Epithelial Cell Adhesion Molecule (EpCAM), also known as GA733-2 antigen, is a type â…transmembrane glycoprotein composed of an extracellular domain with two EGF-Like repeats and a cystenin-rich region, a transmembrane domain and a cytoplasmic domain. It modulates cell adhesion and proliferation. Its overexpression has been detected in many epithelial tumours and has been associated with high stage, high grade and a worse survival in some tumour types. EpCAM has been shown to function as a calcium-independent homophilic cell adhesion molecule that does not exhibit any obvious relationship to the four known cell adhesion molecule superfamilies. However, recent insights have revealed that EpCAM participates in not only cell adhesion, but also in proliferation, migration and differentiation of cells. In addition, recent study revealed that EpCAM is the Wnt-beta-catenin signaling target gene and may be used to facilitate prognosis. It has oncogenic potential and is activated by release of its intracellular domain, which can signal into the cell nucleus by engagement of elements of the wnt pathway.
Epithelial Cell Adhesion Molecule (EpCAM) , also known as GA733-2 antigen , is a type I transmembrane glycoprotein composed of an extracellular domain with two EGF-Like repeats and a cystenin-rich region , a transmembrane domain and a cytoplasmic domain. It modulates cell adhesion and proliferation. Its overexpression has been detected in many epithelial tumours and has been associated with high stage , high grade and a worse survival in some tumour types. EpCAM has been shown to function as a calcium-independent homophilic cell adhesion molecule that does not exhibit any obvious relationship to the four known cell adhesion molecule superfamilies. However , recent insights have revealed that EpCAM participates in not only cell adhesion , but also in proliferation , migration and differentiation of cells. In addition , recent study revealed that EpCAM is the Wnt-beta-catenin signaling target gene and may be used to facilitate prognosis. It has oncogenic potential and is activated by release of its intracellular domain , which can signal into the cell nucleus by engagement of elements of the wnt pathway.
Endothelial protein C receptor (EPCR); also known as activated protein C receptor (APC receptor) or PROCR; is a receptor for Protein C. Protein C plays an important role in many metabolism processes in humans and other animals after activated by binding to Endothelial protein C receptor (EPCR). Because of the EPCR is found primarily on endothelial cells (cells on the inside of blood vessels); activated protein C is found maily near endothelial cells. Protein C is pleiotropic; with two main functions: anticoagulation and cytoprotection. Which function will be performed depend on whether or not protein C remains bind to EPCR after activated. The anticoagulation occurs when it does not. In this case; protein C functions as an anticoagulant by irreversibly proteolytically inactivating Factor Va and Factor VIIIa; turning them into Factor Vi and Factor VIIIi respectively. When still bound to EPCR; activated protein C performs its cytoprotective effects; acting on the effector substrate PAR-1; protease-activated receptor-1. To a degree; APC's anticoagulant properties are independent of its cytoprotective ones; in that expression of one pathway is not affected by the existence of the other.
Endothelial Protein C Receptor (EPCR) is a Vitamin K-dependent Serine Protease that plays a major role in blood coagulation. Binding of Protein C to EPCR leads to the proteolytic activation of PAR1 (Protease-Activated Receptor 1) on endothelial cells and subsequent up-regulation of Protein C-induced genes. EPCR is a type I transmembrane glycoprotein in the CD1/MHC family. It is expressed most strongly in the endothelial cells of arteries and veins in heart and lung. Membrane bound EPCR is released by metalloproteolytic cleavage to generate the soluble receptor. The extracellular domain of human and mouse EPCR shares approximately 61% amino acid sequence homology. EPCR plays an important role in augmenting Protein C activation by the Thrombin-Thrombomodulin complex and in regulating blood coagulation and inflammation. EPCR is found primarily on endothelial cells. Deletion of EPCR function results in embryonic death; at least in part due to placental thrombosis.
EPDR1 is a member of the ependymin family. EPDR1 is a type II transmembrane protein that is similar to two families of cell adhesion molecules, the protocadherins and ependymins. It may play a role in calcium-dependent cell adhesion. EPDR1 is glycosylated, and the orthologous mouse protein is localized to the lysosome. Alternative splicing results in multiple transcript variants. A related pseudogene has been identified on chromosome 8.
EPHA1 or EPH receptor A1 belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. 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. An important role of Eph receptors and their ligands ephrins is to mediate cell-contact-dependent repulsion. Eph receptors and ephrins also act at boundaries to channel neuronal growth cones along specific pathways, restrict the migration of neural crest cells, and via bidirectional signaling prevent intermingling between hindbrain segments. Eph receptors and ephrins can also trigger an adhesive response of endothelial cells and are required for the remodeling of blood vessels. Eph receptors and ephrins have emerged as key regulators of the repulsion and adhesion of cells that underlie the establishment, maintainence, and remodeling of patterns of cellular organization. The ephrins and Eph receptors are implicated as positional labels that may guide the development of neural topographic maps.
Ephrin type-A receptor 1/EphA1 is a glycosylated member of the Eph family of transmembrane receptor tyrosine kinases. 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. The A and B classes of Eph proteins are distinguished by Ephrin ligand binding preference but have a common structural organization. Eph-Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression. EphA1 can form pH sensitive cishomodimers on the cell surface. Membrane-bound or clustered Ephrin ligands interact with EphA1 and activate its kinase domain which is capable of Ser, Thr, and Tyr phosphorylation. Reverse signaling is propagated through the Ephrin ligand. EphA1 is widely expressed in differentiated epithelial cells, particularly in bone marrow, spleen, thymus, and testes. EphA1 is upregulated or downregulated in a variety of human carcinomas and is implicated in tumor invasiveness.
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