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High EPHA3 expression is associated with tumor growth and angiogenesis in gastric cancer.
To investigate the relationship between five EPHA3 single nucleotide polymorphisms (SNPs) and Nonsyndromic Cleft Lip With or Without Cleft Palate (NSCL/P), EPHA3 SNPs (rs7650466, rs1398197, rs17801309, rs1054750, and rs7632427) were genotyped. The rs7650466 T allele was associated with the incidence of NSCL/P as well as with protective and dominant effects in both conditions.
Although EPHA3 was reported to be one of the most frequently mutated genes in colorectal tumors, our studies using inducible isogenic cell line systems, mouse models and large human tumor collections, did not reveal a major role of this EPH receptor on proliferation/motility/invasion of cancer cells, tumor initiation/progression/metastasis in mouse models or survival of colorectal cancer patients.
The interaction of AR and SP1 contributes to regulate EPHA3 expression.
Findings suggest that EPH receptor A3 (EphA3) plays an important role in the pathogenesis of multiple myeloma (MM).
Study shows that EphA3 is highly overexpressed in multiple myeloma (MM) and provides evidence that EphA3 plays an important role in MM angiogenesis.
Results indicate that EphA3 protein expression is reduced in clear-cell renal cell carcinoma, suggesting the possibility that this receptor functions as a tumor suppressor in this disease.
EphA3 promotes malignant transformation of colorectal epithelial cells by upregulating oncogenic signaling pathways.
Data indicate that EPHA3 is involved in regulating the multidrug resistance (MDR) of small cell lung cancer (SCLC) via PI3K/BMX/STAT3 signaling and may be a therapeutic target in SCLC.
PTP-PEST regulates EphA3 activation both by affecting cytoskeletal remodelling and through its direct action as a PTP controlling EphA3 phosphorylation.
This study showed that EPHA3 gene involved in neuronal growth and cerebellum development and associated with neurological and psychological disorders.
A novel association between the EPHA3 deletion and prostate cancer risk was observed in Finnish individuals.
the structure of the ligand-binding domain of the EphA3 receptor in complex with its preferred ligand, ephrin-A5, is reported.
EphA3 forms dimers in the absence of ligand binding.
Data indicate that hypoxia increased EphA3 receptor (EphA3) mRNA expression in EphA3+ endometrial multipotent mesenchymal stromal cells (eMSCs).
EphA3 was induced by PC-1 and contributed to the malignant progression of prostate cancer
Based on the knowledge that EPHA4 has been previously shown to rescue SOD1 transgenic mice from ALS phenotype and prolongs survival, EPHA3 may be a promising candidate for therepuetic interventions
EphA3 may represent a novel candidate marker for patient prognosis as well a molecular target for HCC therapy.
EPHA3 mutations may promote tumorigenesis only when key senescence-inducing pathways have been inactivated.
EphA3 may play important roles in the angiogenesis and prognosis of gastric carcinoma
study delineates a mechanism in which NCAM promotes ephrin-A5-dependent clustering of EphA3 through interaction of the NCAM Ig2 domain and the EphA3 CRD, stimulating EphA3 autophosphorylation and RhoA signaling necessary for growth cone repulsion in GABAergic interneurons in vitro, which may extend to remodeling of axonal terminals of interneurons in vivo.
Ephrin-A3 has a role in promoting and maintaining slow muscle fiber identity during postnatal development and reinnervation
the physiological role of the putative lung cancer tumor suppressor EPH receptor A3, is reported.
Mutations in EPHA family genes may cause cleft lip/palate with functional redundancy between family members perhaps at play.
ephrinA5/EphA3 triggers proteolysis of the neural cell adhesion molecule (NCAM) by the metalloprotease a disintegrin and metalloprotease (ADAM)10 to promote growth cone collapse in neurons from mouse neocortex.
EphA3 receptor localized only in neuronal cells of the hippocampus was enhanced without transcriptional regulation during synaptic plasticity through activation of the nicotinic acetylcholine receptor.
Data show that a number of Eph receptors and ephrins were expressed in hematopoietic stem cells.
Neocortical expression of Epha3 during development remains stable in the absence of cellular contacts and thalamocortical connections.
Retrograde labeling studies in EphA3(-/-) embryos and adults indicate that EphA3 is not necessary to direct motor axons to axial muscle targets.
A discrepancy between mRNA and protein expression was found between early and later developmental stages, suggesting that EphA3 might regulate the formation of various neuronal networks in the developing brain.
results indicate that EphA3 plays a crucial role in the development and morphogenesis of the cells that give rise to the atrioventricular valves and septa.
in axial nerves, establishment of discrete afferent & efferent pathways depends on signaling between coextending sensory & motor projections; the axon-axon interactions require motor axonal EphA3/EphA4 activated by cognate sensory axonal ephrin-A ligands
This gene belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. This gene encodes a protein that binds ephrin-A ligands. Two alternatively spliced transcript variants have been described for this gene.
EPH-like kinase 4
, TYRO4 protein tyrosine kinase
, eph-like tyrosine kinase 1
, ephrin type-A receptor 3
, human embryo kinase 1
, tyrosine-protein kinase receptor ETK1
, ephrin receptor EphA3
, EPH receptor A3
, ephrin type-A receptor 3-like
, tyrosine-protein kinase TYRO4
, tyrosine-protein kinase receptor REK4
, receptor tyrosine kinase