The (ephrin receptor type 1) is a protein encoded by a gene in human EPHA1 EPH receptor A1. This gene belongs to the ephrin receptor subfamily of protein tyrosine kinase. In the central nervous system, EPH-related receptors EPH is involved in mediating a particular developmental event. Usually, EPH subfamily receptors, have an extracellular region containing two fibronectin type III repeats and cysteine-rich domain and kinase domain of the single. Are divided into two groups based on the similarity of their affinity for the ligand ephrin binding and ephrin-AB extracellular domain sequence of the ephrin receptor. Expressed in human cancer cell lines of some, this gene is related to carcinogenesis.

This gene belongs to the ephrin receptor subfamily of protein tyrosine kinase. In the central nervous system, EPH-related receptors EPH is involved in mediating a particular developmental event. Usually, EPH subfamily receptors, have an extracellular region containing two fibronectin type III repeats and cysteine-rich domain and kinase domain of the single. Are divided into two groups based on the similarity of their affinity for the ligand ephrin binding and ephrin-AB extracellular domain sequence of the ephrin receptor. Expressed in human cancer cell lines of some, this gene is related to carcinogenesis.

This gene belongs to the ephrin receptor subfamily of protein tyrosine kinase. In the central nervous system, EPH-related receptors EPH1 is involved in mediating a particular developmental event. Usually, EPH subfamily receptors, have an extracellular region containing two fibronectin type III repeats and cysteine-rich domain and kinase domain of the single. Are divided into two groups based on the similarity of their affinity for the ligand ephrin binding and ephrin-AB extracellular domain sequence of the ephrin receptor. Expressed in human cancer cell lines of some, this gene is related to carcinogenesis.

Receptor tyrosine kinase that binds the ligand family – membrane-bound ephrin present in the cell adjacent to the lead contact-dependent bidirectional signaling device in a cell adjacent to the random. The signaling path of the receptor in the downstream signaling of the first downstream, to the ephrin signaling pathway of Ligands are known as reverse signaling. To binds with high affinity and a EFNA3 EFNA4 and low affinity to EFNA1 most likely to represent the function of its cognate ligand. To induce cell adhesion to RAC RhoA and the downstream side suppression of cell proliferation and motility by regulating the extracellular matrix, an ILK EFNA1 is activated. Plays a role in angiogenesis, to regulate cell proliferation. I may play a role in apoptosis

I have been involved in the form and behavior of cells in the ligand system – Eph – ephrin receptor. EphA1 is a founding member of the Eph receptor, but little, very little is known about its function. Here, EphA1 shows the activation of the kinase to inhibit the migration and cell proliferation-dependent manner-ROCK of RhoA. In addition, our results referring to the interaction with the actin cytoskeleton integrin-linked kinase new interaction and EphA1 (ILK), and integrin-mediated. Ankyrin and regions (SAM) domain EphA1 need C-terminal α sterilization motif of ILK enough to EphA1 ILK interaction. Interaction is independent of the EphA1 kinase activity, but is dependent on the stimulation of ligand EphA1 ephrin-A1. Activation of EphA1 kinase, leads to a reduction in ILK activity. Finally, we show that the expression of kinase active form of ILK (S343D) to save EphA1 mediated growth of defects, reducing the activation of RhoA. These results, I show that EphA1 regulates motility and morphology of the cells in-ROCK ILK-RhoA by the route. EPHA1 gene encodes a protein of 976 amino acids with an isoelectric point of 6.6254 and the calculated molecular weight of 108,126.89. Amino acids 1-25 represent the signal peptide.

EphA1 is a founding member of what is recognized as a sub-family of the maximum of the receptor tyrosine kinase. This protein is a member of the group of ancient fungi exist, worms, fruit flies in evolutionarily. , That contribute to the complexity of the bilateral body plan to increase the number of genes encoding receptors of the Eph and the gene encoding the ligand (Eph receptor interaction protein) ephrin is proposed are. Eph receptors are 14, have been identified in vertebrates. To subclass the structure of the ligand binding is different mainly (or is EphA1, EphA2, of EphA3, EphA4, EphA5 is, of EphA6, EphA7, EphA8, EphA10) of (EphB1, EPHB2, EphB3, EphB4, EPHA EPHB or EphB6 they Domains) split.

EPHB receptor, shows the binding affinity GPI-linked ephrin ligand receptor EPHA also large while bound to the transmembrane ephrin-B ligand. It is a chaotic interaction is small, Eph receptor between each cross-linking several classes going on exhibit different affinities for ephrin ligands different. EPH-ephrin binding, with a cell-to-cell contact. Dimer to Epesoefurin time and binding, protein, pass the cluster and higher in each cell. This leads to repulsion signaling and adhesion of subsequent cells that interact ephrin-bearing cells (return signal) and F-two. In this way, cells – Effects and cell contact – ephrin signaling Eph – may be terminated either by enzymatic cleavage of the extracellular domain of endocytosis or Eph ephrin ligand receptor or ephrin complex. High affinity ligand is ephrin-A3 and EphA1 ephrin-A1. You are not bound to the activating ligand at all fibronectin also EphA1.

Embryos differentiated (including epiblast, primitive streak, near mesoderm, tail bud mesoderm, the bud limb distal), human lung, from the intestine dynamic expressions of local cells, in mouse embryonic development at the time of in vitro of ES embryoid body or (ES) cells, kidney, bladder, thymus, skin, colon stem. (I include the collection system skin, vagina endometrial and skin, kidney) adult mouse epithelial tissue. Liver of a normal rat, kidney, lung. Cell line of epithelial origin and human tumors.

It has not been established yet completely. Usually repulsive interaction with ephrin-A3 and high affinity ligand ephrin-A1. (., Unpublished and Duffy) transgene expression in blastula EphA1 preimplantation mouse, is fatal. In EphA1 homozygous deficient mice, I show vagina (18% for women) fall tail bent (80%). In vertebrate reptiles (zebrafish, medaka, fugu), amphibians and (Xenopus laevis) EphA1 fish, lack of apparent and poultry (anole lizard) and (chicken) its appearance, and transition of life from water to land environment I suggest an association. The presence of nonionic Glu547 residue incorporated transmembrane domain of membrane receptors Ephesians unique also EphA1. The structural mechanical properties of the transmembrane domain, be dependent on the state of ionization of this portion is shown, that it is, for example pH, receptor activation EphA1 flexibility and conformation, these indicates that it can be adjusted by the local sources and the outside of the membrane that may be particularly important for EphA1 kidney function or skin with the detection of the lipid composition and discovery.