SELPLG
Description
The SELPLG (selectin P ligand) is a protein-coding gene located on chromosome 12.
SELPLG, also known as CD162, is a human gene that encodes PSGL-1, the high affinity counter-receptor for P-selectin on myeloid cells and stimulated T lymphocytes. It plays a crucial role in tethering these cells to activated platelets or endothelia expressing P-selectin. The gene structure of SELPLG resembles CD43 and GpIb-alpha, with an intron in the 5'-noncoding region, a long second exon containing the coding region, and TATA-less promoters. PSGL-1 is a glycoprotein expressed on white blood cells and endothelial cells that binds to all three members of the selectin family (P-, E-, and L-selectins), with the highest affinity for P-selectin. PSGL-1 requires two posttranslational modifications for selectin binding activity: sulfation of tyrosines and the addition of the sialyl Lewis x tetrasaccharide (sLex) to its O-linked glycans. PSGL-1 is essential for recruiting white blood cells to inflamed tissue by interacting with P-selectin and/or E-selectin on endothelial cells and adherent platelets.
PSGL-1 is a key player in the early stages of inflammation, enabling leukocytes to roll rapidly along the vascular surfaces. It achieves this by forming high-affinity, calcium-dependent bonds with E-, P-, and L-selectins. This rolling movement is crucial for the initial capture of leukocytes, setting the stage for their recruitment to inflamed tissues.
SELPLG is also known as CD162, CLA, PSGL-1, PSGL1.
