Human P-Selectin Glycoprotein Ligand 1 (SELPLG) Protein

Background

Selectin P ligand (SELPLG), also known as CD162 or P-selectin glycoprotein ligand-1 (PSGL-1), is a critical adhesion molecule that mediates interactions between leukocytes and endothelial cells. Encoded by the SELPLG gene on chromosome 12 in humans, SELPLG plays an essential role in the immune response by facilitating leukocyte tethering and rolling on the endothelium during inflammation and immune surveillance. This glycoprotein ligand interacts with selectins, specifically P-, E-, and L-selectins, which are expressed on activated endothelial cells and platelets, to initiate leukocyte adhesion at inflammation sites. SELPLG's ability to engage in interactions with multiple selectins allows it to participate in a variety of immune functions, from neutrophil recruitment to lymphocyte homing and trafficking. This glycoprotein ligand is particularly important in pathological conditions where leukocyte migration into tissues is crucial, such as infection, inflammation, and tissue injury.