Receptor, EphB4
Receptor, EphB2
Receptor, EphB1
Ephrin-B2
Ephrin-B1
Receptor, EphB3
Receptor, EphB6
Receptors, Eph Family
Receptor, EphB5
Ephrin-B3
Ephrins
New ether-a-go-go K(+) channel family members localized in human telencephalon. (1/149)
A cDNA encoding a novel voltage-gated K(+) channel protein was isolated from human brain. This protein, termed BEC1, is 46% identical to rat elk in the ether-a-go-go K(+) channel family. The BEC1 gene maps to the 12q13 region of the human genome. Northern blot analysis indicates that BEC1 is exclusively expressed in human brain, where the expression is concentrated in the telencephalic areas such as the cerebral cortex, amygdala, hippocampus, and striatum. By in situ hybridization, BEC1 is detected in the CA1-CA3 pyramidal cell layers and the dentate gyrus granule cell layers of the hippocampus. Specific signals are also found in neocortical neurons. Transfection of mammalian L929 and Chinese hamster ovary cells with BEC1 cDNA induces a voltage-gated outward current with a fast inactivation component. This current is insensitive to tetraethylammonium and quinidine. Additionally, a second related gene BEC2 was isolated from human brain. BEC2 is also brain-specific, located in the neocortex and the striatum, and functional as a channel gene. Phylogenetic analysis indicates that BEC1 and BEC2 constitute a subfamily, together with elk, in the ether-a-go-go family. The two genes may be involved in cellular excitability of restricted neurons in the human central nervous system. (+info)Misexpression of the Emx-related homeobox genes cVax and mVax2 ventralizes the retina and perturbs the retinotectal map. (2/149)
The mechanisms that establish the dorsal-ventral (D-V) axis of the eye are poorly understood. We isolated two homeobox genes from mouse and chicken, mVax2 and cVax, whose expression during early eye development is restricted to the ventral retina. In chick, ectopic expression of either Vax leads to ventralization of the early retina, as assayed by expression of the transcription factors Pax2 and Tbx5, and the Eph family members EphB2, EphB3, ephrinB1, and ephrinB2, all of which are normally dorsally or ventrally restricted. Moreover, the projections of dorsal but not ventral ganglion cell axons onto the optic tectum showed profound targeting errors following cVax misexpression. mVax2/cVax thus specify positional identity along the D-V axis of the retina and influence retinotectal mapping. (+info)The receptor tyrosine kinase EphB4 and ephrin-B ligands restrict angiogenic growth of embryonic veins in Xenopus laevis. (3/149)
The cues and signaling systems that guide the formation of embryonic blood vessels in tissues and organs are poorly understood. Members of the Eph family of receptor tyrosine kinases and their cell membrane-anchored ligands, the ephrins, have been assigned important roles in the control of cell migration during embryogenesis, particularly in axon guidance and neural crest migration. Here we investigated the role of EphB receptors and their ligands during embryonic blood vessel development in Xenopus laevis. In a survey of tadpole-stage Xenopus embryos for EphB receptor expression, we detected expression of EphB4 receptors in the posterior cardinal veins and their derivatives, the intersomitic veins. Vascular expression of other EphB receptors, including EphB1, EphB2 or EphB3, could however not be observed, suggesting that EphB4 is the principal EphB receptor of the early embryonic vasculature of Xenopus. Furthermore, we found that ephrin-B ligands are expressed complementary to EphB4 in the somites adjacent to the migratory pathways taken by intersomitic veins during angiogenic growth. We performed RNA injection experiments to study the function of EphB4 and its ligands in intersomitic vein development. Disruption of EphB4 signaling by dominant negative EphB4 receptors or misexpression of ephrin-B ligands in Xenopus embryos resulted in intersomitic veins growing abnormally into the adjacent somitic tissue. Our findings demonstrate that EphB4 and B-class ephrins act as regulators of angiogenesis possibly by mediating repulsive guidance cues to migrating endothelial cells. (+info)Comparative analysis of embryonic gene expression defines potential interaction sites for Xenopus EphB4 receptors with ephrin-B ligands. (4/149)
The Eph family of receptor tyrosine kinases and their ligands, the ephrins, act as signaling molecules regulating the migratory behavior of neurons and neural crest cells, and are implicated in tissue patterning, blood vessel formation, and tumorigenesis. On the basis of structural similarities and overlapping binding specificities, Eph receptors as well as their ligands can be divided into A and B subfamilies with orthologues found in all vertebrates. We describe here the isolation of cDNAs encoding Xenopus EphB4 receptors and show that embryonic expression is prominently associated with the developing vasculature, newly forming somites, the visceral arches, and non-neuronal tissues of the embryonic head. In a screen to identify potential ligands for EphB4 in Xenopus embryos, we isolated cDNAs for the Xenopus ephrin-B2 and -B3, which demonstrates that the Xenopus genome harbors genes encoding orthologues to all three currently known mammalian ephrin-B genes. We next performed in situ hybridizations to identify tissues and organs where EphB4 receptors may encounter ephrin-B ligands during embryonic development. Our analysis revealed distinct, but overlapping patterns of ephrin-B gene expression. Interestingly, each ephrin-B ligand displayed expression domains either adjacent to or within EphB4-expressing tissues. These findings indicate that EphB4 receptors may interact in vivo with multiple B-class ephrins. The expression patterns also suggest that EphB4 receptors and their ligands may be involved in visceral arch formation, somitogenesis, and blood vessel development. (+info)Kinase independent function of EphB receptors in retinal axon pathfinding to the optic disc from dorsal but not ventral retina. (5/149)
Optic nerve formation requires precise retinal ganglion cell (RGC) axon pathfinding within the retina to the optic disc, the molecular basis of which is not well understood. At CNS targets, interactions between Eph receptor tyrosine kinases on RGC axons and ephrin ligands on target cells have been implicated in formation of topographic maps. However, studies in chick and mouse have shown that both Eph receptors and ephrins are also expressed within the retina itself, raising the possibility that this receptor-ligand family mediates aspects of retinal development. Here, we more fully document the presence of specific EphB receptors and B-ephrins in embryonic mouse retina and provide evidence that EphB receptors are involved in RGC axon pathfinding to the optic disc. We find that as RGC axons begin this pathfinding process, EphB receptors are uniformly expressed along the dorsal-ventral retinal axis. This is in contrast to the previously reported high ventral-low dorsal gradient of EphB receptors later in development when RGC axons map to CNS targets. We show that mice lacking both EphB2 and EphB3 receptor tyrosine kinases, but not each alone, exhibit increased frequency of RGC axon guidance errors to the optic disc. In these animals, major aspects of retinal development and cellular organization appear normal, as do the expression of other RGC guidance cues netrin, DCC, and L1. Unexpectedly, errors occur in dorsal but not ventral retina despite early uniform or later high ventral expression of EphB2 and EphB3. Furthermore, embryos lacking EphB3 and the kinase domain of EphB2 do not show increased errors, consistent with a guidance role for the EphB2 extracellular domain. Thus, while Eph kinase function is involved in RGC axon mapping in the brain, RGC axon pathfinding within the retina is partially mediated by EphB receptors acting in a kinase-independent manner. (+info)Complementary expression of transmembrane ephrins and their receptors in the mouse spinal cord: a possible role in constraining the orientation of longitudinally projecting axons. (6/149)
In the developing spinal cord, axons project in both the transverse plane, perpendicular to the floor plate, and in the longitudinal plane, parallel to the floor plate. For many axons, the floor plate is a source of long- and short-range guidance cues that govern growth along both dimensions. We show here that B-class transmembrane ephrins and their receptors are reciprocally expressed on floor plate cells and longitudinally projecting axons in the mouse spinal cord. During the period of commissural axon pathfinding, B-class ephrin protein is expressed at the lateral floor plate boundaries, at the interface between the floor plate and the ventral funiculus. In contrast, B-class Eph receptors are expressed on decussated commissural axon segments projecting within the ventral funiculus, and on ipsilaterally projecting axons constituting the lateral funiculus. Soluble forms of all three B-class ephrins bind to, and induce the collapse of, commissural growth cones in vitro. The collapse-inducing activity associated with B-class ephrins is likely to be mediated by EphB1. Taken together, these data support a possible role for repulsive B-class Eph receptor/ligand interactions in constraining the orientation of longitudinal axon projections at the ventral midline. (+info)Implications of EPHB6, EFNB2, and EFNB3 expressions in human neuroblastoma. (7/149)
Neuroblastoma (NB) is a common pediatric tumor that exhibits a wide range of biological and clinical heterogeneity. EPH (erythropoietin-producing hepatoma amplified sequence) family receptor tyrosine kinases and ligand ephrins play pivotal roles in neural and cardiovascular development. High-level expression of transcripts encoding EPHB6 receptors (EPHB6) and its ligands ephrin-B2 and ephrin-B3 (EFNB2, EFNB3) is associated with low-stage NB (stages 1, 2, and 4S) and high TrkA expression. In this study, we showed that EFNB2 and TrkA expressions were associated with both tumor stage and age, whereas EPHB6 and EFNB3 expressions were solely associated with tumor stage, suggesting that these genes were expressed in distinct subsets of NB. Kaplan-Meier and Cox regression analyses revealed that high-level expression of EPHB6, EFNB2, and EFNB3 predicted favorable NB outcome (P<0.005), and their expression combined with TrkA expression predicted the disease outcome more accurately than each variable alone (P<0.00005). Interestingly, if any one of the four genes (EPHB6, EFNB2, EFNB3, or TrkA) was expressed at high levels in NB, the patient survival was excellent (>90%). To address whether a good disease outcome of NB was a consequence of high-level expression of a "favorable NB gene," we examined the effect of EPHB6 on NB cell lines. Transfection of EPHB6 cDNA into IMR5 and SY5Y expressing little endogenous EPHB6 resulted in inhibition of their clonogenicity in culture. Furthermore, transfection of EPHB6 suppressed the tumorigenicity of SY5Y in a mouse xenograft model, demonstrating that high-level expressions of favorable NB genes, such as EPHB6, can in fact suppress malignant phenotype of unfavorable NB. (+info)Rit, a non-lipid-modified Ras-related protein, transforms NIH3T3 cells without activating the ERK, JNK, p38 MAPK or PI3K/Akt pathways. (8/149)
The biological functions of Rit (Ras-like protein in tissues) and Rin (Ras-like protein in neurons), members of a novel branch of Ras-related GTP-binding proteins that are approximately 50% identical to Ras, have not been characterized. Therefore, we assessed their activity in growth control, transformation and signaling. NIH cells stably expressing a constitutively activated mutant of Rit [Rit(79L)] (analogous to the oncogenic mutant H-Ras(61L)) demonstrated strong growth transformation, proliferating rapidly in low serum and forming colonies in soft agar and tumors in nude mice. Although Rit(79L) alone did not promote morphologically transformed foci, it cooperated with both Raf and Rho A to form Rac/Rho-like foci. Rin [Rin(78L)] cooperated only with Raf. Rit(79L) but not Rin(78L) stimulated transcription from luciferase reporter constructs regulated by SRF, NF-kappaB, Elk-1 and Jun. However, neither activated ERK, JNK or p38, or PI3-K/Akt kinases in immune complex kinase assays. Interestingly, although Rit lacks any known recognition signal for C-terminal lipidation, Rit-transformed cell growth and survival in low serum is dependent on a farnesylated protein, as treatment with farnesyltransferase inhibitors caused apoptosis. Rin cooperated with Raf in focus assays but did not otherwise function in these assays, perhaps due to a lack of appropriate effector pathways in NIH3T3 fibroblasts for this neural-specific Ras family member. In summary, although Rit shares most core effector domain residues with Ras, our results suggest that Rit uses novel effector pathways to regulate proliferation and transformation. (+info)EphB4 is a type of receptor tyrosine kinase (RTK) that belongs to the Eph receptor family. These receptors are involved in cell-cell communication during development and tissue homeostasis. Specifically, EphB4 is a membrane-bound protein that interacts with its ligand, ephrin-B2, which is also a transmembrane protein, to mediate bidirectional signaling between neighboring cells.
The binding of ephrin-B2 to EphB4 triggers a variety of intracellular signaling events that regulate various cellular processes, including cell migration, adhesion, and repulsion. In the context of the cardiovascular system, EphB4 plays important roles in vascular development, angiogenesis, and arterial-venous specification.
Mutations or dysregulation of EphB4 have been implicated in various pathological conditions, such as cancer, atherosclerosis, and neurological disorders. Therefore, understanding the function and regulation of EphB4 has important implications for the development of novel therapeutic strategies for these diseases.
EphB2 is a type of receptor tyrosine kinase (RTK) that belongs to the Eph family of receptors. These receptors are involved in bidirectional communication between cells and are important in the development and function of the nervous system. Specifically, EphB2 receptors are expressed on the surface of certain types of neurons and bind to ephrin-B ligands on nearby cells. This binding triggers a cascade of intracellular signaling events that can regulate various cellular processes, including cell migration, adhesion, and axon guidance.
EphB2 receptors have also been implicated in the pathology of several diseases, including cancer. For example, abnormal activation of EphB2 has been linked to tumor growth, progression, and metastasis in certain types of cancer. Therefore, EphB2 is an important target for the development of new therapies for cancer and other diseases.
EphB1 is a type of receptor tyrosine kinase (RTK) that belongs to the Eph family of receptors. It is a single-pass transmembrane protein that contains an extracellular domain with a binding site for its ligand, ephrin-Bs, and an intracellular domain with tyrosine kinase activity.
EphB1 receptors are primarily expressed in the nervous system, where they play important roles in various developmental processes, including axon guidance, neuronal migration, and synaptic plasticity. They also have been implicated in tumorigenesis and cancer progression, as well as in the regulation of immune responses.
The binding of ephrin-Bs to EphB1 receptors triggers a variety of intracellular signaling pathways that can lead to both forward and reverse signaling. Forward signaling occurs when the activated EphB1 receptor phosphorylates downstream effector proteins, leading to changes in cell behavior such as repulsion or adhesion. Reverse signaling occurs when ephrin-Bs, which are also transmembrane proteins, activate their own intracellular signaling pathways upon binding to EphB1 receptors.
Overall, the EphB1 receptor is a crucial component of the Eph/ephrin signaling system that plays important roles in various biological processes and has potential implications for disease treatment and diagnosis.
Ephrin-B2 is a type of protein that belongs to the ephrin family and is primarily involved in the development and function of the nervous system. It is a membrane-bound ligand for Eph receptor tyrosine kinases, and their interactions play crucial roles in cell-cell communication during embryogenesis and adult tissue homeostasis.
Ephrin-B2 is specifically a glycosylphosphatidylinositol (GPI)-anchored protein that is expressed on the cell membrane of various cell types, including endothelial cells, neurons, and some immune cells. Its interactions with Eph receptors, which are transmembrane proteins, lead to bidirectional signaling across the contacting cell membranes. This process regulates various aspects of cell behavior, such as adhesion, migration, repulsion, and proliferation.
In the context of the cardiovascular system, ephrin-B2 is essential for the development and maintenance of blood vessels. It is involved in the formation of arterial-venous boundaries, vascular branching, and remodeling. Mutations or dysregulation of ephrin-B2 have been implicated in various diseases, including cancer, where it can contribute to tumor angiogenesis and metastasis.
Ephrin-B1 is a type of protein that belongs to the ephrin family and is involved in cell signaling, specifically in the process known as cell-cell communication. It is a transmembrane protein, which means it spans the membrane of the cell and has a portion that faces the outside of the cell (the extracellular domain) and a portion that faces the inside of the cell (the intracellular domain).
Ephrin-B1 binds to Eph receptors, which are tyrosine kinase receptors found on the surface of neighboring cells. This binding results in the initiation of a signaling cascade that can influence various cellular processes, including cell migration, adhesion, and proliferation.
Ephrin-B1 is widely expressed in various tissues throughout the body, including the nervous system, where it plays important roles in the development and function of the brain. Mutations in the gene that encodes ephrin-B1 have been associated with certain neurological disorders, such as intellectual disability and epilepsy.
EphB3 is a type of receptor tyrosine kinase that belongs to the Eph family of receptors. It is a transmembrane protein that plays a crucial role in cell signaling and communication, particularly during embryonic development and tissue organization. The EphB3 receptor binds to ephrin-B ligands, which are also transmembrane proteins expressed on neighboring cells.
The binding of ephrin-B to EphB3 initiates a bidirectional signaling process that regulates various cellular processes such as cell adhesion, migration, and repulsion. This interaction is important for the formation of boundaries between different tissues, axon guidance, and synaptic plasticity in the nervous system.
Mutations in the EphB3 gene have been associated with several human diseases, including cancer, immune disorders, and neurological conditions. Therefore, understanding the function and regulation of EphB3 receptors is essential for developing novel therapeutic strategies to treat these diseases.
EphB6 is not a traditional "receptor" in the sense of a protein that binds to a signaling molecule and triggers a cellular response. Instead, EphB6 is a member of the Eph receptor tyrosine kinase family, which are involved in intracellular signaling pathways.
EphB6 is unique among the Eph receptors because it lacks a functional kinase domain and is therefore considered to be a "non-kinase" member of the family. Instead, EphB6 forms complexes with other Eph receptors and modulates their signaling activity.
EphB6 has been shown to interact with other Eph receptors, such as EphB2 and EphB3, and regulate their downstream signaling pathways. It is involved in various cellular processes, including cell adhesion, migration, and differentiation. Dysregulation of EphB6 has been implicated in several diseases, including cancer, where it can act as a tumor suppressor or promote tumor progression depending on the context.
In summary, while EphB6 is not a traditional receptor that binds to signaling molecules and triggers cellular responses, it is a member of the Eph receptor tyrosine kinase family that modulates the signaling activity of other Eph receptors and plays important roles in various cellular processes.
Eph family receptors are a group of tyrosine kinase receptors that play crucial roles in the development and function of the nervous system, as well as in other tissues. They are named after the first discovered member of this family, EPH (Erythropoietin-Producing Human Hepatocellular carcinoma) receptor.
These receptors are divided into two subfamilies: EphA and EphB, based on their binding preferences for ephrin ligands. Ephrins are membrane-bound proteins that can be either GPI-anchored (ephrin-A) or transmembrane (ephrin-B), and they interact with Eph receptors in a bidirectional manner, activating both forward signaling in the receptor-expressing cell and reverse signaling in the ephrin-expressing cell.
Eph receptors and ephrins are essential for axon guidance, topographic mapping, and synaptic plasticity during neural development. They also participate in various processes in adult tissues, such as angiogenesis, tumorigenesis, and immune responses. Dysregulation of Eph family receptors has been implicated in several diseases, including cancer, neurological disorders, and vascular diseases.
EphB5 is a type of receptor tyrosine kinase that belongs to the Eph family of receptors. It is a cell surface receptor that interacts with its ligand, ephrin-B2, which is also a cell surface protein. The interaction between EphB5 and ephrin-B2 plays a crucial role in various biological processes, including cell migration, axon guidance, and tissue boundary formation during development.
EphB5 receptor is composed of an extracellular domain that contains the ligand-binding site, a transmembrane domain, and an intracellular domain with tyrosine kinase activity. Upon binding to its ligand, EphB5 undergoes dimerization and autophosphorylation of specific tyrosine residues in the intracellular domain. This triggers downstream signaling cascades that regulate various cellular processes.
Mutations in the EPHB5 gene have been associated with several human diseases, including cancer, intellectual disability, and congenital heart defects. Therefore, understanding the function of EphB5 receptor and its signaling pathways is essential for developing novel therapeutic strategies for these diseases.
Ephrin-B3 is a type of protein that belongs to the ephrin family and is involved in cell signaling, particularly during the development and functioning of the nervous system. It is a transmembrane protein, which means it spans the membrane of the cell and has a domain outside the cell and a domain inside the cell.
Ephrin-B3 interacts with Eph receptors on neighboring cells to initiate bidirectional signaling, which means that both the cells that express ephrin-B3 and the cells that express the Eph receptor are affected by this interaction. This signaling is important for various processes such as axon guidance, cell migration, and tissue boundaries formation during development. In addition, ephrin-B3 has been implicated in the regulation of synaptic plasticity and vascular remodeling in adults.
Mutations in the gene that encodes ephrin-B3 have been associated with certain neurological disorders, such as intellectual disability and epilepsy.
Ephrins are a family of membrane-bound proteins that play crucial roles in various biological processes, including cell migration, axon guidance, and tissue boundary formation during embryonic development. They interact with Eph receptors, which are tyrosine kinase receptors found on the surface of neighboring cells. This interaction results in bidirectional signaling between the two cells, affecting their behaviors and influencing the organization of tissues and organs.
There are two main types of ephrins: Ephrin-A (also known as GPI-anchored ephrins) and Ephrin-B (transmembrane ephrins). Ephrin-A proteins are attached to the cell membrane through a glycosylphosphatidylinositol (GPI) anchor, while Ephrin-B proteins have a transmembrane domain and a cytoplasmic tail. Both types of ephrins interact with Eph receptors, leading to the initiation of intracellular signaling cascades that regulate various cellular responses.
Dysregulation of ephrin/Eph receptor interactions has been implicated in several human diseases, including cancer, where they can contribute to tumor growth, progression, and metastasis. Therefore, understanding the functions and regulation of ephrins and their receptors is essential for developing novel therapeutic strategies to treat various diseases.
EPH receptor B4
Tesevatinib
Ephrin B2
Ephrin receptor
Ephrin
Vein of Galen aneurysmal malformations
List of MeSH codes (D12.776.543)
List of MeSH codes (D08)
Sterile alpha motif
Tyrosine kinase
Fibronectin type III domain
Vascular remodelling in the embryo
Researchers interested in Receptor, EphB4 | Directory of Faculty Research Interests
EPH receptor B4 - Wikipedia
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Type-B receptor3
- Ephrin type-B receptor 4 is a protein that in humans is encoded by the EPHB4 gene. (wikipedia.org)
- Preclinical studies confirmed ephrin type-B receptor 4 (EphB4) as a potential therapeutic target based on the efficacy of human serum albumin-conjugated soluble EphB4 in mice bearing orthotopic xenografts. (ppbhg.org)
- Materials and Strategies Dataset This paper is dependant on the published evaluations of IC50 ideals dependant on AstraZeneca researchers [19], [20] (Fig 1) for inhibition against the Ephrin type-B receptor 4 (EphB4), a membrane-bound receptor tyrosine kinase that binds to ephrin-B2 ligands destined to the areas of additional cells to induce angiogenic occasions. (careersfromscience.org)
Tyrosine kinases4
- EphB4 is a member of the largest family of receptor tyrosine kinases and is an important regulator of fundamental physiological and pathophysiological processes such as tissue patterning during development, angiogenesis and tumour progression [ 1 ]. (oncotarget.com)
- Considering the relevance of receptor tyrosine kinases and Eph in NSCLC, these seven mutations were assessed for change in the folding pattern using molecular dynamic simulation. (genominfo.org)
- Cell migration is influenced by chemodirectants including a large family of receptor tyrosine kinases collectively referred to as Ephs. (bio-techne.com)
- The mass spectrometric analysis revealed widespread and heterogeneous activation of both receptor and non-receptor tyrosine kinases. (ppbhg.org)
Membrane-bound receptor tyrosi1
- EphB4 is a membrane-bound receptor tyrosine kinase (RTK) commonly over-produced by many epithelial cancers but with low to no expression in most normal adult tissues. (oncotarget.com)
Extracellular7
- The Eph family of receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. (wikipedia.org)
- An EphB4-specific polyclonal antibody, targeting a region of 200 amino acids in the extracellular portion of EphB4, showed potent in vitro anti-cancer effects measured by an increase in apoptosis and a decrease in anchorage independent growth. (oncotarget.com)
- A monoclonal antibody which specifically targets this identified extracellular epitope of EphB4 significantly reduced breast cancer xenograft growth in vivo confirming that EphB4 is a useful target for ligand-mimicking antibody-based anti-cancer therapies. (oncotarget.com)
- Binding of the extracellular sequence of EphB4 receptor to its transmembrane ligand ephrinB2 protein on the surface of endothelial cells of blood vessels, stimulates angiogenesis and growth of new vessels from existing vasculature. (neurodegenerationresearch.eu)
- Furthermore, in vitro assays show that treatment of ephrinB2expressing endothelial cells with the extracellular domain of EphB4 stimulates cell sprouting and tube formation, processes considered crucial initial steps in angiogenesis, while transgenic mouse experiments indicate that the intracellular (cytoplasmic) domain of ephrinB2 protein is necessary for ephrinB2-dependent angiogenesis. (neurodegenerationresearch.eu)
- EphB4 protein has tumor suppressor activities and that regulation of cell proliferation, extracellular matrix remodeling, and invasive potential are important mechanisms of tumor suppression. (betalifesci.com)
- Structurally Eph receptors are similar to RTKs, comprises extracellular region, a ligand binding and fibronectin repeat domain, whereas intracellular has a juxtamembrane, kinase, and SAM domain. (genominfo.org)
Antibody2
- Peptide exclusion was used to identify the epitope targeted by this antibody within the cysteine-rich region of the EphB4 protein, a sequence defined as a potential ligand interacting interface. (oncotarget.com)
- Addition of antibody to cancer cells resulted in phosphorylation and subsequent degradation of the EphB4 protein, suggesting a mechanism that is ligand mimetic and tumour suppressive. (oncotarget.com)
Cysteine-rich region1
- All Eph receptors contain an N-terminal Ig-like domain, a cysteine-rich region with 19 conserved cysteines and two fibronectin type III domains. (bio-techne.com)
Transmembrane2
- secretase may affect angiogenesis by regulating processing of transmembrane protein ephrinB2, a critical step in EphB4-induced angiogenesis. (neurodegenerationresearch.eu)
- Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. (cancer.gov)
IC501
- Open up in another window Shape 1 The EphB4 IC50 ideals created via acoustic transfer with immediate dilution are considerably lower (even more biologically energetic) than when generated with tip-based transfer and serial dilutions.The ratio of the EphB4 IC50 values varies widely and correlates poorly using the calculated logP from the compounds (see also Desk S1). (careersfromscience.org)
Kinase12
- Ephrin receptors make up the largest subgroup of the receptor tyrosine kinase (RTK) family. (wikipedia.org)
- The epidermal growth factor receptor (EGFR) is a receptor tyrosine kinase (RTK) commonly targeted for inhibition by anti-cancer therapeutics. (biorxiv.org)
- The epidermal growth factor receptor (EGFR) is a HER-family receptor tyrosine kinase (RTK) that is involved in cell signaling in healthy tissue. (biorxiv.org)
- Mast cells are activated after receptor tyrosine kinase EphB4 phosphorylation. (yes4yes.com)
- Research title: "Evaluation of expression and function of the EphA2 receptor tyrosine kinase in canine and human osteosarcoma. (usask.ca)
- It is a single-pass type I membrane protein belonging to the ephrin receptor subfamily of protein kinase superfamily. (betalifesci.com)
- Ephs belong to the largest family of receptor tyrosine kinase and are highly conserved both sequentially and structurally. (genominfo.org)
- Receptor tyrosine kinase (RTKs), a sub-class of tyrosine kinase, regulates numerous physiological events such as cell growth, division, metabolism, and motility. (genominfo.org)
- PDGFR (platelet-derived growth factor receptor) is a group of cell surface tyrosine kinase receptors for members of the PDGF (platelet-derived growth factor) family. (glpbio.cn)
- GC62145 Chiauranib Chiauranib (CS2164) selectively inhibits multiple kinase targets aurora B kinase (AURKB), colony-stimulating factor 1 receptor (CSF1R), and vascular endothelial growth factor receptor (VEGFR)/platelet-derived growth factor receptor (PDGFR)/c-Kit , thereby inhibiting the rapid proliferation of tumor cells, enhancing the antitumor immunity, and inhibiting tumor angiogenesis, to achieve the anti-tumor efficacy. (glpbio.cn)
- One potential candidate identified from the screen was EphA2 a cell surface receptor tyrosine kinase implicated in development stem cell niche maintenance and cancer progression (14). (researchatlanta.org)
- Conversely, one report describes expansion of a biopsy-proven capillary malformation following partial surgical excision in an adult in whom the newly expanded capillary malformation expressed marked elevations of both tyrosine kinase receptor (Tie2) and its ligand angiopoietin-1 and no increase in VEGF. (medscape.com)
Serine1
- PP121 exhibits no significant effect on receptor serine/threonine kinases (RSTKs). (activebiopharma.com)
Inhibition2
- PP121 blocks the proliferation of tumor cells by direct inhibition of PI 3-K, mTOR, Src and the VEGF receptor. (activebiopharma.com)
- Our Western could be gene] introduce inappropertified in human intron in EphB4 inhibition and −786T>C polymorphisms. (iamlearningdisabled.com)
Ephrin-B ligands1
- Eph receptors that bind preferentially to ephrin-B ligands are referred to as EphB. (bio-techne.com)
Ligands3
- Ephrin receptors and their ligands, the ephrins, mediate numerous developmental processes, particularly in the nervous system. (wikipedia.org)
- Unified nomenclature for Eph family receptors and their ligands, the ephrins. (wikipedia.org)
- Despite significant promiscuity between other Eph family members and the ephrin ligands, the single physiologically-relevant ligand of the EphB4 receptor is ephrin-B2 [ 2 ]. (oncotarget.com)
Ligand-independent1
- EphB4 over-production promotes ligand-independent signaling pathways that increase cancer cell viability and stimulate migration and invasion. (oncotarget.com)
Inhibitor3
- In summary, we present a comprehensive landscape of Diazepam-Binding Inhibitor Fragment, human tyrosine phosphoproteome with EphB4 Diazepam-Binding Inhibitor Fragment, human as a promising Diazepam-Binding Inhibitor Fragment, human therapeutic target in pancreatic ductal adenocarcinoma. (ppbhg.org)
- GC39314 Tyrphostin AG1433 Tyrphostin AG1433 (AG1433, SU1433) is a selective platelet-derived growth factor receptor β (PDGFRβ) and vascular endothelial growth factor receptor 2 (VEGFR-2, Flk-1/KDR) inhibitor with IC50s of 5.0 μM and 9.3 μM, respectively. (glpbio.cn)
- GC38380 Vorolanib X-82 (Vorolanib, CM082) is an oral, multikinase, dual inhibitor of vascular endothelial growth factor receptor (VEGFR) and platelet-derived growth factor receptor (PDGFR) with antiangiogenic and antineoplastic activities. (glpbio.cn)
Expression4
- Research title: "Expression and function of the EphB4 receptor in canine and human osteosarcoma. (usask.ca)
- Immunohistochemistry-based validation using tissue microarrays from 346 patients with PDAC showed significant expression of EphB4 in 70% of patients. (ppbhg.org)
- Correlation analysis revealed that mRNA TNF receptor associated factor 4 (TRAF4) was associated with DLEU1 expression. (spandidos-publications.com)
- The potent endothelial cell mitogen vascular endothelial growth factor (VEGF)-A and its most active receptor VEGF-R2 expression are significantly increased in capillary malformation skin tissue compared with control skin. (medscape.com)
Tumor1
- Furthermore, EphB4 protein and the corresponding ligand Ephrin-B2 contribute to tumor growth in various human tumors. (betalifesci.com)
Sequence1
- A DNA sequence encoding the EPHB4 (NP_004435.3) (Met1-Ala539) was expressed with a C-terminal His tag. (betalifesci.com)
VEGFR2
- Venous valve structural and regulatory components that might be dysregulated in this schema include α9-integrin/fibronectin (FNIIIa), Ephrin B2/EphB4, FOXC2/Prox1/NFATC1, and VEGFR-3. (biomedcentral.com)
- VEGFR, vascular endothelial growth factor receptor. (biomedcentral.com)
GABA1
- The chorein deficiency has been also linked to upregulation of gephyrin and GABA(A) receptors. (medscape.com)
Vascular2
- Additional literature shows that the EphB4/ephrinB2 system is an important regulator of the development and function of the vascular system. (neurodegenerationresearch.eu)
- and Vascular Endothelial cadherin (VE-cadherin) and we made the novel observation (preliminary data) that treatment of endothelial cell cultures with EphB4 increases these angiogenic complexes. (neurodegenerationresearch.eu)
Mutations1
- Germline loss-of-function mutations in EPHB4 cause a second form of capillary malformation-arteriovenous malformation (CM-AVM2) deregulating RAS-MAPK signaling. (expasy.org)
Regulate1
- The juxtamembrane domain has two highly conserved tyrosine that regulate activation of catalytic core of the receptor. (genominfo.org)
Human1
- Research is not surprising manikin studies with human skim mid-LV cavity and EMMPRIN were recurrent endosomes in Chinese pationally, receptors are investigate through in this in an inframedic gastric cance among and control violacein-labeled CAI on the intrahepatic activity" disease, the marker events. (iamlearningdisabled.com)
Nuclear1
- OBs improve the success and differentiation of OC precursor cells by expressing receptor activator of nuclear aspect B ligand (RANKL) and macrophage-colony rousing aspect (M-CSF), and inhibiting osteoclastogenesis via secretion of osteoprotegerin (OPG), a decoy receptor for RANKL. (cell-signaling-pathways.com)
Molecular1
- The recombinant EPHB4 consists of 535 a.a. and predicts a molecular mass of 58.5 kDa. (betalifesci.com)
Family1
- Eph receptor belongs to the largest family of RTK. (genominfo.org)
Growth2
- This landmark ruling opened enormous omline bilities for the commercial growth of genetic en- gineering. (binaryoptionsforex625.com)
- OCs modulate OB features by mobilizing OBs to resorption sites through released cytokines such as for example transforming INK4B growth aspect (TGF-), or activating OB A-582941 supplier activity by immediate cell get in touch with via ephrinB2-EphB4 engagement [7, 8]. (cell-signaling-pathways.com)
Research1
- Research title: "Towards the identification of the receptor of a new bat alphacoronavirus. (usask.ca)