E-Selectin
(Endothelial Leukocyte Adhesion Molecule-1, ELAM-1, CD62E), a member of the
Selectin family, is a 107 - 115 kDa cell surface glycoprotein. E-selectin is a cell
adhesion molecule that is critical for inflammation and neovascularization in
areas of wound healing and ischemia. In response to tissue injury, release of
cytokines/chemokines, including stromal cell-derived factor 1α (SDF-1α),
induces local endothelial expression of membrane-bound E-selectin and systemic
reciprocal E-selectin ligand expression on endothelial progenitor cells (EPCs)
in the bone marrow via C-X-C motif chemokine receptor 4 (CXCR4). 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. It is a cell surface glycoprotein that plays a role in immune
adhesion. By interacting with SELPLG/PSGL1, it mediates the adhesion of blood
neutrophils in the endothelium activated by cytokines. May play a role in
capillary morphogenesis. 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.
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