Selectin E and Selectin P (SELE and SELP)

Selectin E (E-selectin) and Selectin P (P-selectin) are vital cell adhesion molecules expressed on the surface of activated vascular endothelial cells. They belong to the C-type lectin family and are primary mediators of the initial rolling phase of leukocyte recruitment to sites of inflammation and injury (UniProt P16581, P16109). P-selectin is rapidly mobilized from intracellular stores known as Weibel-Palade bodies upon stimulation, whereas E-selectin expression is induced over several hours by pro-inflammatory cytokines like TNF-alpha (StatPearls, Selectins). These proteins bind to carbohydrate ligands, such as Sialyl Lewis X on P-selectin glycoprotein ligand-1 (PSGL-1), facilitating the tethering of neutrophils and monocytes to the vessel wall. Dysregulation of this process is central to the pathogenesis of various conditions, including sickle cell disease vaso-occlusive crises and chronic inflammatory disorders (PubMed: 31722151). Additionally, selectins are exploited by certain cancer cells to facilitate metastasis through the bloodstream. Pharmacological inhibition of these targets, such as with the monoclonal antibody crizanlizumab, aims to disrupt these adhesive interactions to prevent vascular occlusion and reduce tissue damage (FDA, Adakveo).

Other names

E-selectinP-selectinCD62ECD62PEndothelial-leukocyte adhesion molecule 1 (ELAM-1)Granule membrane protein 140 (GMP-140)Platelet activation dependent granule-external membrane protein (PADGEM)Leukocyte-endothelial cell adhesion molecule 2 (LECAM2)

Selectin antagonism; inhibition of leukocyte-endothelial adhesion; blockade of the N-terminal lectin domain to prevent binding with sialylated carbohydrate ligands such as Sialyl Lewis X and PSGL-1.