Endothelial selectins (Selectin E and Selectin P) (E-selectin and P-selectin)

Endothelial selectins, specifically E-selectin (CD62E) and P-selectin (CD62P), are cell surface glycoproteins that play a critical role in the initial steps of the inflammatory cascade (UniProt P16581, P16109). E-selectin is synthesized and expressed on endothelial cells following stimulation by inflammatory cytokines like TNF-alpha, while P-selectin is rapidly translocated from intracellular Weibel-Palade bodies to the cell surface upon activation by stimuli such as thrombin (StatPearls, 'Selectins'). Their primary biological function is to mediate the rolling of leukocytes along the vascular wall by binding to carbohydrate ligands, such as P-selectin glycoprotein ligand-1 (PSGL-1), on the surface of white blood cells (PubMed: 29371399). This interaction is essential for the recruitment of immune cells to sites of injury or infection. In pathological states, over-expression of endothelial selectins contributes to diseases including sickle cell disease, where they facilitate vaso-occlusive crises, and cancer metastasis, where they assist tumor cell adhesion to the endothelium (NIH, 'Crizanlizumab'). Therapeutic targeting of these selectins, such as with the monoclonal antibody crizanlizumab or the E-selectin antagonist uproleselan, aims to disrupt these adhesive interactions to treat sickle cell disease or enhance chemotherapy sensitivity in leukemia (ClinicalTrials.gov: NCT03616470).

Other names

CD62ECD62PELAM-1GMP-140LECAM-2PADGEMSELESELPSelectin ESelectin P

Selectin antagonists/inhibitors block the interaction between endothelial selectins and their carbohydrate ligands (such as Sialyl Lewis X or PSGL-1) on the surface of leukocytes, platelets, or circulating tumor cells, thereby inhibiting cell-to-cell adhesion and rolling on the vascular endothelium.