Selectins (L-, P-, E-) (CD62 family (CD62L, CD62P, CD62E))

Selectins are a family of calcium-dependent, type I transmembrane glycoproteins that mediate the initial "capture" and "rolling" of leukocytes on the vascular endothelium, an essential step in inflammation and immune surveillance[1][3][5][7][9]. L-selectin is constitutively expressed on most leukocytes, facilitating lymphocyte homing and migration into tissues[1][3]. P-selectin is stored in platelet and endothelial cell granules and rapidly translocated to the cell surface upon stimulation, playing a role in leukocyte–platelet and leukocyte–endothelial interactions[1][5]. E-selectin is induced on endothelial cells by inflammatory cytokines, regulating adhesion and recruitment of immune cells to sites of injury or infection[1][4][5]. All three selectins share homologous extracellular domains (a C-type lectin, an EGF-like domain, and complement-regulatory domains) but differ in expression, ligand specificity, and physiological roles[3][4][5][7]. Therapeutically, selectins are targeted to attenuate inflammation, metastatic spread of cancer cells, and vascular disease, but redundancy among selectins and their ligands complicates selective inhibition.[2][4][8]

Other names

LECAM-1LAM-1gp90PADGEMGMP-140ELAM-1CD62 family

Blockade of selectin-ligand interactions, inhibiting rolling/tethering of leukocytes; Inhibition of selectin-mediated cell adhesion, reducing tissue infiltration by immune cells; Antagonists (monoclonal antibodies, carbohydrate mimetics) compete with natural ligands and prevent downstream inflammatory signaling