P-selectin glycoprotein ligand-1

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SELPLG
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases SELPLG, CD162, CLA, PSGL-1, PSGL1, selectin P ligand
External IDs MGI: 106689 HomoloGene: 2261 GeneCards: 6404
Genetically Related Diseases
Disease Name References
Conduct disorder
RNA expression pattern
PBB GE SELPLG 209879 at tn.png

PBB GE SELPLG 209880 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001206609
NM_003006

NM_009151

RefSeq (protein)

NP_001193538.1
NP_002997.2

n/a

Location (UCSC) Chr 12: 108.62 – 108.63 Mb Chr 5: 113.82 – 113.83 Mb
PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

Selectin P ligand, also known as SELPLG or CD162 (cluster of differentiation 162), is a human gene.


SELPLG codes for PSGL-1, 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 SELPLG 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.[1]


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

Posttranslational modification[edit]

PSGL-1 protein requires two distinct posttranslational modifications to gain its selectin binding activity:[2][3][4][5]

Function[edit]

PSGL-1 is expressed on all white blood cells and plays an important role in the recruitment of white blood cells into inflamed tissue: White blood cells normally do not interact with the endothelium of blood vessels. However, inflammation causes the expression of cell adhesion molecules (CAM) such as P-selectin on the surface of the blood vessel wall. White blood cells present in flowing blood can interact with CAM. The first step in this interaction process is carried out by PSGL-1 interacting with P-selectin and/or E-selectin on endothelial cells and adherent platelets. This interaction results in "rolling" of the white blood cell on the endothelial cell surface followed by stable adhesion and transmigration of the white blood cell into the inflamed tissue.[citation needed]

In mice it seems to be an immune factor regulating T-cell checkpoints, and it could be a target for future checkpoint inhibitor anti-cancer drugs.[6]

References[edit]

  1. ^ "Entrez Gene: SELPLG selectin P ligand". 
  2. ^ Li F, Wilkins PP, Crawley S, et al. (1996). "Post-translational modifications of recombinant P-selectin glycoprotein ligand-1 required for binding to P- and E-selectin.". J. Biol. Chem. 271 (6): 3255–64. doi:10.1074/jbc.271.6.3255. PMID 8621728. 
  3. ^ Wilkins PP, Moore KL, McEver RP, Cummings RD (1995). "Tyrosine sulfation of P-selectin glycoprotein ligand-1 is required for high affinity binding to P-selectin.". J. Biol. Chem. 270 (39): 22677–80. doi:10.1074/jbc.270.39.22677. PMID 7559387. 
  4. ^ Sako D, Comess KM, Barone KM, et al. (1995). "A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding.". Cell 83 (2): 323–31. doi:10.1016/0092-8674(95)90173-6. PMID 7585949. 
  5. ^ Pouyani T, Seed B (1995). "PSGL-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus.". Cell 83 (2): 333–43. doi:10.1016/0092-8674(95)90174-4. PMID 7585950. 
  6. ^ Immune Factor Seen to Control T-Cell Checkpoints Involved in Spread of Cancers and Infections. June 2016

Further reading[edit]

External links[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.