L-selectin (Lymphocyte cell adhesion molecule) (L-selectin (CD62L))

L-selectin is a calcium-dependent C-type lectin cell adhesion receptor of the selectin family, expressed on most leukocytes and the blastocyst, encoded by the SELL gene (CD62L). It contains an N-terminal C-type lectin domain that binds sialylated carbohydrates (notably sialyl Lewis X), an EGF-like domain, multiple short consensus repeat (SCR) domains, a single-pass transmembrane segment, and a cytoplasmic tail; its ectodomain can be cleaved by ADAM17. L-selectin mediates the initial capture and rolling of leukocytes on endothelial cells under shear flow, enabling lymphocyte homing through high endothelial venules and recruitment of neutrophils and monocytes to inflamed tissue; its binding exhibits catch–slip bond behavior dependent on Ca2+ and shear, with conformational transitions between bent and extended states influencing affinity. Beyond immunity, it contributes to blastocyst attachment during implantation and is an early marker on lymphoid-primed hematopoietic progenitors, suggesting roles in stem cell trafficking.

Other names

CD62LSELLLAM-1LECAM-1 (or LECCAM-1)Lymphocyte homing receptorLeukocyte adhesion molecule-1

Antagonist/blockade of L-selectin–ligand binding to inhibit leukocyte tethering/rolling on endothelium under shear (e.g., function-blocking antibodies). Allosteric modulation to stabilize extended/high-affinity conformation, altering rolling velocity and adhesion (e.g., DREG-55 heterotropic modulation). Inhibition of ectodomain interactions with sialyl Lewis X (sLeX)-bearing ligands and sulfated glycoproteins on HEV/endothelium, disrupting homing/recruitment