Transports L-glutamate and also L-and D-aspartate. Essential for terminating the postsynaptic action of glutamate by rapidly removing released glutamate from the synaptic cleft. Acts as a symport by cotransporting sodium.
Endothelial cell-selective adhesion molecule (ESAM) is a member of JAM family of immunoglobulin superfamily and consists of one V-type and one C2-type immunoglobulin domain; as well as a hydrophobic signal sequence; a single transmembrane region; and a cytoplasmic domain. It is specifically expressed at endothelial tight junctions and on activated platelets. ESAM at endothelial tight junctions participates in the migration of neutrophils through the vessel wall; possibly by influencing endothelial cell contacts. The adaptor protein membrane-associated guanylate kinase MAGI-1 has been identified as an intracellular binding partner of ESAM. Previous studies have indicated that ESAM regulates angiogenesis in the primary tumor growth and endothelial permeability. It suggest that ESAM has a redundant functional role in physiological angiogenesis but serves a unique and essential role in pathological angiogenic processes such as tumor growth.
Endothelial Cell Adhesion Molecule (ESAM) is a 55 kDa type I transmembrane glycoprotein member of the JAM family of immunoglobulin superfamily molecules. The 390 amino acid Human ESAM contains a 216 amino acid extracellular domain (ECD) with a V-type and a C2-type immunoglobulin (Ig) domain. The ECD of human and mouse ESAM share 69% amino acid identity. ESAM is specifically expressed at endothelial tight junctions and on activated platelets and performs homophilic adhesion activity. The adaptor protein membrane-associated guanylate kinase MAGI-1 has been identified as an intracellular binding partner of ESAM. In addition; ESAM at endothelial tight junctions participates in the migration of neutrophils through the vessel wall; possibly by influencing endothelial cell contacts. ESAM-deficient mice were described with lowered angiogenic potential; and accordingly; overexpression of ESAM is closely associated with certain tumor growth and metastasis.
Endothelial Cell Adhesion Molecule (ESAM) is a 55 kDa type I transmembrane glycoprotein member of the JAM family of immunoglobulin superfamily molecules. The 390 amino acid Human ESAM contains a 216 amino acid extracellular domain (ECD) with a V-type and a C2-type immunoglobulin (Ig) domain. ESAM is specifically expressed at endothelial tight junctions and on activated platelets and performs homophilic adhesion activity. The adaptor protein membrane-associated guanylate kinase MAGI-1 has been identified as an intracellular binding partner of ESAM. In addition; ESAM at endothelial tight junctions participates in the migration of neutrophils through the vessel wall; possibly by influencing endothelial cell contacts. ESAM-deficient mice were described with lowered angiogenic potential; and accordingly; overexpression of ESAM is closely associated with certain tumor growth and metastasis. ESAM is expressed on endothelial cells; activated platelets and megakaryocytes. The ECD of human and mouse ESAM share 69% amino acid identity.
E-selectin, also known as endothelial leukocyte adhesion molecule-1 (ELAM-1) and CD62E, is an inducible adhesion molecule that is expressed on the surfaces of stimulated vascular endothelial cells and is sometimes involved in cancer cell metastasis. E-selectin exhibits a complex mosaic structure consisting of a large extracellular region comprised of a lectin domain, an EGF-like domain, and a short consensus repeat (SCR) domain, followed by a transmembrane region and a relatively short (32 aa) cytoplasmic tail. As a member of the LEC-CAM or selectin family, E-selectin recognises and binds to sialylated carbohydrates including members of the Lewis X and Lewis A families found on monocytes, granulocytes, and T-lymphocytes. E-selectin supports rolling and stable arrest of leukocytes on activated vascular endothelium, and furthermore, it was indicated that it can also transduce an activating stimulus via the MAPK cascade into the endothelial cell during leukocyte adhesion. E-selectin regulates adhesive interactions between certain blood cells and endothelium. The soluble form of E selectin (sE-selectin) is a marker of endothelial activation, and has a potential role in the pathogenesis of cardiovascular disease as raised levels have been found in hypertension, diabetes and hyperlipidemia, although its association in established atherosclerosis disease and its value as a prognostic factor is more controversial. soluble E-selectin is inversely associated with the muscular component of the left ventricle, thereby suggesting that the lack of such a reparative factor may be associated with cardiac remodeling in end-stage renal disease (ESRD) patients. Besides, this adhesion molecule appears to be involved in the pathogenesis of atherosclerosis.
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