SELPLG
SELPLG encodes P-selectin glycoprotein ligand 1, also known as PSGL-1 or CD162, a membrane glycoprotein that acts as a high-affinity counter-receptor for P-, E- and L-selectin on myeloid cells and stimulated T lymphocytes. Browse Assay Genie's current range of SELPLG research reagents below, or read on for the biology behind the target.
SELPLG (selectin P ligand) encodes a glycoprotein that serves as a high-affinity counter-receptor for the cell adhesion molecules P-, E- and L-selectin. It is expressed on myeloid cells and stimulated T lymphocytes. By binding selectins presented on activated platelets or on endothelia, it tethers leukocytes to these surfaces, and in this way it plays a critical role in leukocyte trafficking during inflammation.
High-affinity binding depends on two post-translational modifications of the protein: tyrosine sulfation and the addition of the sialyl Lewis x tetrasaccharide (sLex) to its O-linked glycans. This means that the functional activity of PSGL-1 reflects glycosylation and sulfation status as well as expression of the polypeptide itself. UniProt also records that the protein acts as a receptor for enterovirus 71 in the context of microbial infection.
The protein is a membrane protein and is classed by HGNC among the CD molecules and receptor ligands, hence the alias CD162. Aberrant expression of the SELPLG gene, and polymorphisms in it, are associated with defects in the innate and adaptive immune response. Alternate splicing results in multiple transcript variants. The mouse ortholog is Selplg, which is commonly used in in vivo studies of leukocyte adhesion.
SELPLG tethers leukocytes to activated platelets or selectin-expressing endothelia, making it central to studies of leukocyte recruitment.
As a counter-receptor for P-, E- and L-selectin, PSGL-1 is a focus for work on how inflammatory responses are initiated.
Aberrant expression and polymorphisms in SELPLG are linked to defects in innate and adaptive immunity.
Tyrosine sulfation and sLex modification govern binding, and PSGL-1 also acts as a receptor for enterovirus 71.
SELPLG encodes PSGL-1, a high-affinity counter-receptor for P-, E- and L-selectin on myeloid cells and stimulated T lymphocytes. By tethering leukocytes to activated platelets or selectin-expressing endothelia, it contributes to leukocyte trafficking during inflammation. It also acts as a receptor for enterovirus 71.
SELPLG stands for selectin P ligand, and the protein is called P-selectin glycoprotein ligand 1. Common aliases are PSGL-1 and CD162. The gene produces multiple transcript variants through alternate splicing, so literature may refer to several forms.
High-affinity selectin binding requires tyrosine sulfation and the addition of the sialyl Lewis x tetrasaccharide to the O-linked glycans of the protein. Aberrant expression and polymorphisms in SELPLG are associated with defects in innate and adaptive immune responses. The mouse ortholog is Selplg.
Selectins, adhesion molecules and other leukocyte trafficking targets relevant to SELPLG biology.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q14242; product specifications from Assay Genie datasheets.