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Findings suggest a putative novel mechanism for desipramine to modulate long-term potentiation through the regulation of the ephrinA3/EphA4 signaling pathway
The ephrin-A2/-A3 DKO mice have utility as a novel ASD model with an emphasis on sensory abnormalities and restricted, repetitive behavioral symptoms.
Ephrin-A2 and -A3 are negative regulators of the proliferative and neurogenic potentials of Muller cells.
Ephrin-A3 suppresses Wnt signaling to control retinal stem cell potency.
Downregulation of the EphA4 receptor via siRNA transfection reduced the repulsive effect of ephrin-A3, indicating that EphA4 mediates at least in part the repulsive effect of ephrin-A3.
Data show that a number of Eph receptors and ephrins were expressed in hematopoietic stem cells.
Ephrin-A3 is localized on astrocytic processes that envelop spines. Activation of EphA4 by ephrin-A3 caused spine retraction; inhibiting ephrin/EphA4 interactions distorted spine shape and organization in hippocampal slices.
Organ of Corti and spiral ganglion showed strong expression of ephrin-A3, ephrin-B2 and ephrin-B3. In lateral wall, ephrin-A3 and ephrin-B2 were strongly expressed. Ephrin-A3 was strongly expressed in utricular and saccular sensory epithelia.
Results demonstrate that neurons expressing different odorant receptors express different levels of ephrin-A3 and -A5 protein on their axons.
In mice deficient for ephrin-A2, A3 and A5, eye-specific inputs segregated but shape and location of eye-specific layers were profoundly disrupted. Ephrin-As and neural activity act together to control patterning of eye-specific retinogeniculate layers.
Whole-mount in situ hybridization revealed overlapping expression of the Epha1 receptor and its high-affinity ligands ephrin A1 (Efna1) and ephrin A3 (Efna3) in the primitive streak and the posterior paraxial mesoderm during early mouse development.
ephrin-A3 not only accelerates anagen development but also increases the density of hair follicles.
heparan sulfate modulates ephrin-A3/Eph signaling, suggesting a physiological role for heparan sulfate proteoglycans in the regulation of ephrin-A3-dependent biological processes
Results suggest that the interaction between neuronal EphA4 and glial ephrin-A3 bidirectionally controls synapse morphology and glial glutamate transport, ultimately regulating hippocampal function.
These results suggest that EphA4/ephrin-A3 signaling is a critical mechanism for astrocytes to regulate synaptic function and plasticity.
E2F3 and ephrin A3 are putative targets of miR-210, and their protein expression was up-regulated in the angiosarcoma cells
Results show that EFNA3 serves as a tumor suppressor in malignant peripheral nerve sheath tumor cells and it may play a critical role in the FAK signaling and VEGF-associated tumor angiogenesis pathway.
The present study provides evidence that microglia upregulates endothelial ephrin-A3 and ephrin-A4 to facilitate in vitro angiogenesis of brain endothelial cells, which is mediated by microglia-released TNF-alpha.
The interaction between ephrin-As, Eph receptors and integrin alpha3 is plausibly important for the crosstalk between Eph and integrin signalling pathways at the membrane protrusions and in the migration of brain cancer cells.
EphA2/ephrin-A3 interactions may play a role in the localization and network of Langerhans cells in the epithelium and in the regulation of their trafficking.
analysis of molecular surfaces in ephrin-A5 essential for a functional interaction with EphA3
Increasing ephrin-A expression enhances T-cell interactions not only with purified integrin ligands but also endothelial cells, while EphA activation down-regulates these interactions.
MicroRNA-210 modulates endothelial cell response to hypoxia and inhibits the receptor tyrosine kinase ligand Ephrin-A3.
EphA3 mutants with constitutively-released kinase domains efficiently support shedding, even when their kinase is disabled. Our data suggest that this phosphorylation-activated conformational switch of EphA3 directly controls ADAM-mediated shedding.
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.
, ephrin A3
, EHK1 ligand
, EPH-related receptor tyrosine kinase ligand 3
, eph-related receptor tyrosine kinase ligand 3
, ligand of eph-related kinase 3