Endothelial selectin and Platelet selectin (E-selectin and P-selectin) (E-selectin and P-selectin)

E-selectin (CD62E) and P-selectin (CD62P) are type I transmembrane glycoproteins belonging to the C-type lectin family of cell adhesion molecules [1, 3, 5]. They play a fundamental role in the immune system by initiating the leukocyte adhesion cascade, specifically mediating the initial tethering and rolling of leukocytes on the vascular endothelium at sites of inflammation [1, 2, 7]. P-selectin is rapidly translocated to the cell surface from storage granules in platelets and endothelial cells upon stimulation, while E-selectin is expressed on endothelial cells after several hours of cytokine induction [2, 12, 16]. Beyond normal immune surveillance, these receptors are significantly involved in the pathogenesis of various conditions, including chronic inflammation, cardiovascular diseases, and cancer metastasis, where they facilitate the docking of tumor cells to the endothelium [3, 4, 11]. In sickle cell disease, E- and P-selectin-mediated interactions among sickled red blood cells, leukocytes, and platelets are primary drivers of painful vaso-occlusive crises [5, 8, 20]. Consequently, they have become high-value therapeutic targets; drugs such as crizanlizumab (a P-selectin inhibitor) and uproleselan (an E-selectin antagonist) are designed to disrupt these adhesive interactions to treat hematologic disorders and reduce the spread of malignancies [19, 20, 22].

Other names

CD62ECD62PSELESELPEndothelial-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 (LECAM-2)

Competitive inhibition of the interaction between selectins and their carbohydrate ligands (e.g., Sialyl Lewis X on PSGL-1), preventing leukocyte tethering and rolling on the endothelium.