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
- Vemurafenib (VEM) is a BRAF inhibitor that improves the prognosis of melanoma, but acquired resistance represents a key limitation to its clinical efficacy. This study investigated the potential of A11, an Annexin A1 (ANXA1)-derived peptide, to enhance VEM efficacy in both VEM-sensitive and VEM-resistant melanoma cells. We evaluated the effects of A11 in melanoma through in vitro assays (including MTT, clonogenic survival, apoptosis, and cell cycle analysis) and in vivo xenograft models in nude mice. Furthermore, we mechanistically interrogated A11-mediated suppression of EphA2 expression and the downstream pS897-EphA2/AKT/ERK signalling pathway in resistant and parental cell lines via Western blotting and immunohistochemistry (IHC). Critically, our study demonstrates that A11 inhibits melanoma cell proliferation and reverses VEM resistance through EphA2 downregulation, consequently ablating this oncogenic pathway. This research highlights the promising application value of A11 in improving the efficacy of VEM treatment in melanoma, particularly in VEM-resistant melanoma. - Source: PubMed
Feng JuanHuang Xiao-PuZhang MingHuang WeiLu Shan-ShanXiao Zhi-QiangXie Zhi-HaiYi Hong - Keloids are pathological fibroproliferative skin disorders resulting from abnormal wound healing, characterized by excessive extracellular matrix (ECM) deposition and chronic local inflammation. While dermal fibroblasts are the primary effector cells in this process, the role of keloid keratinocytes (KKs) and their metabolic alterations in sustaining the pro-inflammatory and fibrotic microenvironment remains poorly understood. - Source: PubMed
Publication date: 2026/08/13
Li ZhaoheChen JiaZhao JingxiaYu XiaohanZhu HaoyueMa HuikeDi TingtingChen WeiwenWang YanLi Ping - EphA2 (ephrin type-A receptor 2) is a representative member of the Eph receptor tyrosine kinase family and is frequently overexpressed in a broad spectrum of malignant tumors. It participates in regulating tumor cell proliferation, migration, invasion, and angiogenesis through ligand-dependent and ligand-independent signaling pathways, thus emerging as a promising target for anticancer drug discovery. In recent years, extensive research has been carried out toward the discovery and optimization of small-molecule EphA2 inhibitors, covering a variety of chemical scaffolds with distinct mechanisms of action. This review provides a comprehensive overview of the research progress of EphA2-targeted small-molecule inhibitors reported to date. We systematically summarize their representative chemical scaffolds, structure-activity relationships, binding modes, and pharmacological profiles, and highlight the current challenges in selectivity, pharmacokinetic properties, and clinical translation. This review is expected to offer valuable guidance for the rational design and optimization of next-generation EphA2-targeted therapeutics. - Source: PubMed
Publication date: 2026/08/07
Yang LiyanHe JunXiao WenjingJia GuiqingShi Jianyou - The potential for using therapeutic antisense oligonucleotides (ASOs) has been hampered by a lack of understanding of how they enter cells and subsequently access their targets. Endocytosis contributes to ASO uptake, but the machinery mediating subsequent ASO trafficking to permit suppression of their target mRNAs has not been described. Here, we show that direct ASO engagement with a scavenger receptor (CD44) activates the ERK-RSK axis to promote serine phosphorylation of a receptor tyrosine kinase (EPHA2). Serine phosphorylation of EPHA2 permits endocytosis, trafficking, and accumulation of ASOs in nuclear-captured endosomes. These endosomes are then subject to lipid peroxidation and become leaky, allowing ASOs to escape and effectively suppress target mRNA expression. Inhibition of stress granule-mediated repair of these leaky endosomes further enhances ASO effectiveness. These data identify an endocytic route to the nucleus which may be exploited to maximize the effectiveness of ASO-mediated therapies. - Source: PubMed
Publication date: 2026/08/11
Marco SergiWalsh Peter JRevenko Alexey SSchmidt TobiasThomason Peter AMcGarry LynnMacLeod A RobertAnsel SonamTataran DinaBushell MartinBraconi ChiaraNorman Jim C - Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal cancers, primarily because late detection, a lack of effective therapies and an abundant desmoplastic reaction result in elevated proliferation, invasion and immune evasion. KRas is the most frequently mutated driver gene in PDAC and, while drugs are now available that target this GTPase, there remains a need for further pharmacological options to treat the disease. As a first step to identify potential targets, this study aimed to define the molecular environment of KRas using proximity proteomics. A KRas-biotin ligase chimera was stably expressed in several PDAC cell lines and organoids, and associating proteins identified following biotin addition, streptavidin affinity isolation and mass spectrometry (MS). Among the 126 proteins that were specifically associated in all cell lines, five integrin subunits and the receptor tyrosine kinase ephrin type-A receptor 2 (EphA2) were consistently enriched. Both classes of receptor have been previously implicated in both Ras signalling and desmoplastic responses. A range of protein biochemical and microscopic analyses confirmed the spatial association of integrin β1 and EphA2 with KRas. Cellular KRas levels were reduced following depletion of both integrin β1 and EphA2, and depletion of EphA2 inhibited KRas-dependent migration. Taken together, these findings highlight a ternary crosstalk between receptor tyrosine kinase, integrin and KRas signalling, which provides insight into PDAC progression and signposts potential therapeutic vulnerabilities. - Source: PubMed
Publication date: 2026/08/10
Fatima MahakHaider NasirCain Stuart AAcharya Bipul RChastney Megan RZha JunzheJones Matthew CWarwood StaceyKnight DavidO'Reilly Derek AHumphries Jonathan DGoult Benjamin TJørgensen ClausHumphries Martin J