Selectin

The selectin family comprises a group of structurally related, calcium-dependent, type I transmembrane glycoproteins known as cell adhesion molecules. The three known members—L-selectin (CD62L), E-selectin (CD62E), and P-selectin (CD62P)—function as carbohydrate-binding receptors (C-type lectins) and are critical for mediating the initial steps of leukocyte tethering and rolling on vascular endothelium during inflammation, immune surveillance, and lymphocyte homing. They recognize specific glycan motifs, such as sialyl Lewis^x, on target cells, allowing regulated cell–cell interactions during physiological and pathological processes including inflammation, thrombosis, and cancer metastasis. Each selectin exhibits distinct cellular expression: L-selectin on leukocytes, E-selectin on activated endothelial cells, and P-selectin on platelets and activated endothelium. The selectin family, as a group, is considered a therapeutic target in diseases characterized by aberrant leukocyte adhesion and trafficking, though treatment strategies typically require targeting the individual family members[2][3][4][5][6].

Other names

SelectinsCD62 (as a cluster designation for the group)C-type lectins (specifically this subfamily)Cell adhesion molecule (CAM)

Inhibition of selectin–ligand interactions to reduce leukocyte adhesion and rolling Blockade of selectin-mediated cell trafficking to reduce inflammation or vascular occlusion