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In a model of temporal lobe epilepsy, Ephrin-A4 and Ephrin-A5 (show EFNA5 Proteins) increase in the hippocampus in a spatiotemporal course.
ephrin-A4 plays an important role in retinal NV and is a potential target against retinal NV. The proangiogenic function of ephrin-A4 may be linked to its crucial role in the VEGF (show VEGFA Proteins) signaling pathway.
Downregulation of the EphA4 (show EPHA4 Proteins) receptor via siRNA transfection reduced the repulsive effect of ephrin-A3 (show EFNA3 Proteins), indicating that EphA4 (show EPHA4 Proteins) mediates at least in part the repulsive effect of ephrin-A3 (show EFNA3 Proteins).
LIM homeodomain proteins control axon pathways topographic projections in the limb through control of EphA receptors and ephrin-A ligands in motor neurons and limb mesenchymal cells.
Ephrin A4 receptor in the thalamus and ephrin A4 in the cerebral cortex control intra-areal topographic mapping of thalamocortical axons.
Study present for the first time in vitro and in vivo evidence suggesting that the major role of two ephrin A4 isoforms in chronic lymphocytic leukemia could be related with a non-previously described mechanism of survival linked to extravasation strongly dependent on integrin signaling.
The present study provides evidence that microglia upregulates endothelial ephrin-A3 (show EFNA3 Proteins) and ephrin-A4 to facilitate in vitro angiogenesis of brain endothelial cells, which is mediated by microglia-released TNF-alpha (show TNF Proteins).
The interaction between ephrin-As, Eph (show EPHA1 Proteins) receptors and integrin alpha3 is plausibly important for the crosstalk between Eph (show EPHA1 Proteins) and integrin signalling pathways at the membrane protrusions and in the migration of brain cancer cells.
The cytoplasmic pattern of ephrin A4 could identify a subgroup of primary osteosarcoma patients with a high liability for progression, poor prognosis, and inferior response to chemotherapy.
This provides genetic evidence that Twist1 (show TWIST1 Proteins), Msx2 and Efna4 function together in boundary formation and the pathogenesis of coronal synostosis.
CLL B-cells showed a more heterogeneous Eph (show EPHA1 Proteins)/EFN profile, specially EFNA4, EphB6 (show EPHB6 Proteins) and EphA10 (show EPHA10 Proteins). EphB6 (show EPHB6 Proteins) and EFNA4 were further related with the clinical course of CLL.
EFNA4-EphA2 (show EPHA2 Proteins) interactions are involved in Chronic lymphocytic leukemia cell trafficking between blood and the tissues
This gene encodes a member of the ephrin (EPH) family. The ephrins and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. This gene encodes an EFNA class ephrin. Three transcript variants that encode distinct proteins have been identified.
, EPH-related receptor tyrosine kinase ligand 4
, eph-related receptor tyrosine kinase ligand 4
, ligand of eph-related kinase 4