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Ephrin B2

Ephrin-B2, EFNB2
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 EFNB class ephrin which binds to the EPHB4 and EPHA3 receptors. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: EphB4, Eph, Ephrin-B1, CAN, V1a
Papers on Ephrin-B2
Bradykinin receptors and EphB2/EphrinB2 pathway in response to high glucose-induced osteoblast dysfunction and hyperglycemia-induced bone deterioration in mice.
Liu et al., Xi'an, China. In Int J Mol Med, Feb 2016
Moreover, the mRNA and protein expression levels of bradykinin receptor B1 (BK1R)/bradykinin receptor B2 (BK2R) and EphB2/EphrinB2 were significantly decreased in the osteoblasts following exposure to high glucose.
Chondrocytic EphrinB2 promotes cartilage destruction by osteoclasts in endochondral ossification.
Sims et al., Melbourne, Australia. In Development, Feb 2016
EphrinB2 is a receptor tyrosine kinase expressed by osteoblasts and growth plate chondrocytes that promotes osteoblast differentiation and inhibits osteoclast formation.
Fetal liver hematopoietic stem cell niches associate with portal vessels.
Frenette et al., United States. In Science, Feb 2016
After closure of the umbilical inlet at birth, portal vessels undergo a transition from Neuropilin-1(+)Ephrin-B2(+) artery to EphB4(+) vein phenotype, associated with a loss of periportal Nestin(+)NG2(+) cells and emigration of HSCs away from portal vessels.
Interrogating cellular fate decisions with high-throughput arrays of multiplexed cellular communities.
Schaffer et al., Berkeley, United States. In Nat Commun, Dec 2015
Our results suggest a potential signalling hierarchy between Delta-like 1 and ephrin-B2 ligands, as neural stem cells adopt the Delta-like 1 phenotype of stem cell maintenance on simultaneous presentation of both signals.
Androgen Modulates Functions of Endothelial Progenitor Cells through Activated Egr1 Signaling.
Yang et al., Suzhou, China. In Stem Cells Int, Dec 2015
Angiogenesis-related genes like Egr-1, Vcan, Efnb2, and Cdk2ap1 were identified to be regulated upon DHT treatment.
Periostin: A Downstream Mediator of EphB4-Induced Osteogenic Differentiation of Human Bone Marrow-Derived Mesenchymal Stem Cells.
Dai et al., Chongqing, China. In Stem Cells Int, Dec 2015
Treatment with ephrinB2-FC significantly increased the expression of POSTN in MSCs, and the inhibition of EphB4 could abrogate this effect.
Why increased nuchal translucency is associated with congenital heart disease: a systematic review on genetic mechanisms.
Haak et al., Amsterdam, Netherlands. In Prenat Diagn, Jun 2015
Fifteen candidate genes involved in both cardiac and lymphatic development were identified: Adrenomedullin; Chicken ovalbumin upstream promoter-transcription factor 2 (COUP-TFII); Cyp51; Ephrin-B2; Forkhead box protein C2 (Foxc2); Nuclear factor of activated T cells, cytoplasmic 1 (Nfatc1); Neurofibromatosis type 1 (Nf1); Phosphoinositide 3-kinase encoding isoform p110α (Pik3ca); Podoplanin; Prospero-related homeobox 1 (Prox1); T-box 1 (Tbx1); Tyrosine kinase with immunoglobulin-like and endothelial growth factor-like domains 1 (Tie1); vascular endothelial growth factor (Vegf)-A; Vegf receptor-3 (Vegfr-3); and Vascular endothelial zinc finger 1 (Vezf1).
Direct cell-cell contact with the vascular niche maintains quiescent neural stem cells.
Parrinello et al., Tübingen, Germany. In Nat Cell Biol, 2014
Mechanistically, endothelial ephrinB2 and Jagged1 mediate these effects by suppressing cell-cycle entry downstream of mitogens and inducing stemness genes to jointly inhibit differentiation.
Multiple myeloma mesenchymal stromal cells: Contribution to myeloma bone disease and therapeutics.
Garayoa et al., Salamanca, Spain. In World J Stem Cells, 2014
Importantly, pMSCs also readily contribute to MBD by promoting OC formation and activity at various levels (i.e., increasing RANKL to OPG expression, augmenting secretion of activin A, uncoupling ephrinB2-EphB4 signaling, and through augmented production of Wnt5a), thus further contributing to OB/OC uncoupling in osteolytic lesions.
Regulation of signaling interactions and receptor endocytosis in growing blood vessels.
Adams et al., Münster, Germany. In Cell Adh Migr, 2013
During growth and tissue regeneration but also in many pathological settings, these vascular networks expand, which is critically controlled by the receptor EphB4 and the ligand ephrin-B2.
Multivalent ligands control stem cell behaviour in vitro and in vivo.
Schaffer et al., Berkeley, United States. In Nat Nanotechnol, 2013
The ectodomain of ephrin-B2, normally an integral membrane protein ligand, was conjugated to a soluble biopolymer to yield multivalent nanoscale conjugates that potently induce signalling in neural stem cells and promote their neuronal differentiation both in culture and within the brain.
[Effects of bidirectional EphB4-EphrinB2 signaling on bone remodeling].
Bao et al., Nanjing, China. In Zhongguo Gu Shang, 2013
EphrinB2 is expressed on osteoblasts and EphB4 is expressed on osteoclasts.
Spatial regulation of VEGF receptor endocytosis in angiogenesis.
Adams et al., Münster, Germany. In Nat Cell Biol, 2013
aPKC phosphorylates Dab2, a clathrin-associated sorting protein that, together with the transmembrane protein ephrin-B2 and the cell polarity regulator PAR-3, enables VEGF receptor endocytosis and downstream signal transduction.
Henipavirus infections: lessons from animal models.
Horvat et al., Lyon, France. In Pathogens, 2012
These three, negative-sense single-stranded RNA viruses, are hosted by fruit bats and use EphrinB2 receptors for entry into cells.
T cell-specific deletion of EFNB2 minimally affects T cell development and function.
Luo et al., Montréal, Canada. In Mol Immunol, 2012
results suggest the involvement of EFNB2 in thymocyte development; however, heavy redundancy among Eph/EFN family members prevents the occurrence of detrimental phenotypes in the T cell compartment caused by T cell-specific EFNB2 gene null mutation
BMP9 induces EphrinB2 expression in endothelial cells through an Alk1-BMPRII/ActRII-ID1/ID3-dependent pathway: implications for hereditary hemorrhagic telangiectasia type II.
Hughes et al., Irvine, United States. In Angiogenesis, 2012
in an in vitro model of HHT2, loss of Alk1 blocks BMP9 signaling, resulting in reduced EphrinB2 expression, enhanced VEGFR2 expression, and misregulated EC sprouting and anastomosis
Blocking ephrinB2 with highly specific antibodies inhibits angiogenesis, lymphangiogenesis, and tumor growth.
Martínez-Torrecuadrada et al., Madrid, Spain. In Blood, 2012
Specific Ab-based ephrinB2 targeting may represent an effective therapeutic strategy to be used as an alternative or in combination with existing antiangiogenic drugs for treating patients with cancer and other angiogenesis-related diseases.
Contextual learning increases dendrite complexity and EphrinB2 levels in hippocampal mouse neurons.
Bevilacqua et al., Roma, Italy. In Behav Brain Res, 2012
The results of this study suggested that rapid accumulation of EphrinB2 in hippocampal CA1 neurons is involved in the behavioural and cellular modifications induced by contextual fear conditioning.
Novel strategy for selection of monoclonal antibodies against highly conserved antigens: phage library panning against ephrin-B2 displayed on yeast.
Jin et al., Ithaca, United States. In Plos One, 2011
Monoclonal antibody developed in this study may be used as a reagent to probe ephrin-B2 distribution in normal as well as in pathological conditions and to antagonize ephrin-B2 interaction with EphB4 for basic science and therapeutic applications.
Ephrin Bs are essential components of the Reelin pathway to regulate neuronal migration.
Acker-Palmer et al., Frankfurt am Main, Germany. In Nature, 2011
Notably, compound mouse mutants (Reln(+/-); Efnb3(-/-) or Reln(+/-); Efnb2(-/-)) and triple ephrin B1, B2, B3 knockouts show neuronal migration defects that recapitulate the ones observed in the neocortex, hippocampus and cerebellum of the reeler mouse.
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