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Academic literature on the topic 'Ephrin'

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Published: 4 June 2021
Last updated: 6 July 2024

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Journal articles on the topic "Ephrin"

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PRESTOZ, LAETITIA, ELLI CHATZOPOULOU, GREGORY LEMKINE, NATHALIE SPASSKY, BARBARA LEBRAS, TETSUSHI KAGAWA, KATZUHIRO IKENAKA, BERNARD ZALC, and JEAN-LÉON THOMAS. "Control of axonophilic migration of oligodendrocyte precursor cells by Eph–ephrin interaction." Neuron Glia Biology 1, no. 1 (February 2004): 73–83. http://dx.doi.org/10.1017/s1740925x04000109.

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The migration of oligodendrocyte precursor cells (OPCs) is modulated by secreted molecules in their environment and by cell–cell and matrix–cell interactions. Here, we ask whether membrane-anchored guidance cues, such as the ephrin ligands and their Eph receptors, participate in the control of OPC migration in the optic nerve. We postulate that EphA and EphB receptors, which are expressed on axons of retinal ganglion cells, interact with ephrins on the surface of OPCs. We show the expression of ephrinA5, ephrinB 2 and ephrinB3 in the migrating OPCs of the optic nerve as well as in the diencephalic sites from where they originate. In addition, we demonstrate that coated EphB2-Fc receptors, which are specific for ephrinB2/B3 ligands, induce dramatic changes in the contact and migratory properties of OPCs, indicating that axonal EphB receptors activate ephrinB signaling in OPCs. Based on these findings, we propose that OPCs are characterized by an ephrin code, and that Eph–ephrin interactions between axons and OPCs control the distribution of OPCs in the optic axonal tracts, and the progress and arrest of their migration.
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Kuang, Shao-qing, Zhi-Hong Fang, Gonzalo Lopez, Weigang Tong, Hui Yang, and Guillermo Garcia-Manero. "Eph Receptor Tyrosine Kinases and Ephrin Ligands Are Epigenetically Inactivated in Acute Lymphoblastic Leukemia and Are Potential New Tumor Suppressor Genes in Human Leukemia." Blood 110, no. 11 (November 16, 2007): 2128. http://dx.doi.org/10.1182/blood.v110.11.2128.2128.

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Abstract The Eph (erythroprotein-producing hepatoma amplified sequence) family receptor tyrosine kinases and their ephrin ligands (ephrins) are involved in a variety of functions in normal cell development and cancer. We have identified several members of this family as potential targets of aberrant DNA methylation using Methylated CpG Island Amplification (MCA) / DNA promoter microarray technology. This is of importance as there are no prior reports of potential Eph receptor or Ephrin epigenetic inactivation in human leukemia. To further investigate the role of Eph receptor and ephrin family genes in leukemia, we have analyzed their DNA methylation status in a panel of 23 leukemia cell lines and 65 primary ALL patient samples. Aberrant DNA methylation of 9 of these genes (EPHA4, EPHA5, EPHA6, EPHB2, EPHB3, EPHB4, EphrinA5, Ephrin B2, and EphrinB3) was detected in multiple leukemia cell lines but not in normal samples by bisulfite pyrosequencing. In ALL patient samples, the frequencies of DNA methylation detected in the promoter regions of these genes ranged from 23% to 87% for EPHA4, EPHA5, EPHA6, EPHB2, EPHB3, EPHB4, EphrinA5, Ephrin B2, and EphrinB3. Expression analysis of 3 of these genes (EPHA5, EPHB4 and Ephrin B2) in leukemia cell lines by real-time PCR further confirmed methylation associated gene silencing. Treatment of methylated/silenced cell lines with DNA methyltransferase inhibitor 5′-aza-2′-deoxycytidine resulted in gene re-expression. Forced overexpression of EPHB4 using a lentivirus transduction system in Raji cell lines resulted in decreased cell proliferation and adhesion-independent cell growth, as well as in an increase in staurosporine induction of apoptosis. In addition, EPHB4 overexpression resulted in a significant downregulation of phosphorylated Akt pathway but had no effect on mitogen-activated protein kinase pathway. In summary, we describe for the first time the epigenetic suppression of Ephrin receptors and their ligands in human leukemia, indicating that these genes may be potential tumor suppressors in leukemia. Targeting of these pathways may result in the development of new potential therapies and biomarkers for patients with ALL.
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Li, Wenqing, Lai Wen, Bhavisha Rathod, Anne-Claude Gingras, Klaus Ley, and Ho-Sup Lee. "Kindlin2 enables EphB/ephrinB bi-directional signaling to support vascular development." Life Science Alliance 6, no. 3 (December 27, 2022): e202201800. http://dx.doi.org/10.26508/lsa.202201800.

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Direct contact between cells expressing either ephrin ligands or Eph receptor tyrosine kinase produces diverse developmental responses. Transmembrane ephrinB ligands play active roles in transducing bi-directional signals downstream of EphB/ephrinB interaction. However, it has not been well understood how ephrinB relays transcellular signals to neighboring cells and what intracellular effectors are involved. Here, we report that kindlin2 can mediate bi-directional ephrinB signaling through binding to a highly conserved NIYY motif in the ephrinB2 cytoplasmic tail. We show this interaction is important for EphB/ephrinB-mediated integrin activation in mammalian cells and for blood vessel morphogenesis during zebrafish development. A mixed two-cell population study revealed that kindlin2 (in ephrinB2-expressing cells) modulates transcellular EphB4 activation by promoting ephrinB2 clustering. This mechanism is also operative for EphB2/ephrinB1, suggesting that kindlin2-mediated regulation is conserved for EphB/ephrinB signaling pathways. Together, these findings show that kindlin2 enables EphB4/ephrinB2 bi-directional signal transmission.
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Riedl, Jurgen A., Dominique T. Brandt, Eduard Batlle, Leo S. Price, Hans Clevers, and Johannes L. Bos. "Down-regulation of Rap1 activity is involved in ephrinB1-induced cell contraction." Biochemical Journal 389, no. 2 (July 5, 2005): 465–69. http://dx.doi.org/10.1042/bj20050048.

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Ephrins are cell surface ligands that activate Eph receptor tyrosine kinases. This ligand–receptor interaction plays a central role in the sorting of cells. We have previously shown that the ephrinB–EphB signalling pathway is also involved in the migration of intestinal precursor cells along the crypts. Using the colon cell line DLD1 expressing the EphB2 receptor, we showed that stimulation of these cells with soluble ephrinB1 results in a rapid retraction of cell extensions and a detachment of cells. On ephrinB1 stimulation, the small GTPases Rho and Ras are activated and Rap1 is inactivated. Importantly, when a constitutively active Rap1 mutant was introduced into these cells, ephrinB1-induced retraction was inhibited. From these results, we conclude that down-regulation of Rap1 is a prerequisite for ephrin-induced cell retraction in colon cells.
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Minami, Masayoshi, Tatsuya Koyama, Yuki Wakayama, Shigetomo Fukuhara, and Naoki Mochizuki. "EphrinA/EphA signal facilitates insulin-like growth factor-I–induced myogenic differentiation through suppression of the Ras/extracellular signal–regulated kinase 1/2 cascade in myoblast cell lines." Molecular Biology of the Cell 22, no. 18 (September 15, 2011): 3508–19. http://dx.doi.org/10.1091/mbc.e11-03-0183.

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Insulin-like growth factor-I (IGF-I) activates not only the phosphatidylinositol 3-kinase (PI3K)–AKT cascade that is essential for myogenic differentiation but also the extracellular signal–regulated kinase (ERK) 1/2 cascade that inhibits myogenesis. We hypothesized that there must be a signal that inhibits ERK1/2 upon cell–cell contact required for skeletal myogenesis. Cell–cell contact–induced engagement of ephrin ligands and Eph receptors leads to downregulation of the Ras-ERK1/2 pathway through p120 Ras GTPase-activating protein (p120RasGAP). We therefore investigated the significance of the ephrin/Eph signal in IGF-I–induced myogenesis. EphrinA1-Fc suppressed IGF-I–induced activation of Ras and ERK1/2, but not that of AKT, in C2C12 myoblasts, whereas ephrinB1-Fc affected neither ERK1/2 nor AKT activated by IGF-I. IGF-I–dependent myogenic differentiation of C2C12 myoblasts was potentiated by ephrinA1-Fc. In p120RasGAP-depleted cells, ephrinA1-Fc failed to suppress the Ras-ERK1/2 cascade by IGF-I and to promote IGF-I–mediated myogenesis. EphrinA1-Fc did not promote IGF-I–dependent myogenesis when the ERK1/2 was constitutively activated. Furthermore, a dominant-negative EphA receptor blunted IGF-I–induced myogenesis in C2C12 and L6 myoblasts. However, the inhibition of IGF-I–mediated myogenesis by down-regulation of ephrinA/EphA signal was canceled by inactivation of the ERK1/2 pathway. Collectively, these findings demonstrate that the ephrinA/EphA signal facilitates IGF-I–induced myogenesis by suppressing the Ras-ERK1/2 cascade through p120RasGAP in myoblast cell lines.
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Gaitanos, Thomas N., Jorg Koerner, and Ruediger Klein. "Tiam–Rac signaling mediates trans-endocytosis of ephrin receptor EphB2 and is important for cell repulsion." Journal of Cell Biology 214, no. 6 (September 5, 2016): 735–52. http://dx.doi.org/10.1083/jcb.201512010.

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Ephrin receptors interact with membrane-bound ephrin ligands to regulate contact-mediated attraction or repulsion between opposing cells, thereby influencing tissue morphogenesis. Cell repulsion requires bidirectional trans-endocytosis of clustered Eph–ephrin complexes at cell interfaces, but the mechanisms underlying this process are poorly understood. Here, we identified an actin-regulating pathway allowing ephrinB+ cells to trans-endocytose EphB receptors from opposing cells. Live imaging revealed Rac-dependent F-actin enrichment at sites of EphB2 internalization, but not during vesicle trafficking. Systematic depletion of Rho family GTPases and their regulatory proteins identified the Rac subfamily and the Rac-specific guanine nucleotide exchange factor Tiam2 as key components of EphB2 trans-endocytosis, a pathway previously implicated in Eph forward signaling, in which ephrins act as in trans ligands of Eph receptors. However, unlike in Eph signaling, this pathway is not required for uptake of soluble ligands in ephrinB+ cells. We also show that this pathway is required for EphB2-stimulated contact repulsion. These results support the existence of a conserved pathway for EphB trans-endocytosis that removes the physical tether between cells, thereby enabling cell repulsion.
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FINNE, Eivind F., Else MUNTHE, and Hans-Christian AASHEIM. "A new ephrin-A1 isoform (ephrin-A1b) with altered receptor binding properties abrogates the cleavage of ephrin-A1a." Biochemical Journal 379, no. 1 (April 1, 2004): 39–46. http://dx.doi.org/10.1042/bj20031619.

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Ephrins are ligands for the Eph receptor tyrosine kinases, which play important roles in patterning nervous and vascular systems. Ephrin-A1 is a glycosylphosphatidylinositol-anchored ligand that binds to the EphA receptor tyrosine kinases. In the present study, we have identified a new ephrin-A1 isoform, denoted ephrin-A1b (ephrin-A1 isoform b). Compared with the originally described ephrin-A1 sequence, ephrin-A1a [Holzman, Marks and Dixit (1990) Mol. Cell. Biol. 10, 5830–5838], ephrin-A1b lacks a segment of 22 amino acids (residues 131–152). At the transcript level, exon 3 is spliced out in the transcript encoding ephrin-A1b. Transfection of HEK-293T cells (human embryonic kidney 293 cells) with an ephrin-A1b-expressing plasmid resulted in a significant expression of the protein on the cell surface. However, soluble EphA2 receptor (EphA2-Fc) bound weakly to ephrin-A1b-expressing transfectants, but bound strongly to ephrin-A1a-expressing transfectants. Ephrins have been shown to undergo regulated cleavage after interaction with their receptors. This process is inhibited by co-expression of ephrin-A1a and ephrin-A1b, indicating that ephrin-A1b influences the cleavage process. Taken together, these findings indicate that this newly described isoform may regulate the function of its ephrin-A1a counterpart.
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Gong, Jingyi, Roman Körner, Louise Gaitanos, and Rüdiger Klein. "Exosomes mediate cell contact–independent ephrin-Eph signaling during axon guidance." Journal of Cell Biology 214, no. 1 (June 27, 2016): 35–44. http://dx.doi.org/10.1083/jcb.201601085.

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The cellular release of membranous vesicles known as extracellular vesicles (EVs) or exosomes represents a novel mode of intercellular communication. Eph receptor tyrosine kinases and their membrane-tethered ephrin ligands have very important roles in such biologically diverse processes as neuronal development, plasticity, and pathological diseases. Until now, it was thought that ephrin-Eph signaling requires direct cell contact. Although the biological functions of ephrin-Eph signaling are well understood, our mechanistic understanding remains modest. Here we report the release of EVs containing Ephs and ephrins by different cell types, a process requiring endosomal sorting complex required for transport (ESCRT) activity and regulated by neuronal activity. Treatment of cells with purified EphB2+ EVs induces ephrinB1 reverse signaling and causes neuronal axon repulsion. These results indicate a novel mechanism of ephrin-Eph signaling independent of direct cell contact and proteolytic cleavage and suggest the participation of EphB2+ EVs in neural development and synapse physiology.
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Psilopatis, Iason, Eleni Souferi-Chronopoulou, Kleio Vrettou, Constantinos Troungos, and Stamatios Theocharis. "EPH/Ephrin-Targeting Treatment in Breast Cancer: A New Chapter in Breast Cancer Therapy." International Journal of Molecular Sciences 23, no. 23 (December 3, 2022): 15275. http://dx.doi.org/10.3390/ijms232315275.

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Breast cancer (BC) is the most common malignant tumor in women. Erythropoietin-producing hepatocellular receptors (EPHs), receptor tyrosine kinases binding the membrane-bound proteins ephrins, are differentially expressed in BC, and correlate with carcinogenesis and tumor progression. With a view to examining available therapeutics targeting the EPH/ephrin system in BC, a literature review was conducted, using the MEDLINE, LIVIVO, and Google Scholar databases. EPHA2 is the most studied EPH/ephrin target in BC treatment. The targeting of EPHA2, EPHA10, EPHB4, ephrin-A2, ephrin-A4, as well as ephrin-B2 in BC cells or xenograft models is associated with apoptosis induction, tumor regression, anticancer immune response activation, and impaired cell motility. In conclusion, EPHs/ephrins seem to represent promising future treatment targets in BC.
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Matsui, Toshimitsu, Hiroshi Matsuoka, Akira Tamekane, Ryuichi Inoue, Manabu Shimoyama, Atsushi Okamura, Hiroya Obama, Meghan L. Kelly, and Masaru Nakamoto. "Cell Adhesion and Migration Regulated by EphB6 Expressed on Human Hematopoietic Progenitors." Blood 106, no. 11 (November 16, 2005): 1386. http://dx.doi.org/10.1182/blood.v106.11.1386.1386.

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Abstract Normal human hematopoietic progenitors as well as leukemia/lymphoma cells express kinase-defective EphB6 receptors. The only unique high affinity ligand for EphB6 among eight known mammalian ephrins, ephrins-B2 is expressed not only on hematopoietic malignancies, but also on mesenchymal stem cells. However, the biological functions of the receptor and its ligand in hematopoietic cells are largely unknown. In the present study, we showed that the interaction between EphB6 and ephrinB2 could initiate forward as well as reverse signaling in vitro. Both pre-clustered and unclustered ligands could trigger the signal transduction, but pre-clustered ones more rapidly down-regulated the signaling. We also examined the EphB6/ephrinB2 function in cell adhesion and migration. Figure Figure HEK-EphB6 cells placed in the upper chamber of a Transwell apparatus, in which the lower side of filter was coated with different concentrations of ephrin-B2-Fc or Fc, were allowed to migrate to the lower side at 37°C overnight. Vector-transfected cells were used as controls. The cells that had migrated to the lower side of filter were stained, photographed. A BSA-coated filter is shown as a control. EphB6 exerted biphasic effects in response to different concentrations of the ephrin-B2. EphB6 promoted cell adhesion and migration when stimulated with low concentrations of ephrin-B2, whereas it induced repulsion and inhibited migration upon stimulation with high concentrations of ephrin-B2. A truncated EphB6 receptor lacking the cytoplasmic domain showed monophasic positive effects on cell adhesion and migration, indicating that the cytoplasmic domain is essential for the negative effects. We further explored the signal transduction of the biphasic effects. Figure Figure The Src family kinase, Fyn was co-immunoprecipitated with anti-EphB6 antibody in the absence or presence of ephrin-B2 stimulation. High concentrations of ephrin-B2 induced tyrosine phosphorylation of EphB6 through a Src family kinase activity. These results indicate that EphB6 can both positively and negatively regulate cell adhesion and migration, and suggest that tyrosine phosphorylation of the kinase-defective EphB6 receptor by a Src family kinase acts as the molecular switch for the functional transition. Thus, EphB6 expressed on hematopoietic cells may play an important role in the regulation of cell homing to hematopoietic tissues as well as leukemia cell infiltration.
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Dissertations / Theses on the topic "Ephrin"

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Tosch, Paul. "Investigations of ephrin ligands during development." Title page, abstract and table of contents only, 2002. http://web4.library.adelaide.edu.au/theses/09PH/09pht713.pdf.

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"May 2002." Addendum inside back cover. Bibliography: p. 139-157. Aims to isolate ephrin ligands from Drosophila melanogaster and analyse their involvement in Drosophila deveopment. Also investigates the potential of ephrin B-1 as a causative gene in the human condition Aicardi's syndrome.
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Brodie, James Cameron. "Investigation of ephrin regulation during hindbrain segmentation." Thesis, University College London (University of London), 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.249431.

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Eberhart, Johann. "EphA4/Ephrin interactions in motor axon guidance /." free to MU campus, to others for purchase, 2002. http://wwwlib.umi.com/cr/mo/fullcit?p3060095.

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Schmidt, Tim Sebastian. "Ephrin-B2 overexpression in the vascular endothelium." Thesis, University College London (University of London), 2006. http://discovery.ucl.ac.uk/1446088/.

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Previous work has established that Eph family receptor tyrosine kinases and ephrin ligands control a wide range of morphogenetic processes in vertebrate embryos through cell-contact dependent signalling interactions. In the developing cardiovascular system, ephrin-B2, a transmembrane protein is expressed by arterial endothelial cells (ECs) whereas the cognate receptor EphB4 is predominantly found on the venous endothelium. Gene targeting studies in mice have demonstrated that both molecules are critically required for angiogenic remodelling of embryonic blood vessels and survival beyond midgestation. To gain more insight into the role of ephrin-B2 in vascular development and its arterial expression, I have used the tetracycline-controlled expression systems to overexpress the ligand in the endothelium of all vascular beds (i.e. in arteries, veins and microvessels) of transgenic mice. In the course of this study, I have employed several different transgenic EC-specific driver lines in combination with tetracycline-controlled (tTA, Tet-OFF) and reverse tetracycline-controlled (rtTA, Tet-ON) transactivators. Ephrin-B2 overexpression triggers enhanced activation of EphB receptors particularly in the venous endothelium. This leads to severe vascular malformations such as oedema and haemorrhaging. Induction of ephrin-B2 expression at different stages of embryonic development controls not only vascular patterning and the recruitment of supporting pericytes and vascular smooth muscle cells but it can also trigger tissue-specific responses. In summary, my work has established that ephrin-B2 is an important regulator of blood vessel morphogenesis throughout embryonic development. Some results suggest that the ligand may also be involved in pathological conditions such as fibrosis as ectopic expression of ephrin-B2 in the embryonic liver triggers the activation of hepatic stellate cells. The resulting increase in matrix deposition around hepatic blood vessels could represent early signs of a fibrotic phenotype.
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Zimmer, Manuel. "Mechanisms of Eph, ephrin mediated cell-cell communication." Diss., [S.l.] : [s.n.], 2003. http://edoc.ub.uni-muenchen.de/archive/00001547.

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Bochenek, Magdalena Ludmila. "Regulation of cell motility by ephrin-B2 signalling." Thesis, University of Bristol, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.492474.

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Ephrin ligands and their Eph receptor tyrosine kinases both are surface tethered proteins that control cell shape and movements through direct cell-cell contact. Their binding, and subsequent clustering, triggers bidirectional signalling pathways, with signals transduced from the receptor (forward) and the ligand (reverse), that regulate the behaviour of both Eph- and ephrin- expressing cells. Recent evidence suggests that reverse ephrin-B2 signalling controls endothelial cell sprout outgrowth and tip elongation, and smooth muscle cell shape changes and behaviour. In addition, misregulation of ephrin-B2 expression is observed in various tumour types and high expression of this ligand is correlated with increased tumour vascularisation and tendency to metastasise. To investigate how ephrin-B2 "reverse" signalling pathways direct changes during angiogenesis and how the expression level of ephrin ligands influences changes in cell behaviour and cell mot motility, I have used Human Umbilical Vein Endothelial Cells (HUVECs) overexpressing ephrin ligands as a model system.
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Khan, Taslima. "Isolation and functional analysis of Xenopus Ephrin-A3." Thesis, University College London (University of London), 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.399711.

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Koch, William Tyler. "Elucidating Mechanisms of Canonical Wnt - ephrin-B Crosstalk." Thesis, West Virginia University, 2016. http://pqdtopen.proquest.com/#viewpdf?dispub=10146608.

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Throughout development, canonical Wnt signaling contributes to the formation and maintenance of a wide array of cells, tissues, and organs. Dys-regulated Wnt signaling during embryonic development is implicated in developmental defects known as neurochristopathies, including craniofacial and heart defects, as well as defects in neural development. Due to its roles in stem cell maintenance and self-renewal, tissue homeostasis, and regeneration, aberrant Wnt signaling in adult tissues can result in various forms of cancer, including colorectal cancer, breast cancer, lung cancer, and gastro-intestinal cancer, among others. Dys-regulated Wnt signaling is also implicated in other pathologies including bone disease, and metabolic diseases, such as Type II diabetes. Our lab has previously identified a novel crosstalk between canonical Wnt signaling and ephrin signaling. Ephrin signaling occurs through the interaction of ephrin ligands and Eph receptor tyrosine kinases, and is bidirectional. Due to the roles of ephrin signaling in tissue development and maintenance, aberrant ephrin signaling is implicated in many diseases including bone remodeling diseases, diabetes, and cancer. The molecular mechanism of the crosstalk between canonical Wnt signaling and ephrin-B signaling remains unknown. β-catenin is a key intracellular effector of canonical Wnt signaling that transduces the signal to the nucleus, where β-catenin interacts with the TCF/LEF transcription factors and activates transcription of target genes. Due to its central role in transducing the canonical Wnt signal to the nucleus, we predict that ephrin-B signaling antagonizes canonical Wnt signaling by affecting the stability and/or sub-cellular localization of β-catenin, or the interaction between β-catenin and TCF/LEF transcription factors. By employing mouse ephrin-B constructs in human cell lines, we show that the canonical Wnt - ephrin-B crosstalk is conserved between frogs and mammals. We also found that ephrin-B antagonism of canonical Wnt signaling is likely independent of ubiquitin proteasome system (UPS)-mediated degradation of β-catenin. Furthermore, confocal immunofluorescence microscopy revealed that overexpression of ephrin-B in HEK293T cells treated with lithium chloride (LiCl) seems to promote membrane localization of β-catenin, particularly at the apical Z sections. These results suggests that re-localization of β-catenin to the cell membrane may contribute to the ephrin-B antagonism of canonical Wnt signaling.

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Gregory, L. G. L. "Eph-ephrin signalling in cell sorting and directional migration." Thesis, University College London (University of London), 2011. http://discovery.ucl.ac.uk/1318081/.

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An important problem in developmental biology is to understand how precise patterns of cell types are maintained during development. Eph receptor tyrosine kinases and ephrins have key roles in stabilising these patterns of cell organisation and segregation during development and can restrict the movement of cells by promoting cell repulsion. Previous work by Alexei Poliakov in the Wilkinson lab has shown that Eph-ephrin signalling leads to directional persistence of migration, and modelling suggests that this can contribute to cell segregation. In order to test experimentally the contribution of directional persistence in cell segregation, I have used and developed in vitro assays to dissect the roles of EphB2-ephrinB1 signalling in cell segregation, boundary sharpening and directional persistence. In these assays, stable HEK293 cell lines expressing EphB2 or ephrinB1 are mixed in cell culture and this leads to segregation of the two cell populations. Plating these cells either side of a removable barrier and allowing migration of cells towards each other leads to the formation of a sharp boundary on interaction. Analysis of cell behaviour shows EphB2 cells to move more persistently after interaction with ephrinB1 cells. To analyse how EphB2-ephrinB1 interactions lead to directional persistence of migration, my studies have focussed on the role of components potentially involved in directional persistence that act downstream of EphB2-ephrinB1 signalling, including the planar cell polarity (PCP) pathway (Dishevelled and Daam1) and core polarity components such as the PAR proteins (PAR-3 and PAR-6B). The PCP and PAR components were all found to have roles in cell segregation, as siRNA-mediated knockdown of each of these components disrupted EphB2-ephrinB1 mediated cell segregation and boundary sharpening. However, cell behaviour studies showed that only Dishevelled and PAR-6B have roles in EphB2-ephrinB1 mediated directional persistence, whilst Daam1 knockdown has no effect on the migratory response of cells. PAR-3 knockdown affects the basal ability of cells to migrate, potentially due to its role in establishing front-rear polarity. Taken together, these findings can be explained by a model in which Dishevelled and PAR-6B have a role in EphB2-ephrinB1 mediated directional persistence required for cell segregation and boundary sharpening. I propose that Daam1 may function in the contact inhibition of locomotion between cells also required for segregation.
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Harbott, Lene Karen. "Signalling pathways mediating ephrin-A-induced growth cone collapse." Thesis, University College London (University of London), 2004. http://discovery.ucl.ac.uk/1446636/.

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The ephrin-A family of axon guidance cues, which activate the EphA family of receptor tyrosine kinases, guide the axons of many types of neuron to the correct target during embryonic development. One particularly well-studied example is the projection of RGC processes to precise positions in the midbrain target that reflect the position of the RGC in the retina. Ephrin-As are membrane-tethered molecules expressed in a gradient in the midbrain, and they govern the formation of the retinotectal map by differential, contact-mediated repulsion of Eph-A-expressing RGC axons. In order to identify signalling molecules that mediate ephrin-A induced repulsion of RGCs, I have developed a novel co-culture assay in which contact with a single non-neuronal cell that expresses endogenous levels of ephrin-A induces rapid loss of RGC growth cone lamella, followed by axon retraction. I have confirmed that these cellular responses are mediated by neuronal EphA receptor signalling and, in combination with the traditional soluble collapse assay, have used this physiologically relevant co-culture assay to identify a more specific role for the Rho effector ROCK in ephrin-A-induced RGC responses than has previously been published. Specifically ROCK activity mediates ephrin-A-induced RGC axon retraction, but not loss of growth cone lamella. I have also identified the non-receptor tyrosine kinase Abl as having a major role in the ephrin-A-induced RGC repulsive response, as the Abl kinase inhibitor STI571 prevents both the ephrin-A-induced loss of RGC lamella and axon retraction. I have demonstrated the existence of a protein complex containing active Eph receptors, Abl and Mena, and shown that disruption of this complex correlates with STI571-dependent inhibition of the ephrin-A-induced RGC repulsive responses. These results comprise the first evidence that Abl plays a role in mediating Eph receptor signals, and is involved in the cytoskeletal rearrangements that underlie ephrin-A-induced growth cone collapse in vitro, and thus both complement and extend the published evidence demonstrating a role for Abl in mediating axon guidance in vivo.
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Books on the topic "Ephrin"

1

Ephron, Nora. Nora Ephron collected. New York: Avon Books, 1991.

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Ephron, Nora. Nora Ephron collected. New York: Avon Books, 1991.

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Foundation, Ephraim Historical, ed. Ephraim. Charleston, SC: Arcadia Pub., 2008.

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Paul, Burton. Ephraim stories. Ephraim, Door County, Wis: Stonehill Pub., 1999.

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Albrecht, Wolfgang. Gotthold Ephraim Lessing. Stuttgart: J.B. Metzler, 1997. http://dx.doi.org/10.1007/978-3-476-03993-4.

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Gotthold Ephraim Lessing. Stuttgart: P. Reclam, 2000.

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Gotthold Ephraim Lessing. München: Verlag C.H. Beck, 2016.

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Kröger, Wolfgang. Gotthold Ephraim Lessing. Stuttgart: Reclam, 1995.

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Albrecht, Wolfgang. Gotthold Ephraim Lessing. Stuttgart: J.B. Metzler, 1996.

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Gotthold Ephraim Lessing. Stuttgart: Fink, 2010.

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Book chapters on the topic "Ephrin"

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Salajegheh, Ali. "Erythropoietin-Producing Hepatocellular Receptors A: Ephrin A1, Ephrin A2 and Ephrin A3." In Angiogenesis in Health, Disease and Malignancy, 75–87. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-28140-7_14.

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Allocca, Chiara, and Maria Domenica Castellone. "Ephrin Receptor A2." In Encyclopedia of Signaling Molecules, 1581–87. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101649.

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Allocca, Chiara, and Maria Domenica Castellone. "Ephrin Receptor A2." In Encyclopedia of Signaling Molecules, 1–7. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101649-1.

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Salajegheh, Ali. "Erythropoietin-Producing Hepatocellular Receptors B: Ephrin B2, Ephrin B4." In Angiogenesis in Health, Disease and Malignancy, 89–96. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-28140-7_15.

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Matsuo, Koichi. "Eph and Ephrin Interactions in Bone." In Advances in Experimental Medicine and Biology, 95–103. Boston, MA: Springer US, 2009. http://dx.doi.org/10.1007/978-1-4419-1050-9_10.

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Ieguchi, Katsuaki, and Yoshiro Maru. "Eph/Ephrin Signaling in the Tumor Microenvironment." In Advances in Experimental Medicine and Biology, 45–56. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-47189-7_3.

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Miao, Hui, and Bingcheng Wang. "Eph/Ephrin Signaling in Postnatal Epithelial Growth." In Handbook of Growth and Growth Monitoring in Health and Disease, 2811–23. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-1795-9_167.

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Jorgensen, Claus, and Alexei Poliakov. "Proteomics Analysis of Contact-Initiated Eph Receptor–Ephrin Signaling." In Cell-Cell Interactions, 1–16. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-604-7_1.

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Darie, Costel C., Vivekananda Shetty, Daniel S. Spellman, Guoan Zhang, Chongfeng Xu, Helene L. Cardasis, Steven Blais, David Fenyo, and Thomas A. Neubert. "Blue Native PAGE and Mass Spectrometry Analysis of Ephrin Stimulation-Dependent Protein-Protein Interactions in NG108-EphB2 Cells." In NATO Science for Peace and Security Series A: Chemistry and Biology, 3–22. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-8811-7_1.

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Peter, Helga, and Thomas Penzel. "Ephedrin." In Springer Reference Medizin, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2020. http://dx.doi.org/10.1007/978-3-642-54672-3_497-1.

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Conference papers on the topic "Ephrin"

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Schlesinger, Nicole. "Abstract 1236: Ephrin signaling in medulloblastoma." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-1236.

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Vadivel, A., G. Rey-Parra, F. Eaton, and B. Thebaud. "The Axonal Guidance Cue Ephrin Promotes Alveolar Development." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a4106.

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Ferluga, Sara, and Waldemar Debinski. "Abstract 3860: Glycosylation is indispensable for ephrin A1 activity." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-3860.

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Lee, Hungyen, Kamal A. Mohammed, Sriram S. Peruvemba, Eugene P. Goldberg, and Najmunnisa Nasreen. "Ephrin-A1 Loaded Albumin Microspheres For Lung Cancer Therapy." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a5156.

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Bennett, KM, C. Dravis, M. Henkemeyer, and MA Schwarz. "Inhibition of Ephrin B2 Reverse Signaling Alters Distal Alveolar Morphogenesis." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a5392.

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Perez-Tenorio, Gizeh, Olle Stål, and Elena B. Pasquale. "Abstract 1981: Ephrin B2 as a tumor suppressor in breast cancer." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-1981.

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Kamoun, Walid S., Shinji Oyama, Tad Kornaga, Theresa Feng, Lia Luus, Minh T. Pham, Dmitri B. Kirpotin, et al. "Abstract 750: Nanoliposomal targeting of Ephrin receptor A2 (EphA2): Clinical translation." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-750.

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Perez-Tenorio, Gizeh, Anna-Maria Husa, and Olle Stål. "Abstract 3819: Clinical potential of the Eph/ephrin profile in breast cancer." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-3819.

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Bartenschlager, F., O. Kershaw, J. Braun, W. Reineking, W. Baumgärtner, C. Schwarz, T. Leeb, and A. D. Gruber. "Hereditärer Ephrin-B3-Gendefekt bei drei Weimaranerwelpen mit Ataxie, Dysbasie und Paraparese." In 67. Jahrestagung der Fachgruppe Pathologie der Deutschen Veterinärmedizinischen Gesellschaft. Georg Thieme Verlag KG, 2024. http://dx.doi.org/10.1055/s-0044-1787320.

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Yang, Nai-Ying Michelle, Nikki Noren Hooten, and Elena B. Pasquale. "Abstract 3115: Ephrin-dependent and -independent activities of the receptor tyrosine kinase EphB4." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-3115.

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Reports on the topic "Ephrin"

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Koury, Jeffrey. Elucidating the role of ephrin-B1 in IFNB mediated neuroprotection in HIV associated neurocognitive disorder (HAND). ResearchHub Technologies, Inc., November 2022. http://dx.doi.org/10.55277/researchhub.l8vj1ujl.

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Landslides and debris flows in Ephraim Canyon, central Utah. US Geological Survey, 1989. http://dx.doi.org/10.3133/b1842c.

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Kinematics of the Aspen Grove landslide, Ephraim Canyon, central Utah. US Geological Survey, 1993. http://dx.doi.org/10.3133/b1842f.

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