E-Selectin (Endothelial Leukocyte Adhesion Molecule-1, ELAM-1, or 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 mouse E‑Selectin proteins share 81% amino acid similarity.
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.
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