P-Selectin Glycoprotein Ligand 1 (PSGL1)

SELPLG is the high affinity counter-receptor for P-selectin on myeloid cells and stimulated T lymphocytes. As such, it plays a critical role in the tethering of these cells to activated platelets or endothelia expressing P-selectin. The organization of the SELPG gene closely resembles that of CD43 and the human platelet glycoprotein GpIb-alpha both of which have an intron in the 5-prime-noncoding region, a long second exon containing the complete coding region, and TATA-less promoters.

P-selectin glycoprotein ligand-1 is a glycoprotein found on white blood cells and endothelial cells that binds to P-selectin (P stands for platelet). It is one of a family of selectins that includes E-selectin (endothelial) and L-selectin (leukocyte). PSGL-1 can bind to all three members of the family but binds best (with the highest affinity) to P-selectin.