Receptors eph family. Medical search

A large family of receptor protein-tyrosine kinases that are structurally-related. The name of this family of proteins derives from original protein Eph (now called the EPHA1 RECEPTOR), which was named after the cell line it was first discovered in: Erythropoietin-Producing human Hepatocellular carcinoma cell line. Members of this family have been implicated in regulation of cell-cell interactions involved in nervous system patterning and development.

A GLYCOINOSITOL PHOSPHOLIPID MEMBRANE ANCHOR-containing ephrin with a high affinity for the EPHA3 RECEPTOR. Early in embryogenesis it is expressed at high levels in the MESENCEPHALON; SOMITES; branchial arches, and LIMB BUDS.

An eph family receptor found in variety of tissues including BRAIN. During embryogenesis, EphA4 receptor exhibits a diverse spatial and temporal patterns of expression suggesting its role in multiple developmental processes.

A transmembrane domain containing ephrin that is specific for EPHB1 RECEPTOR; EPHB2 RECEPTOR and EPHB3 RECEPTOR. It is widely expressed in a variety of developing and adult tissues.

Signaling proteins that are ligands for the EPH FAMILY RECEPTORS. They are membrane-bound proteins that are attached to the CELL MEMBRANE either through a GLYCOINOSITOL PHOSPHOLIPID MEMBRANE ANCHOR or through a transmembrane domain. Many of the ephrins are considered important intercellular signaling molecules that control morphogenic changes during embryogenesis.

An eph family receptor that is found primarily in adult BRAIN and variety of tissues in the developing embryo tissues. During embryonic development high levels of EphA3 receptor expression is seen in the nervous system and coincides with neuronal cell migration, suggesting a role for this protein in axonal pathfinding.

An eph family receptor found widely expressed in embryo tissues, including the NERVOUS SYSTEM. In the BRAIN high levels of EphA7 expression occurs in the anterior tectum, medulla, RHOMBENCEPHALON, and SUBCOMMISSURAL ORGAN. Several isoforms of the protein occur due to multiple alternative spicing of the EphA7 mRNA.

An eph family receptor found widely expressed in embryonic and adult tissues. High levels of EphB2 receptor are observed in growing AXONS and NERVE FIBERS. Several isoforms of the protein exist due to multiple alternative mRNA splicing.

An eph family receptor found primarily in differentiated neuronal tissues. Several isoforms of EphA5 receptor occur due to multiple alternative RNA splicing. The protein is prominently expressed in the NEURONS of the LIMBIC SYSTEM during development and throughout adult life, suggesting its role in the plasticity of limbic structure and function.

A GLYCOINOSITOL PHOSPHOLIPID MEMBRANE ANCHOR containing ephrin found in developing tectum. It has been shown to mediate the bundling of cortical axons and repel the axonal growth of retinal ganglia axons. It is found in a variety of adult tissues of BRAIN; HEART; and KIDNEY.

The founding member of the EPH FAMILY RECEPTORS. It was first cloned from an erythropoietin-producing human hepatocellular carcinoma cell line and is highly conserved among many mammalian species. Overproduction of the EphA1 receptor is associated with tumors and tumor cells of epithelial origin. It is also expressed at high levels in LIVER; LUNG; and KIDNEY; which is in contrast to many other members of the Eph receptor that are found primarily in tissues of the nervous system.

A transmembrane domain containing ephrin that binds with high affinity to EPHB1 RECEPTOR; EPHB3 RECEPTOR; and EPHB4 RECEPTOR. Expression of ephrin-B2 occurs in a variety of adult tissues. During embryogenesis, high levels of ephrin-B2 is seen in the PROSENCEPHALON; RHOMBENCEPHALON; developing SOMITES; LIMB BUD; and bronchial arches.

An eph family receptor found in a variety of adult and embryonic tissues. Unlike the majority of proteins in this class there is little or no expression of EphB4 receptor in the BRAIN. It has been found at high levels in developing mammary glands and in invasive mammary tumors.

A GLYCOINOSITOL PHOSPHOLIPID MEMBRANE ANCHOR containing ephrin with a high affinity for the EPHA3 RECEPTOR; EPHA5 RECEPTOR; EPHA6 RECEPTOR; EPHA7 RECEPTOR; and EPHA8 RECEPTOR. It is found primarily in NERVE TISSUE.

An ephrin that was originally identified as the product of an early response gene induced by TUMOR NECROSIS FACTORS. It is linked to the CELL MEMBRANE via a GLYCOINOSITOL PHOSPHOLIPID MEMBRANE ANCHOR and binds EPHA2 RECEPTOR with high affinity. During embryogenesis high levels of ephrin-A1 are expressed in LUNG; KIDNEY; SALIVARY GLANDS; and INTESTINE.

An eph family receptor found exclusively in BRAIN. EphA8 receptors may play a role in the axonal guidance of a subset of tectal commissural NEURONS.

A GLYCOINOSITOL PHOSPHOLIPID MEMBRANE ANCHOR containing ephrin found in variety of adult tissue such as KIDNEY; LUNG; COLON and OVARY. During embryonic development, ephrin-A4 is expressed in the HIPPOCAMPUS and CEREBRAL CORTEX. It binds preferentially to ephA receptors (EPH FAMILY RECEPTORS) with the exception of the EPHA1 RECEPTOR.

An Eph family receptor found abundantly in tissues of epithelial origin. It is expressed in a diverse array of tissues during embryonic development, suggesting that it may play a role in embryogenesis. In adult tissues high levels of the receptor are expressed in the LUNG; SKIN; SMALL INTESTINE and OVARY.

An eph family receptor found primarily in BRAIN and THYMUS. The EphB6 receptor is unusual in that its tyrosine kinase domain shares little homology with other members of this class. The unusual tyrosine kinase domain of this receptor appears to result in its lack of tyrosine kinase activity.

An eph family receptor found primarily in the nervous system. In the embryonic BRAIN EphB1 receptor expression occurs in the mantle layer and increases with the progression of embryogenesis. In adult brain it is found in the several regions including the CEREBELLUM; CEREBRAL CORTEX; and CAUDATE NUCLEUS; and PUTAMEN.

A class of cellular receptors that have an intrinsic PROTEIN-TYROSINE KINASE activity.

A transmembrane domain containing ephrin. Although originally found to be specific for the EPHB3 RECEPTOR it has since been shown to bind a variety of EPH FAMILY RECEPTORS. During embryogenesis ephrin-B3 is expressed at high levels in the ventral neural tube. In adult tissues, it is found primarily in the BRAIN and HEART.

Proteins that are preferentially expressed or upregulated during FETAL DEVELOPMENT.

A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed)

Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.

Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action during the developmental stages of an organism.

The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.

Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.

An eph family receptor found in a number of tissues including BRAIN; LUNG; KIDNEY; PANCREAS; INTESTINE; and HEART. During embryogenesis EphB3 receptor is expressed at high levels in the brain.

The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.

An eph family receptor found at high levels in adult THYMUS and RETINA. In embryonic tissues it is found in many developing organs.

Bulbous enlargement of the growing tip of nerve axons and dendrites. They are crucial to neuronal development because of their pathfinding ability and their role in synaptogenesis.

The posterior of the three primitive cerebral vesicles of an embryonic brain. It consists of myelencephalon, metencephalon, and isthmus rhombencephali from which develop the major BRAIN STEM components, such as MEDULLA OBLONGATA from the myelencephalon, CEREBELLUM and PONS from the metencephalon, with the expanded cavity forming the FOURTH VENTRICLE.

New ether-a-go-go K(+) channel family members localized in human telencephalon. (1/294)

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. (2/294)

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. (3/294)

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. (4/294)

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. (5/294)

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. (6/294)

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. (7/294)

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. (8/294)

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)

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.

Ephrin-A2 is a type of protein that belongs to the ephrin family. It is a membrane-bound ligand for Eph receptors, which are tyrosine kinase receptors located on the cell surface. Ephrin-A2 and Eph receptors play critical roles in various biological processes, including axon guidance, tissue boundary formation, and tumorigenesis.

Ephrin-A2 is encoded by the EFNB2 gene and is expressed on the cell membrane as a glycosylphosphatidylinositol (GPI)-anchored protein. It can interact with several Eph receptors, including EphA3, EphA4, EphA5, and EphA7, leading to bidirectional signaling that regulates cell-cell interactions and communication.

In the nervous system, ephrin-A2 and its receptors are essential for the development and maintenance of neural circuits. They help to establish precise connections between neurons by mediating repulsive interactions that guide axon growth and fasciculation. Additionally, ephrin-A2 has been implicated in various pathological conditions, such as cancer, where it can contribute to tumor progression and metastasis.

EphA4 is a type of receptor tyrosine kinase that belongs to the Eph (Erythropoietin-producing hepatocellular) family of receptors. It is a transmembrane protein found on the surface of various types of cells, including neurons and glial cells in the nervous system.

EphA4 receptors play critical roles in several biological processes, such as cell migration, axon guidance, and synaptic plasticity during development and throughout adulthood. They interact with ephrin proteins, which are ligands (molecules that bind to receptors) found on adjacent cells. The interaction between EphA4 and ephrins triggers a cascade of intracellular signaling events that ultimately influence cell behavior.

In summary, EphA4 is a type of receptor involved in cell-cell communication, particularly during the development and functioning of the nervous system. Its dysfunction has been implicated in several neurological disorders, such as spinal cord injuries, Alzheimer's disease, and various forms of cancer.

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.

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.

EphA3 is a type of receptor tyrosine kinase (RTK) that belongs to the Eph family of receptors. It is a transmembrane protein involved in cell-cell communication and signal transduction. The EphA3 receptor specifically binds to ephrin-A5, its ligand, leading to various intracellular signaling events that regulate cell behavior, including cell migration, adhesion, and differentiation.

EphA3 is widely expressed in various tissues, including the nervous system, hematopoietic cells, and epithelial cells. In the nervous system, EphA3 plays a crucial role in axon guidance and neuronal positioning during development. In hematopoietic cells, it has been implicated in the regulation of immune cell function and the development of certain types of leukemia.

Mutations or aberrant expression of EphA3 have been associated with several diseases, including cancer, making it a potential target for therapeutic intervention.

EphA7 is a type of receptor that belongs to the EPH receptor tyrosine kinase family. These receptors are involved in intracellular signaling and play crucial roles in various biological processes, including cell growth, differentiation, and migration.

EphA7 receptors are specifically activated by ephrin-A ligands, which are membrane-bound proteins expressed on adjacent cells. When an ephrin-A ligand binds to an EphA7 receptor, it triggers a cascade of intracellular signaling events that can affect various cellular functions.

EphA7 receptors have been implicated in several physiological and pathological processes, including nervous system development, angiogenesis, and cancer. In the nervous system, EphA7 receptors help to establish connections between neurons and guide their migration during development. In cancer, abnormal expression or activation of EphA7 receptors has been linked to tumor growth, progression, and metastasis.

It's worth noting that while I strive to provide accurate and up-to-date information, medical definitions can be complex and nuanced. Therefore, it may be helpful to consult authoritative medical resources or speak with a healthcare professional for more detailed information on this topic.

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.

EphA5 is a type of receptor tyrosine kinase that belongs to the Eph receptor family. Eph receptors are the largest subfamily of receptor tyrosine kinases and play critical roles in various biological processes, including cell migration, axon guidance, and tissue boundary formation during embryonic development.

EphA5 receptor specifically binds to ephrin-A5 ligand, which is a member of the ephrin family of membrane-bound proteins. The binding of ephrin-A5 to EphA5 triggers bidirectional signaling, meaning that both the receptor and the ligand can transmit signals into their respective cells. This interaction leads to various cellular responses, such as changes in cytoskeletal organization, cell adhesion, and intracellular signaling pathways.

EphA5 has been implicated in several physiological and pathological processes, including neural development, vascular remodeling, tumor angiogenesis, and cancer metastasis. Mutations in the EPHA5 gene have been associated with various human diseases, such as intellectual disability, epilepsy, and congenital heart defects.

Ephrin-A5 is a type of protein that belongs to the ephrin family. Ephrins are membrane-bound proteins that interact with Eph receptors, which are tyrosine kinase receptors found on the surface of cells. The interaction between ephrins and Eph receptors plays a crucial role in the development and function of the nervous system, including axon guidance, cell migration, and synaptic plasticity.

Ephrin-A5 is specifically classified as a glycosylphosphatidylinositol (GPI)-anchored protein, which means it is attached to the outer layer of the cell membrane through a GPI anchor. It is primarily expressed in various tissues, including the brain, heart, and lungs.

In the nervous system, Ephrin-A5 and its receptor, EphA4, are involved in repulsive guidance cues that help to establish proper neuronal connections during development. Dysregulation of this interaction has been implicated in several neurological disorders, such as spinal cord injuries, Alzheimer's disease, and schizophrenia.

EphA1 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-A5, and an intracellular domain with tyrosine kinase activity.

EphA1 receptors are involved in various biological processes, including cell migration, axon guidance, and tissue boundary formation during embryonic development. They also play a role in angiogenesis, neuroprotection, and tumorigenesis in adults.

The binding of ephrin-A5 to EphA1 receptors triggers bidirectional signaling, affecting both the receptor-expressing cell and the ephrin-presenting cell. This interaction can lead to repulsion, adhesion, or collapse of the growth cone, depending on the context and the specific Eph/ephrin pair involved.

Mutations in EphA1 have been associated with various diseases, including cancer, neurodevelopmental disorders, and cardiovascular disease.

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.

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.

Ephrin-A3 is a type of protein that belongs to the ephrin family. Ephrins are membrane-bound proteins that play crucial roles in various biological processes, including cell signaling and communication during development. Specifically, Ephrin-A3 binds to Eph receptors, which are tyrosine kinase receptors found on the surface of neighboring cells. This binding leads to bidirectional signals that regulate cell adhesion, repulsion, and migration, thereby helping to establish proper tissue and organ architecture during development. Additionally, Ephrin-A3 has been implicated in various physiological and pathological processes, such as angiogenesis, neurogenesis, and cancer.

Ephrin-A1 is a type of protein that belongs to the ephrin family. It is a membrane-bound ligand for Eph receptors, which are tyrosine kinase receptors located on the cell surface. Ephrin-A1 and its receptors play critical roles in various biological processes, including cell migration, axon guidance, and tissue boundary formation during embryonic development. Ephrin-A1 is also involved in angiogenesis, tumorigenesis, and metastasis in cancer. It is encoded by the EFNAs gene in humans.

EphA8 is a type of receptor tyrosine kinase (RTK) that belongs to the Eph receptor subfamily, which is the largest subfamily of RTKs. These receptors are involved in various biological processes, including cell-cell communication, cell migration, and tissue boundary formation during development.

EphA8 receptors specifically bind to ephrin-A ligands, which are membrane-bound proteins expressed on adjacent cells. The binding of ephrin-A to EphA8 initiates a bidirectional signaling process that affects both the receptor-expressing and ligand-expressing cells. This interaction can result in either attraction or repulsion between the cells, depending on the context and the specific ephrin-A/EphA8 pair involved.

In summary, EphA8 is a cell surface receptor that binds to ephrin-A ligands to mediate cell-cell communication and regulate various developmental processes.

Ephrin-A4 is a type of protein that belongs to the ephrin family. Ephrins are membrane-bound proteins that play crucial roles in various biological processes, including cell signaling and communication during development. Specifically, Ephrin-A4 is a ligand for Eph receptors, which are tyrosine kinase receptors located on the cell membrane.

Ephrin-A4 is composed of a glycosylphosphatidylinositol (GPI) anchor that attaches it to the cell membrane and an extracellular domain that interacts with Eph receptors. When Ephrin-A4 binds to an Eph receptor on a neighboring cell, it triggers a cascade of intracellular signaling events that can regulate various cellular processes, such as cell adhesion, migration, and proliferation.

In the medical field, Ephrin-A4 has been studied in the context of various diseases, including cancer. For example, abnormal expression of Ephrin-A4 has been observed in several types of tumors, and it has been suggested to play a role in tumor progression and metastasis. However, more research is needed to fully understand the functional significance of Ephrin-A4 in health and disease.

EphA2 is a type of receptor tyrosine kinase (RTK) that belongs to the Eph (Erythropoietin-producing hepatocellular) family of receptors. It is a transmembrane protein found on the surface of many types of cells, including epithelial, endothelial, and cancer cells.

EphA2 receptors play critical roles in various biological processes such as cell growth, survival, migration, and angiogenesis. They interact with their ligands, called ephrins, which are also transmembrane proteins expressed on adjacent cells. The interaction between EphA2 and ephrins triggers bidirectional signaling that can regulate the adhesion, repulsion, or movement of cells in response to contact with other cells.

In cancer biology, EphA2 receptors have been implicated in tumor progression and metastasis. Overexpression of EphA2 has been observed in various types of human cancers, including breast, lung, prostate, ovarian, and colon cancer. High levels of EphA2 are often associated with poor clinical outcomes, making it an attractive therapeutic target for cancer treatment.

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.

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.

Receptor Protein-Tyrosine Kinases (RTKs) are a type of transmembrane receptors found on the cell surface that play a crucial role in signal transduction and regulation of various cellular processes, including cell growth, differentiation, metabolism, and survival. They are called "tyrosine kinases" because they possess an intrinsic enzymatic activity that catalyzes the transfer of a phosphate group from ATP to tyrosine residues on target proteins, thereby modulating their function.

RTKs are composed of three main domains: an extracellular domain that binds to specific ligands (growth factors, hormones, or cytokines), a transmembrane domain that spans the cell membrane, and an intracellular domain with tyrosine kinase activity. Upon ligand binding, RTKs undergo conformational changes that lead to their dimerization or oligomerization, which in turn activates their tyrosine kinase activity. Activated RTKs then phosphorylate specific tyrosine residues on downstream signaling proteins, initiating a cascade of intracellular signaling events that ultimately result in the appropriate cellular response.

Dysregulation of RTK signaling has been implicated in various human diseases, including cancer, diabetes, and developmental disorders. As such, RTKs are important targets for therapeutic intervention in these conditions.

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.

Fetal proteins are a type of proteins that are produced by the fetus during pregnancy and can be detected in various biological samples, such as amniotic fluid or maternal blood. These proteins can provide valuable information about the health and development of the fetus. One commonly studied fetal protein is human chorionic gonadotropin (hCG), which is produced by the placenta and can be used as a marker for pregnancy and to detect potential complications, such as Down syndrome or spinal cord defects. Other examples of fetal proteins include alpha-fetoprotein (AFP) and human placental lactogen (hPL).

A ligand, in the context of biochemistry and medicine, is a molecule that binds to a specific site on a protein or a larger biomolecule, such as an enzyme or a receptor. This binding interaction can modify the function or activity of the target protein, either activating it or inhibiting it. Ligands can be small molecules, like hormones or neurotransmitters, or larger structures, like antibodies. The study of ligand-protein interactions is crucial for understanding cellular processes and developing drugs, as many therapeutic compounds function by binding to specific targets within the body.

Membrane proteins are a type of protein that are embedded in the lipid bilayer of biological membranes, such as the plasma membrane of cells or the inner membrane of mitochondria. These proteins play crucial roles in various cellular processes, including:

1. Cell-cell recognition and signaling
2. Transport of molecules across the membrane (selective permeability)
3. Enzymatic reactions at the membrane surface
4. Energy transduction and conversion
5. Mechanosensation and signal transduction

Membrane proteins can be classified into two main categories: integral membrane proteins, which are permanently associated with the lipid bilayer, and peripheral membrane proteins, which are temporarily or loosely attached to the membrane surface. Integral membrane proteins can further be divided into three subcategories based on their topology:

1. Transmembrane proteins, which span the entire width of the lipid bilayer with one or more alpha-helices or beta-barrels.
2. Lipid-anchored proteins, which are covalently attached to lipids in the membrane via a glycosylphosphatidylinositol (GPI) anchor or other lipid modifications.
3. Monotopic proteins, which are partially embedded in the membrane and have one or more domains exposed to either side of the bilayer.

Membrane proteins are essential for maintaining cellular homeostasis and are targets for various therapeutic interventions, including drug development and gene therapy. However, their structural complexity and hydrophobicity make them challenging to study using traditional biochemical methods, requiring specialized techniques such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and single-particle cryo-electron microscopy (cryo-EM).

Developmental gene expression regulation refers to the processes that control the activation or repression of specific genes during embryonic and fetal development. These regulatory mechanisms ensure that genes are expressed at the right time, in the right cells, and at appropriate levels to guide proper growth, differentiation, and morphogenesis of an organism.

Developmental gene expression regulation is a complex and dynamic process involving various molecular players, such as transcription factors, chromatin modifiers, non-coding RNAs, and signaling molecules. These regulators can interact with cis-regulatory elements, like enhancers and promoters, to fine-tune the spatiotemporal patterns of gene expression during development.

Dysregulation of developmental gene expression can lead to various congenital disorders and developmental abnormalities. Therefore, understanding the principles and mechanisms governing developmental gene expression regulation is crucial for uncovering the etiology of developmental diseases and devising potential therapeutic strategies.

Signal transduction is the process by which a cell converts an extracellular signal, such as a hormone or neurotransmitter, into an intracellular response. This involves a series of molecular events that transmit the signal from the cell surface to the interior of the cell, ultimately resulting in changes in gene expression, protein activity, or metabolism.

The process typically begins with the binding of the extracellular signal to a receptor located on the cell membrane. This binding event activates the receptor, which then triggers a cascade of intracellular signaling molecules, such as second messengers, protein kinases, and ion channels. These molecules amplify and propagate the signal, ultimately leading to the activation or inhibition of specific cellular responses.

Signal transduction pathways are highly regulated and can be modulated by various factors, including other signaling molecules, post-translational modifications, and feedback mechanisms. Dysregulation of these pathways has been implicated in a variety of diseases, including cancer, diabetes, and neurological disorders.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

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.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

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.

Growth cones are specialized structures found at the tips of growing neurites (axons and dendrites) during the development and regeneration of the nervous system. They were first described by Santiago Ramón y Cajal in the late 19th century. Growth cones play a crucial role in the process of neurogenesis, guiding the extension and pathfinding of axons to their appropriate targets through a dynamic interplay with environmental cues. These cues include various guidance molecules, such as netrins, semaphorins, ephrins, and slits, which bind to receptors on the growth cone membrane and trigger intracellular signaling cascades that ultimately determine the direction of axonal outgrowth.

Morphologically, a growth cone consists of three main parts: the central domain (or "C-domain"), the peripheral domain (or "P-domain"), and the transition zone connecting them. The C-domain contains microtubules and neurofilaments, which provide structural support and transport materials to the growing neurite. The P-domain is rich in actin filaments and contains numerous membrane protrusions called filopodia and lamellipodia, which explore the environment for guidance cues and facilitate motility.

The dynamic behavior of growth cones allows them to navigate complex environments, make decisions at choice points, and ultimately form precise neural circuits during development. Understanding the mechanisms that regulate growth cone function is essential for developing strategies to promote neural repair and regeneration in various neurological disorders and injuries.

The rhombencephalon is a term used in the field of neuroanatomy, which refers to the most posterior region of the developing brain during embryonic development. It is also known as the hindbrain and it gives rise to several important structures in the adult brain.

More specifically, the rhombencephalon can be further divided into two main parts: the metencephalon and the myelencephalon. The metencephalon eventually develops into the pons and cerebellum, while the myelencephalon becomes the medulla oblongata.

The rhombencephalon plays a crucial role in several critical functions of the nervous system, including regulating heart rate and respiration, maintaining balance and posture, and coordinating motor movements. Defects or abnormalities in the development of the rhombencephalon can lead to various neurological disorders, such as cerebellar hypoplasia, Chiari malformation, and certain forms of brainstem tumors.

This gene belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have ... Ephnomenclaturecommittee (1997). "Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph ... Zhou R (1998). "The Eph family receptors and ligands". Pharmacol. Ther. 77 (3): 151-81. doi:10.1016/S0163-7258(97)00112-5. PMID ... EPH receptor A2 (ephrin type-A receptor 2) is a protein that in humans is encoded by the EPHA2 gene. ...

https://en.wikipedia.org/wiki/EPH_receptor_A2

Eph receptor signalling: from catalytic to non-catalytic functions. Oncogene. 2019 Sep;38(39):6567-6584. doi: 10.1038/s41388- ... Structural and functional characterisation of a new family of oncogenic signalling scaffolds Members of the PEAK family of ... The PEAK family of pseudokinases, their role in cell signalling and cancer. FEBS J. 2020 Oct;287(19):4183-4197. doi: 10.1111/ ... Receptor tyrosine pseudokinases have emerged as critical players in developmental processes. Deregulation of this class of ...

https://www.wehi.edu.au/researcher/isabelle-lucet/

... is a member of the Eph receptor family which binds members of the ephrin ligand family. There are two classes of receptors, ... EPH receptor B2; eph tyrosine kinase 3; EphB2; EPH-like kinase 5; ephrin type-B receptor 2; EPHT3MGC87492; EPTH3; Erk; ERKHek5 ... Soluble monomeric ligands bind the receptor but do not induce receptor autophosphorylation and activation (2). In vivo, the ... The ephrin/Eph families also appear to play a role in angiogenesis (3). ...

https://www.rndsystems.com/products/mouse-ephb2-biotinylated-antibody_baf467

The Eph family is a large family of receptor tyrosine kinases. Upon stimulation by ephrin ligands, Eph receptors activate ... Eph receptors and synapses. During development, Eph receptors mediate the repulsive axon guidance function of ephrins, a family ... Eph receptors and axonal pathfinding. Sek4 and Nuk are members of the Eph-related family of receptor protein-tyrosine kinases. ... Eph receptors: Interaction with ligands. The Eph-related family of receptor tyrosine kinases consists of at least 13 members, ...

https://www.sdbonline.org/sites/fly/hjmuller/ephrtk1.htm

Mouse monoclonal Eph receptor A2 antibody [Ka-5H5]. Validated in Flow Cyt, ICC/IF, cELISA and tested in Human. ... Receptor for members of the ephrin-A family. Binds to ephrin-A1, -A3, -A4 and -A5. Plays an important role in angiogenesis and ... Anti-Eph receptor A2 antibody [Ka-5H5]. See all Eph receptor A2 primary antibodies. ... Tyr protein kinase family. Ephrin receptor subfamily.. Contains 2 fibronectin type-III domains.. Contains 1 protein kinase ...

https://www.abcam.com/products/primary-antibodies/eph-receptor-a2-antibody-ka-5h5-ab59551.html

... sub-family F (GCN20), member 1), EPHB3: (EPH receptor B3), CCL5: (chemokine (C-C motif) ligand 5), PTPN21: (protein tyrosine ... phosphatase, non-receptor type 21), DDR1: (discoidin domain receptor family, member 1), 1-4: ACTB (actin, beta), 5-6: B2M (beta ... DDX5 is a highly conserved member of the DEAD box family and is known to be a RNA helicase that is involved in both pre-mRNA ... Moore DJ, Chambers JK, Wahlin JP, Tan KB, Moore GB, Jenkins O, Emson PC, Murdock PR: Expression pattern of human P2Y receptor ...

https://bmcgenomics.biomedcentral.com/articles/10.1186/1471-2164-8-140

... is a member of the Eph receptor family which binds members of the ephrin ligand family. There are two classes of receptors, ... Eph homology kinase-1; EPH receptor A5; EphA5; EPH-like kinase 7; ephrin type-A receptor 5; Hek7; receptor protein-tyrosine ... While soluble monomeric ligands bind the receptor, they do not induce receptor autophosphorylation and activation (2). In vivo ... It has been found that nearly all receptors and ligands are expressed in developing and adult neural tissue (3). The Eph/ephrin ...

https://www.rndsystems.com/cn/products/recombinant-rat-epha5-fc-chimera-protein-cf_541-a5

9. Zhang J, Hughes S. Role of the ephrin and Eph receptor tyrosine kinase families in angiogenesis and development of the ... Eph receptors represent the largest known family of receptors tyrosine kinases and are broadly divided into subclasses, EphA ... Diverse roles for the Eph family of receptor tyrosine kinases in carcinogenesis. Microsc Res Tech. 2002;59:58-67 ... Dohn M, Jiang J, Chen X. Receptor tyrosine kinase EphA2 is regulated by p53-family proteins and induces apoptosis. Oncogene. ...

https://medsci.org/v05p0121.htm

Another family of receptor tyrosine kinases that regulates pathologic angiogenesis is the Ephrin/Eph receptor pathway.[20] The ... PDGF binds PDGF receptor Î² (PDGFR-Î²), which stimulates pericyte recruitment and blood vessel maturation.[11] The FGF family ... Although a specific role in carcinogenesis has not been clarified, the role of Eph receptors in intercellular communication is ... The downstream effects of Eph receptor signaling include activation of integrins and other focal adhesion-associated proteins. ...

https://www.cancernetwork.com/view/anti-angiogenesis-therapy-gynecologic-malignancies

Family A receptors (EPHA) and ligands (EFNA) can act as oncogenes or tumor suppressors and are implicated in chemoresistance. ... EPHA1, EPHA2, EPHA4, EPHA7, EFNA3, EFNA4, and EFNA5 were upregulated in estrogen receptor- (ER-) and progesterone receptor- (PR ... Here, we examined the expression pattern and prognostic value of the EPHA/EFNA family in patients with breast cancer, including ... Our findings systematically elucidate the expression pattern and prognostic value of the EPHA/EFNA family in BrCa, which might ...

https://www.hindawi.com/journals/bmri/2021/5575704/

The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of ... Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to ... Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to ... Recombinant Human EPH Receptor A3, His-tagged E.coli. His. Inquiry. Human. EPHA3-301H. Recombinant Human EPH Receptor A3, GST- ...

https://www.creativebiomart.net/symbolsearch_epha3.htm

... the Hox gene family and the Ephrin/Eph receptor gene families appear to be the most important for establishing and maintaining ... 8] Negative regulators include the ephrins and their Eph receptors, as well as the class 3 semaphorins and their neuropilin/ ... The Shh family of genes play a pivotal role in inducing motor neurons throughout the length of the vertebrate neural tube; in ... The rostral division of the neural tube into its 3 main sections falls under the control of homeobox (Hox) family of genes. [4 ...

https://emedicine.medscape.com/article/845064-overview

Klein previously pioneered in the ephrin/Eph field. Should the hypothesis of the proposed research be correct, the findings ... Genetic analysis of a novel family of repulsive guidance cues acting through Unc5 receptors. ... FLRTs exert their functions by binding to Unc5 receptors. Moreover, FLRTs may also act as cell autonomous signaling receptors. ... Thus, FLRT proteins have the potential to engage in bi-directional signaling (forward via Unc5 receptors and reverse via ...

https://cordis.europa.eu/project/id/274541

... the expression of the Notch target genes of the HES and Hey families or the angiogenic factors and receptors of the ephrin/Eph ... The VEGFR family is composed of 3 type I tyrosine kinase receptors that regulate angiogenesis and lymphangiogenesis (19). Among ... The Notch family of receptors and its ligands are cell surface proteins that regulate cell fate determination through direct ... The Notch family of cell surface receptors and its ligands are highly conserved proteins that regulate cell fate determination ...

https://www.jci.org/articles/view/24311

EPH receptor A2 (ephrin type-A receptor 2) is a protein encoded by the EPHA2 gene and belongs to the ephrin receptor subfamily ... R. C. Scarpulla, "Metabolic control of mitochondrial biogenesis through the PGC-1 family regulatory network," Biochimica et ... Estrogen receptor 1. FOXO1:. Forkhead box protein O1, also known as forkhead in rhabdomyosarcoma, is a protein that in humans ... A. C. Bharti, Y. Takada, S. Shishodia, and B. B. Aggarwal, "Evidence that receptor activator of nuclear factor (NF)-κB ligand ...

https://www.hindawi.com/journals/omcl/2020/3656419/

EPH receptors and SRC families of kinases, and KIT, RET, TIE2, and FLT3 ...

https://reference.medscape.com/drug/iclusig-ponatinib-999800

During signal transduction across plasma membrane, Eph receptors, like other receptor tyrosine kinases, are involved in lateral ... These findings serve as an instructive example of the diversity of transmembrane domain formation within the same family of ... During signal transduction across plasma membrane, Eph receptors, like other receptor tyrosine kinases, are involved in lateral ... The Eph receptor tyrosine kinases and their membrane-bound ephrin ligands control a diverse array of cell-cell interactions in ...

https://www.rcsb.org/structure/2k9y

EFNA1 belongs to the ephrin (EPH) family. The EPH subfamily is the biggest group of receptor protein kinases and they take part ... Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein ... B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis ...

https://www.prospecbio.com/efna1_protein

... email Feldheim studies the role of the Eph family of receptor linkurl:tyrosine kinases;http://www.the-scientist.com/news/ ... and his family were home Saturday morning when fire engulfed their front porch and door. Feldheim and his family - including ...

https://www.the-scientist.com/the-nutshell/calif-animal-scientists-attacked-44897

PURPOSE: EphA2, a member of the Eph receptor tyrosine kinases family, is an important regulator of tumor initiation, ... retinoic acid receptor beta (RARB2), estrogen receptor 1 (ESR1), progesterone receptor (PGR), paired-like homeodomain 2 (PITX2 ... nerve growth factor receptor signaling pathway - Ras protein signal transduction - regulation of small GTPase mediated signal ... The RAS family genes encode small GTP-binding cytoplasmic proteins. Activated KRAS engages multiple effector pathways, notably ...

http://www.cancerindex.org/geneweb/RALGDS.htm

Furthermore, the C-terminal tail of this isozyme is very similar to those of the EPH family of receptor tyrosine kinases. The ... A family of NMR solution structures of the growth factor receptor-bound protein 2 (Grb2) SH2 domain has been determined by ... Ser/Thr protein kinases such as the Akt/Rac family, the beta-adrenergic receptor kinases, the mu isoform of PKC and the ... SIGNAL TRANSDUCTION PLECKSTRIN HOMOLOGY DOMAIN OF G-PROTEIN COUPLED RECEPTOR KINASE 2 (BETA-ADRENERGIC RECEPTOR KINASE 1), C- ...

https://smart.embl.de/smart/do_annotation.pl?DOMAIN=PH&START=86&END=187&E_VALUE=3.31e-5&TYPE=SMART&BLAST=LLIDGPVELKRGLQRQERHLFLFNDLFVSAKIKYNNNFKIKNKIRLTDMWTASCVEEVGEGNMNAQKSFVLGWPTVNFVATFSSPEQKDKWLSLLQRYIALE

https://smart.embl.de/smart/do_annotation.pl?DOMAIN=Blast:PH&START=3&END=111&E_VALUE=5e-18&TYPE=BLAST&BLAST=TTRNMGRLNLFSLDPDIDTLKLQKRDSFENELMIKPFEEKAAKRIMIICRALNFNLQGCVTENEYDPVTNIEPFFVSVALYDLRDNRKISADFHVDLNHPAVRQMLSGT

This gene belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have ... EPHA2; EPH receptor A2; ECK, EphA2; ephrin type-A receptor 2; soluble EPHA2 variant 1; tyrosine-protein kinase receptor ECK; ... Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain ... The ephrin receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their ...

https://www.creativebiomart.net/recombinant-human-epha2-protein-myc-ddk-tagged-c13-and-n15-labeled-510711.htm

NSP1 defines a novel family of adaptor proteins linking integrin and tyrosine kinase receptors to the c-Jun N-terminal kinase/ ... A novel signaling intermediate, SHEP1, directly couples Eph receptors to R-Ras and Rap1A. J Biol Chem. 1999; 274:31941-6. [PMID ... NSP1 Defines a novel family of adaptor proteins linking integrin and tyrosine kinase receptors to the c-jun N-terminal kinase/ ... Among the three NSP family members, only AND-34/BCAR3 induces anti-estrogen resistance in estrogen receptor (ERα)-positive ...

http://www.molvis.org/molvis/v15/a70/

... an epithelial cell receptor protein-tyrosine kinase in the eph/elk family of protein kinases. Mol. Cell. Biol. ... Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity. Science ( ... Pauley R. J., Soule H. D., Tait L., Miller F. R., Wolman S. R., Dawson P. J., Heppner G. H. The MCF10 family of spontaneously ... This antigen was identified as EphA2 (ECK). EphA2 is a Mr 130,000 receptor tyrosine kinase that is expressed on adult epithelia ...

https://aacrjournals.org/cancerres/article/61/5/2301/508433/EphA2-Overexpression-Causes-Tumorigenesis-of

The erythropoietin-producing hepatocellular carcinoma (Eph) receptors are the largest receptor tyrosine kinases family. EphB4 ... The CXC chemokine receptor 4 (CXCR4, CD184) is a member of the G protein-coupled receptor family that is expressed in most ... CC chemokine receptor 6 (CCR6) is one of the members of G protein-coupled receptor (GPCR) family that is upregulated in many ... CC chemokine receptor 6 (CCR6) is a member of the G protein-coupled receptor (GPCR) family that is highly expressed in B ...

https://www.preprints.org/search?search1=antigen%E2%80%93antibody%20biosensor&field1=keywords

This Mouse Ephrin Type-A Receptor 4 (EphA4) ELISA Kit from Innovative Research is intended for quantitative detection of mouse ... This gene belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have ... Expression system for standard: EPH receptor A4 (ephrin type-A receptor 4) is a protein that in humans is encoded by the EPHA4 ... Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain ...

https://www.innov-research.com/products/id688-mouse-ephrin-type-a-receptor-4-epha4-elisa-kit

... versus venous endothelial cells is also poorly understood but recent findings on the distribution of ephrins and Eph receptors ... QH-1 and vascular endothelial growth factor receptor 2 (VEGFR-2) both appear to label these cells as they adopt a mesenchymal ... Since VEGFR-2 is the earliest known VEGF receptor this suggests that VEGF is not involved in angioblast induction. VEGF does ... QH-1 and vascular endothelial growth factor receptor 2 (VEGFR-2) both appear to label these cells as they adopt a mesenchymal ...

https://experts.syr.edu/en/publications/the-role-of-fgf-and-vegf-in-angioblast-induction-and-migration-du

... is to highlight the mechanisms involved in creating and refining such well-defined maps in the brain with a focus on the Eph ... and ephrin families of axon guidance cues. We first describe the transgenic models where ephrin-A expression has been ... Ephrins bind selectively to Eph receptors from the same class, with the exception of the EphA4 receptor that binds to ephrin-As ... The best-known example of this is the Eph and ephrin families of axon guidance molecules, which are the focus of this review. ...

https://www.mdpi.com/1422-0067/24/8/6966

The origins of arterial versus venous endothelial cells is also poorly understood but recent findings on the distribution of ephrins and Eph receptors suggest that molecular differences exist prior to the onset of circulation. (syr.edu)
Such may be the case using the ErbB family members neuregulins 1 and 2, either which can bind ErbB-3 or ErbB-4 receptors (47), or the promiscuous relationships between matching subclasses of ephrins and Eph receptors (26, 27). (woofahs.com)
Ephrins and Eph receptors are especially highly expressed in the embryonic nervous system, where their signalling is important for proper axonal pathfinding and to establish topographic projections [1-3]. (123dok.org)

Eph/ephrin signal transduction occurs not only in the receptor-expressing cell but also in the ligand-expressing cell via bidirectional signaling [ 5 ]. (hindawi.com)
A possible role of membrane lipid rafts in relation to Eph transmembrane domain oligomerization and Eph signal transduction was also discussed. (rcsb.org)

The present project aims to study the role and mechanism of action of the Fibronectin Leucine-Rich Transmembrane (FLRT) family protein in axon guidance and cell migration during mouse central nervous system (CNS) development. (europa.eu)
Spatial structure of dimeric transmembrane domain of EphA2 receptor embedded into lipid bicelle was obtained by solution NMR, showing a left-handed parallel packing of the transmembrane helices (535-559)(2). (rcsb.org)
Importantly, a similar motif AX(3)GX(3)G as was found is responsible for right-handed dimerization of transmembrane domain of the EphA1 receptor. (rcsb.org)
These findings serve as an instructive example of the diversity of transmembrane domain formation within the same family of protein kinases and seem to favor the assumption that the so-called rotation-coupled activation mechanism may take place during the Eph receptor signaling. (rcsb.org)
Cell membranes are highly enriched in signaling receptors, transmembrane mechanosensors, pumps and channels, and, depending on their makeup, can recruit and retain a pool of mechanosensors important in the field of mechanobiology. (mechanobio.info)
Typically, EphA receptors bind to glycosylphosphatidylinositol anchor (GPI)-linked ephrin A proteins and EphB receptors bind to transmembrane ephrin B proteins. (silverchair.com)
Highly promiscuous, it has the unique property among Eph receptors to bind and to be physiologically activated by both GPI-anchored ephrin-A and transmembrane ephrin-B ligands including EFNA1 and EFNB3. (nih.gov)

EphA5, also known as Ehk1, Bsk, Cek7, Hek7, and Rek7 (1), is a member of the Eph receptor family which binds members of the ephrin ligand family. (rndsystems.com)
Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. (creativebiomart.net)
Although both development factors have got well-defined receptor companions, VEGF-A binds to PDGFRs on mesenchymal stem cells (5). (woofahs.com)
Eph binds to respective ephrin ligand, through the ligand binding domain and forms a tetrameric complex to activate the kinase domain. (genominfo.org)

Our lab seeks to understand how the protein kinase family organises complex intracellular communication networks. (edu.au)
The intracellular domains of the EphB6 and EphA10 receptor tyrosine pseudokinases function as dynamic signalling hubs. (edu.au)
A dominant negative form of the GTPase Rho1 , a potential intracellular effector of Eph, led to hyper-aroused flies, memory impairment, less anticipatory behaviour and neurophysiological changes. (sdbonline.org)
Thus, FLRT proteins have the potential to engage in bi-directional signaling ('forward' via Unc5 receptors and 'reverse' via their own intracellular domain), an original and innovative concept which Dr. Klein previously pioneered in the ephrin/Eph field. (europa.eu)
Moreover, Eph/ephrin signalling can be bi-directional, with intracellular pathways operating downstream of both the Eph receptor (forward signalling) and the ephrin ligand (reverse signalling) ( Kullander and Klein, 2002 ). (silverchair.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)

Soluble monomeric ligands bind the receptor but do not induce receptor autophosphorylation and activation (2). (rndsystems.com)
The EphA receptors (A1-A9) bind to EphrinA ligands, a group of glycosyl phosphatidylinositol-linked membrane proteins and EphB receptors (B1-B6) interact with EphrinB ligands [ 9 ]. (medsci.org)
The receptors are also categorized as A or B according to the type of ligand they bind to. (hindawi.com)
The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. (embl.de)
Ephrins bind promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. (bicellscientific.com)

Ephrins, also known as ephrin ligands, and Eph receptors (Ephs), which are RTKs, are key regulators of physiological and pathological processes involved in development and disease, such as cellular motility, cell repulsion, and cell adhesion [ 4 ]. (hindawi.com)

Both receptors and ligands are membrane-bound proteins that require direct cell-cell interaction for activation. (hindawi.com)
Eph and ephrin proteins interact with a number of other ligand/receptor systems to influence how cells translate environmental signals to orchestrate morphogenetic events. (silverchair.com)

Receptor tyrosine kinases have important roles in the development and progression of human tumors [ 8 ]. (medsci.org)
EPHA1, EPHA2, EFNA3, and EFNA4 mRNA expression was significantly higher in human epidermal growth factor receptor 2- (HER2-) positive tumors than in HER2-negative tumors. (hindawi.com)
Several Ephrin A (EPHA/EFNA) family members are overexpressed or downregulated in a variety of tumors, suggesting that they act as oncogenes or as tumor suppressors according to the cellular context [ 9 ]. (hindawi.com)
Recent studies have identified overexpression of HER2 or epidermal growth factor receptor in some tumors and used this knowledge to develop successful approaches for therapeutic targeting of cancer cells (2) . (aacrjournals.org)
However, overexpression of HER2 and epidermal growth factor receptor is limited to a subset of tumors, which creates a need to identify other tyrosine kinases that are responsible for cancer progression and pathogenesis. (aacrjournals.org)

Eph receptors represent the largest known family of receptors tyrosine kinases and are broadly divided into subclasses, EphA and EphB. (medsci.org)
Eph receptors are subdivided into two subclasses, termed EphA and EphB, based on sequence similarity and their preference for binding a particular subclass of ephrins. (silverchair.com)
Such repression persists after Eph receptor activation, but is overridden by Eph receptor inhibition with EphA4/Fc in neonatal cultured cerebellar slices as well as mature acute cerebellar slices, following in vivo infusion of the EphA4/Fc inhibitor and in EphB receptor-deficient mice. (123dok.org)
For example, in EphB1/ EphB2/EphB3-deficient mice dendritic spines (the small protru-sions bearing postsynaptic structures) have reduced density and size [3,7,8] while activation of EphB receptors by ephrins induces rapid dendritic spine formation [7,9]. (123dok.org)
Based on sequence homology, Eph and ephrin have been classified into EphA/EphrinA and EphB/EphrinB class of families [ 2 ]. (genominfo.org)

EPH receptor A2 (ephrin type-A receptor 2) is a protein that in humans is encoded by the EPHA2 gene. (wikipedia.org)
[4] EphB2 and EphA2 of the Eph tyrosine kinase receptor (RTK) family can also be cleaved by TF/VIIa. (wikidoc.org)

A role for a Drosophila Eph receptor tyrosine kinase (Eph) in the control of photoreceptor axon and cortical axon topography in the developing visual system is described. (sdbonline.org)
Thomas, John B. / Drosophila Eph receptor guides specific axon branches of mushroom body neurons . (arizona.edu)

This gene belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. (wikipedia.org)
Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. (wikipedia.org)
The EPH subfamily is the biggest group of receptor protein kinases and they take part in vital nervous system function and development. (prospecbio.com)

Eph receptors constitute the largest family of receptor tyrosine kinases (RTKs). (silverchair.com)
Ephs belong to the largest family of receptor tyrosine kinase and are highly conserved both sequentially and structurally. (genominfo.org)
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)

Eph receptors and ephrin signaling pathways: a role in bone homeostasis. (ox.ac.uk)
Hence gaining a knowledge of the system and pathways that promote Eph receptor and ephrin signaling and exactly how they are governed will probably have got biomedical importance. (cancerrealitycheck.com)
Eph-ephrin regulates many downstream pathways that lead to physiological events such as cell migration, proliferation, and growth. (genominfo.org)

In vivo , the ligands and receptors display reciprocal expression (3). (rndsystems.com)
The interaction between ligands and receptors via bidirectional signaling and its involvement in cancer biology are mediated by complex processes [ 7 , 8 ]. (hindawi.com)

EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. (wikipedia.org)
In the embryo, zygotic transcription of Eph is confined to the nervous system. (sdbonline.org)
In contrast to the large vertebrate Eph/Ephrin family, Drosophila has a single Eph receptor and a single Ephrin ligand, both of which are expressed within the developing nervous system. (arizona.edu)

Roles for Eph receptor tyrosine kinase signaling in the formation of topographic patterns of axonal connectivity have been well established in vertebrate visual systems. (sdbonline.org)
Eph receptors and their associated ligands, ephrins, play critical roles in a number of cellular processes including immune regulation, neuronal development and cancer metastasis. (ox.ac.uk)
The Eph receptors and their membrane-bound ligands ephrins play important roles in a variety of biological processes such as for example cell adhesion and movement. (cancerrealitycheck.com)

Receptor tyrosine kinases (RTKs) play an important role in a variety of cellular processes in cancer [ 3 ]. (hindawi.com)
Receptor tyrosine kinase (RTKs), a sub-class of tyrosine kinase, regulates numerous physiological events such as cell growth, division, metabolism, and motility. (genominfo.org)

Ser/Thr protein kinases such as the Akt/Rac family, the beta-adrenergic receptor kinases, the mu isoform of PKC and the trypanosomal NrkA family. (embl.de)

To further define which neurons express Eph, antibodies were generated to the cytoplasmic portion of the Eph protein. (sdbonline.org)
Immunostaining with an affinity-purified mouse antibody reveals that Eph is highly targeted to axons and growth cones of developing neurons within the VNC. (sdbonline.org)
Based upon the numbers and morphology of the staining axons, Eph is expressed by a large subset of interneurons and does not appear to be expressed by motor neurons (Scully, 1999). (sdbonline.org)
Currently, Hudson and co-workers are investigating the pivotal role of the Eph receptors and ephrin ligands in gustatory neurons and chemotaxis. (kennesaw.edu)
In Eph mutants, these neurons bifurcate normally, but in many cases the dorsal branch fails to project to its appropriate target area. (arizona.edu)

The transcriptional levels of EPHA/EFNA family members were correlated with intrinsic subclasses of breast cancer. (hindawi.com)

Although uniform across the developing eye, Eph is expressed in a concentration gradient appropriate for conveying positional information during cortical axon guidance in the second-order optic ganglion, the medulla. (sdbonline.org)
Growth-cone collapse induced by ephrin-As, a family of repulsive axon guidance molecules, is impaired upon R62D expression, resulting in perseverance of ring-shaped F-actin filaments. (jneurosci.org)
The conserved Eph receptors and their Ephrin ligands regulate a number of developmental processes, including axon guidance. (arizona.edu)
Surprisingly, and in contrast to previous results using RNA-interference techniques, embryos completely lacking Eph function show no obvious axon guidance defects. (arizona.edu)

A trans-interaction of Eph-ephrin followed by heterotetramer formation activates the signaling cascade and transforms the kinase domain from closed to open conformation which in-turn, expose the ATP binding pocket [ 5 ]. (genominfo.org)

The Eph receptor tyrosine kinases and their membrane-bound ephrin ligands control a diverse array of cell-cell interactions in the developing and adult organisms. (rcsb.org)

Eph receptors lie functionally at the interface between pattern formation and morphogenesis. (silverchair.com)

The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. (creativebiomart.net)

The ephrin receptors are divided into two groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. (wikipedia.org)
There are two classes of receptors, designated A and B. Both the A and B class receptors have an extracellular region consisting of a globular domain, a cysteine-rich domain, and two fibronectin type III domains. (rndsystems.com)

These observations reveal a conserved role for Eph kinases as determinants of topographic map formation in vertebrates and invertebrates (Dearborn, 2002). (sdbonline.org)
http://www.santacruzsentinel.com/ci_10080054?source=email Feldheim studies the role of the Eph family of receptor linkurl:tyrosine kinases;http://www.the-scientist.com/news/display/54773/ and their ligands, the linkurl:ephrins,;http://www.the-scientist.com/article/display/19418/ in the development of the mouse visual system. (the-scientist.com)
In the search for signals that cause breast cancer, many lines of investigation have linked cancer with elevated expression or altered function of receptor tyrosine kinases (1) . (aacrjournals.org)
Eph receptor tyrosine kinases are involved in many cellular processes. (123dok.org)
Ephrin ligands and their receptors, the Eph receptor (Eph) tyrosine kinases, are cell surface molecules that mediate commu-nication between cells. (123dok.org)
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)

The receptors are activated upon binding of specific ligands which include EPIDERMAL GROWTH FACTORS, and NEUREGULINS. (bvsalud.org)

Here, we show that Eph and Ephrin can act as a functional receptor-ligand pair in vivo. (arizona.edu)
When electrical activity is blocked in vivo by tetrodotoxin leading to a high spine density in Purkinje cell proximal dendrites, stimulation of Eph receptor activation recapitulates the spine repressive effects of climbing fibres. (123dok.org)

Eph and ephrin are membrane-bound and thus regulate cell-cell interaction, migration, partitioning, and cell adhesion [ 3 ]. (genominfo.org)
The juxtamembrane domain has two highly conserved tyrosine that regulate activation of catalytic core of the receptor. (genominfo.org)

This Mouse Ephrin Type-A Receptor 4 (EphA4) ELISA Kit from Innovative Research is intended for quantitative detection of mouse EphA4 in cell culture supernates, serum and plasma (heparin, EDTA). (innov-research.com)
Expression system for standard: EPH receptor A4 (ephrin type-A receptor 4) is a protein that in humans is encoded by the EPHA4 gene. (innov-research.com)

EFNA1 belongs to the ephrin (EPH) family. (prospecbio.com)
Eph receptor belongs to the largest family of RTK. (genominfo.org)

Mechanistically, Eph/ephrin signalling controls local cytoskeletal dynamics and thereby allows cellular shape changes that underlie repulsive or migratory responses. (silverchair.com)

The reliability of RNAi was enhanced by using unique regions of eph as dsRNA template and by carefully determining the level of Eph antigen in the visual systems of dsRNA-injected animals. (sdbonline.org)
adoptive transfer of genetically engineered t-cells to express antigen-specific t-cell receptor (tcr) is a feasible and effective therapeutic approach for numerous types of cancers, including epstein-barr virus (ebv)-associated malignancies. (liverpool.ac.uk)

Although a huge body of proof supports the idea that ligands are selective for his or her receptors, ligand Rabbit Polyclonal to MB specificity within some ligand/receptor family members is significantly less than total. (woofahs.com)

EPH receptor A2 has been shown to interact with: Ephrin_A1 ACP1 Grb2, PIK3R1, and SHC1. (wikipedia.org)
Ephrin A1 is a member of the ephrin (EPH) family. (bicellscientific.com)

It has been found that nearly all the receptors and ligands are expressed in developing and adult neural tissue (3). (rndsystems.com)
The rostral division of the neural tube into its 3 main sections falls under the control of homeobox (Hox) family of genes. (medscape.com)

In the majority of cases, Eph forward signalling causes cell repulsion away from the ephrin-expressing cell, although adhesive responses have been described. (silverchair.com)

Eph-ephrin signalling can be bi-directional and controls actin cytoskeleton dynamics, thereby leading to changes in cellular shape. (silverchair.com)
Using CHO-K1/A5 cells, a clonal cell line that robustly expresses adult muscle-type nicotinic acetylcholine receptor (nAChR), we explored whether insulin resistance in these mammalian cells affects cell-surface expression of the nAChR, its endocytic internalization, and actin cytoskeleton integrity. (bvsalud.org)

A family of structurally related cell-surface receptors that signal through an intrinsic PROTEIN-TYROSINE KINASE. (bvsalud.org)

By binding to monomeric PDGFR, VEGF-A thwarted PDGF-mediated dimerization and activation of the receptor, aswell as following signaling occasions and cellular replies. (woofahs.com)
Trans interactions of Eph receptors with ephrins at cell-cell interfaces promote a variety of cellular responses, including repulsion, attraction and migration. (silverchair.com)

Eph receptor signalling: from catalytic to non-catalytic functions. (edu.au)

Hence, Eph activation requires direct cell-cell contact. (silverchair.com)

methods: characteristics of clinical material, immunological data and gene mutation of two cases with xmen in the same family in china were retrospectively analyzed. (liverpool.ac.uk)

To better understand the molecular changes associated with AD, genome-wide association studies (GWAS) have identified hundreds of candidate genes linked to the disease, like the receptor tyrosine kinase EphA1. (sdbonline.org)
Utilising fly genetics, this study generated the first Drosophila model of human wild-type and P460L mutant EphA1 and tested the effects of Eph /ephrin signalling on AD-relevant behaviour and neurophysiology. (sdbonline.org)
EphA1 mis-expression did not cause neurodegeneration, shorten lifespan or affect memory but flies mis-expressing the wild-type or mutant receptor were hyper-aroused, had reduced sleep , a stronger circadian rhythm and increased clock neuron activity and excitability. (sdbonline.org)

Anatomy2

Chemicals and Drugs27

Phenomena and Processes3

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New ether-a-go-go K(+) channel family members localized in human telencephalon. (1/294)

Misexpression of the Emx-related homeobox genes cVax and mVax2 ventralizes the retina and perturbs the retinotectal map. (2/294)

The receptor tyrosine kinase EphB4 and ephrin-B ligands restrict angiogenic growth of embryonic veins in Xenopus laevis. (3/294)

Comparative analysis of embryonic gene expression defines potential interaction sites for Xenopus EphB4 receptors with ephrin-B ligands. (4/294)

Kinase independent function of EphB receptors in retinal axon pathfinding to the optic disc from dorsal but not ventral retina. (5/294)

Complementary expression of transmembrane ephrins and their receptors in the mouse spinal cord: a possible role in constraining the orientation of longitudinally projecting axons. (6/294)

Implications of EPHB6, EFNB2, and EFNB3 expressions in human neuroblastoma. (7/294)

Rit, a non-lipid-modified Ras-related protein, transforms NIH3T3 cells without activating the ERK, JNK, p38 MAPK or PI3K/Akt pathways. (8/294)

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New ether-a-go-go K(+) channel family members localized in human telencephalon. (1/294)

Misexpression of the Emx-related homeobox genes cVax and mVax2 ventralizes the retina and perturbs the retinotectal map. (2/294)

The receptor tyrosine kinase EphB4 and ephrin-B ligands restrict angiogenic growth of embryonic veins in Xenopus laevis. (3/294)

Comparative analysis of embryonic gene expression defines potential interaction sites for Xenopus EphB4 receptors with ephrin-B ligands. (4/294)

Kinase independent function of EphB receptors in retinal axon pathfinding to the optic disc from dorsal but not ventral retina. (5/294)

Complementary expression of transmembrane ephrins and their receptors in the mouse spinal cord: a possible role in constraining the orientation of longitudinally projecting axons. (6/294)

Implications of EPHB6, EFNB2, and EFNB3 expressions in human neuroblastoma. (7/294)

Rit, a non-lipid-modified Ras-related protein, transforms NIH3T3 cells without activating the ERK, JNK, p38 MAPK or PI3K/Akt pathways. (8/294)

EPH receptor A2 - Wikipedia

Prof Isabelle Lucet, Division Head | WEHI Researcher Profile

Mouse EphB2 Biotinylated Antibody BAF467: R&D Systems

Eph

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Recombinant Rat EphA5 Fc Chimera Protein, CF 541-A5-200: R&D Systems

Expressions of EphA2 and EphrinA-1 in early squamous cell cervical carcinomas and their relation to prognosis

Anti-Angiogenesis Therapy in Gynecologic Malignancies

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Facial Nerve Embryology: Overview, The Mature Facial Nerve, Overview of Hindbrain Development

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JCI - Notch alters VEGF responsiveness in human and murine endothelial cells by direct regulation of VEGFR-3 expression

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Iclusig (ponatinib) dosing, indications, interactions, adverse effects, and more

RCSB PDB - 2K9Y: EphA2 dimeric structure in the lipidic bicelle at pH 5.0

EFNA1 Protein Human Recombinant | TNFAIP4 Antigen | ProSpec

Calif. animal scientists attacked | The Scientist Magazine®

RALGDS | Cancer Genetics Web

SMART: PH domain annotation

SMART: Schnipsel domain PH

Recombinant Human EPHA2 Protein, MYC/DDK-tagged, C13 and N15-labeled EPHA2-321H - Creative BioMart

Molecular Vision: Loss of AND-34/BCAR3 expression in mice results in rupture of the adult lens

EphA2 Overexpression Causes Tumorigenesis of Mammary Epithelial Cells1 | Cancer Research | American Association for Cancer...

Search | Preprints.org

Mouse Ephrin Type-A Receptor 4 (EphA4) ELISA Kit - Innovative Research

The role of FGF and VEGF in angioblast induction and migration during vascular development<...

IJMS | Free Full-Text | Interactions between Guidance Cues and Neuronal Activity: Therapeutic Insights from Mouse Models

Ephrins and Eph receptors3

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