P-selectin and E-selectin (SELP/SELE)

P-selectin (CD62P) and E-selectin (CD62E) are members of the selectin family of cell adhesion molecules that play critical roles in the initial stages of the inflammatory response [1, 3]. P-selectin is rapidly translocated to the surface of activated platelets and endothelial cells from intracellular stores (Weibel-Palade bodies and alpha-granules), while E-selectin is synthesized and expressed on endothelial cells following cytokine stimulation (e.g., TNF-alpha, IL-1beta) [1, 4, 13]. Together, they mediate the "tethering" and "rolling" of leukocytes along the vascular wall by binding to carbohydrate ligands such as P-selectin glycoprotein ligand-1 (PSGL-1) [3, 8]. This process is essential for leukocyte recruitment to sites of injury or infection but also contributes to the pathology of various diseases, including sickle cell disease (SCD), where it leads to vaso-occlusive crises, and cancer, where it facilitates metastasis [2, 5, 15]. Therapeutic strategies targeting these selectins include monoclonal antibodies like crizanlizumab (targeting P-selectin) and glycomimetic inhibitors like uproleselan (targeting E-selectin) or rivipansel (a pan-selectin inhibitor), which aim to disrupt leukocyte-endothelial interactions to reduce inflammation and vascular complications [4, 8, 12].

Other names

CD62PCD62ESELPSELEGMP-140PADGEMLECAM-3ELAM-1LECAM-2Granule membrane protein 140Platelet activation dependent granule-external membrane proteinEndothelial-leukocyte adhesion molecule 1

Inhibition of selectin-ligand (e.g., PSGL-1) interaction to prevent leukocyte adhesion and rolling