E-Selectin (Endothelial Leukocyte Adhesion Molecule-1, ELAM-1, CD62E), a member of the Selectin family, is a 107‑115 kDa cell surface glycoprotein. It is transiently expressed on vascular endothelial cells in response to IL-1 beta and TNF-alpha, and demonstrates peak expression at 4 hours, and decay at 24 hours, in response to activation. E-Selectin ligands, expressed on neutrophils, monocytes, and a subset of memory T cells, are sialylated, fucosylated molecules which bind to the lectin domain of E-Selectin. Immunocytochemical techniques have demonstrated the expression of E-Selectin on healthy and diseased tissue. The human and rat proteins share approximately 67% amino acid identity. The mouse and rat proteins share approximately 78% amino acid identity.
E-Selectin mediates the attachment of flowing leukocytes to the blood vessel wall during inflammation by binding to E-Selectin ligands on leukocytes. These interactions are labile and permit leukocytes to roll along the vascular endothelium in the direction of blood flow. This initial interaction is followed by a stronger interaction involving ICAM-1 and VCAM-1 that leads eventually to extravasation of the white blood cell through the blood vessel wall into the extracellular matrix tissue.
ELISA techniques have shown that detectable levels of soluble E-Selectin are present in the biological fluids of apparently normal individuals. Furthermore, a number of studies have reported that levels of E-Selectin may be elevated in subjects with a variety of pathological conditions.
