-II-41-27, an EphA2 inhibitor, as a top hit. ALW-II-41-27 demonstrates strong MYC-selective cytotoxicity and induces apoptosis in MYC-activated cells through the intrinsic apoptotic pathway. Importantly, this apoptotic response is independent of p53 status, which is frequently inactivated by loss-of-function mutations in MYC-driven cancers. In vivo, ALW-II-41-27 effectively inhibits tumor growth in MDA-MB-231 and MDA-MB-468 TNBC xenografts without apparent toxicity. These findings highlight EPHA2 as a novel synthetic lethal partner of MYC and suggest that targeting EPHA2 could offer a promising therapeutic strategy for MYC-driven TNBC. - Source: PubMed
Publication date: 2026/04/22
Ye MengWang ZixinWang YuxinSun ZheLuan Xin - Alveolar macrophages (AMs) are central to host defense against Pneumocystis, mediating organism clearance while also contributing to lung inflammation. EphA2, a transmembrane receptor that binds fungal β-glucans, has emerged as a regulator of host-pathogen interactions, but its role in AM responses during Pneumocystis pneumonia (PCP) is unknown. - Source: PubMed
Publication date: 2026/04/23
Kottom Theodore JPellegrino MadelineAchilonu ConradStelzig Kimberly ELimper Andrew H - Erythropoietin-producing hepatocellular receptor A2 (EphA2) is overexpressed in various malignant tumors and represents a promising target for cancer-specific imaging and therapy. However, many therapeutics (as well as imaging probes) targeting overexpressed EphA2 are limited by efficacy and safety concerns. We aimed to develop and preclinically evaluate a novel single-photon emission computed tomography (SPECT) probe, [In]In-DTPA-EphA2-57-1, based on a newly generated anti-EphA2 monoclonal antibody, EphA2-57-1. The antibody was conjugated with DTPA (p-SCN-Bn-DTPA) and radiolabeled with In, achieving a radiochemical purity of 97.3%. In vitro, in EphA2-expressing cells (EphA2-positive U87MG glioblastoma cells), [In]In-DTPA-EphA2-57-1 demonstrated uptake and a high internalization fraction, reaching 74.9% at 24 h. Although DTPA conjugation reduced the apparent binding affinity compared with the native antibody, efficient receptor-mediated internalization contributed to sustained cellular retention. In vivo biodistribution studies in U87MG tumor-bearing mice revealed selective tumor accumulation (6.9-8.8%ID/g) and favorable tumor-to-blood and tumor-to-muscle ratios, which increased over time. Notably, the tumor-to-blood ratio reached 2.4 ± 0.8 and 3.4 ± 0.6 on Days 4 and 7, respectively, post-injection. Blocking with excess unlabeled antibody significantly reduced tumor uptake, confirming EphA2-specific targeting in vivo. SPECT enabled a clear and persistent visualization of EphA2-expressing tumors; however, a relatively high hepatic uptake was observed. [In]In-DTPA-EphA2-57-1 exhibited lower blood retention and higher tumor contrast at earlier time points than did the previously reported probe [In]In-BnDTPA-EphA2-230-1, reflecting improved imaging performance. These results indicate that [In]In-DTPA-EphA2-57-1 is a promising SPECT probe for the noninvasive assessment of EphA2 expression. Additionally, the findings may inform future EphA2-targeted theranostic applications. - Source: PubMed
Publication date: 2026/04/19
Sasaki MinonKimura HiroyukiIwasawa TakumiOshige SatoKawashima HidekazuOmokawa MarinaNaito YukiYagi YusukeKato KazunoriYasui Hiroyuki