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Findings suggest a putative novel mechanism for desipramine to modulate long-term potentiation through the regulation of the ephrinA3/EphA4 (zeige EPHA4 Proteine) signaling pathway
The ephrin-A2 (zeige EFNA2 Proteine)/-A3 DKO mice have utility as a novel ASD (zeige GUSB Proteine) model with an emphasis on sensory abnormalities and restricted, repetitive behavioral symptoms.
Ephrin-A2 (zeige EFNA2 Proteine) and -A3 are negative regulators of the proliferative and neurogenic potentials of Muller cells.
Ephrin-A3 suppresses Wnt (zeige WNT2 Proteine) signaling to control retinal stem cell potency.
Downregulation of the EphA4 (zeige EPHA4 Proteine) receptor via siRNA transfection reduced the repulsive effect of ephrin-A3, indicating that EphA4 (zeige EPHA4 Proteine) mediates at least in part the repulsive effect of ephrin-A3.
Data show that a number of Eph (zeige EPHA1 Proteine) receptors and ephrins were expressed in hematopoietic stem cells.
Ephrin-A3 is localized on astrocytic processes that envelop spines. Activation of EphA4 (zeige EPHA4 Proteine) by ephrin-A3 caused spine retraction; inhibiting ephrin/EphA4 (zeige EPHA4 Proteine) interactions distorted spine shape and organization in hippocampal slices.
Organ of Corti and spiral ganglion showed strong expression of ephrin-A3, ephrin-B2 (zeige EFNB2 Proteine) and ephrin-B3 (zeige EFNB3 Proteine). In lateral wall, ephrin-A3 and ephrin-B2 (zeige EFNB2 Proteine) 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 (zeige NRP1 Proteine) 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.
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 (zeige EFNA4 Proteine) to facilitate in vitro angiogenesis of brain endothelial cells, which is mediated by microglia-released TNF-alpha (zeige TNF Proteine).
The interaction between ephrin-As, Eph (zeige EPHA1 Proteine) receptors and integrin alpha3 is plausibly important for the crosstalk between Eph (zeige EPHA1 Proteine) and integrin signalling pathways at the membrane protrusions and in the migration of brain cancer cells.
EphA2 (zeige EPHA2 Proteine)/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 (zeige EFNA5 Proteine) essential for a functional interaction with EphA3 (zeige EPHA3 Proteine)
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 (zeige RET Proteine) ligand Ephrin-A3.
EphA3 (zeige EPHA3 Proteine) 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 (zeige EPHA3 Proteine) 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