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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 (show NHLH1 Proteins)/P), EPHA3 SNPs (rs7650466, rs1398197, rs17801309, rs1054750, and rs7632427) were genotyped. The rs7650466 T allele was associated with the incidence of NSCL (show NHLH1 Proteins)/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 (show EPHA1 Proteins) 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 (show PSG1 Proteins) 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 (show MOK Proteins), 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 (show PIK3CA Proteins)/BMX (show BMX Proteins)/STAT3 (show STAT3 Proteins) signaling and may be a therapeutic target in SCLC.
PTP-PEST (show PTPN12 Proteins) regulates EphA3 activation both by affecting cytoskeletal remodelling and through its direct action as a PTP (show SLC25A3 Proteins) controlling EphA3 phosphorylation.
study delineates a mechanism in which NCAM (show NCAM1 Proteins) promotes ephrin-A5 (show EFNA5 Proteins)-dependent clustering of EphA3 through interaction of the NCAM (show NCAM1 Proteins) Ig2 domain and the EphA3 CRD (show CRX Proteins), stimulating EphA3 autophosphorylation and RhoA (show RHOA Proteins) 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 (show EFNA3 Proteins) 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.
ephrinA5/EphA3 triggers proteolysis of the neural cell adhesion molecule (NCAM (show NCAM1 Proteins)) by the metalloprotease (show ADAMTS7 Proteins) a disintegrin and metalloprotease (ADAM)10 (show ADAM10 Proteins) 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 (show EPHA1 Proteins) 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.
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