https://www.wikidoc.org/index.php?title=P-selectin_glycoprotein_ligand-1&feed=atom&action=historyP-selectin glycoprotein ligand-1 - Revision history2024-03-29T15:36:38ZRevision history for this page on the wikiMediaWiki 1.40.0https://www.wikidoc.org/index.php?title=P-selectin_glycoprotein_ligand-1&diff=1415588&oldid=preven>JCW-CleanerBot: task, replaced: Trends in molecular medicine → Trends in Molecular Medicine using AWB2017-11-01T19:46:00Z<p><a href="/index.php?title=User:JCW-CleanerBot&action=edit&redlink=1" class="new" title="User:JCW-CleanerBot (page does not exist)">task</a>, replaced: Trends in molecular medicine → Trends in Molecular Medicine using <a href="/index.php?title=wikidoc:AWB&action=edit&redlink=1" class="new" title="wikidoc:AWB (page does not exist)">AWB</a></p>
<p><b>New page</b></p><div>{{Infobox_gene}}<br />
'''Selectin P ligand''', also known as '''SELPLG''' or '''CD162''' ([[cluster of differentiation]] 162), is a human [[gene]].<br />
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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.<br />
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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.<ref>{{cite web | title = Entrez Gene: SELPLG selectin P ligand| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6404| accessdate = }}</ref><br />
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'''P-selectin glycoprotein ligand-1''' ('''PSGL-1''') is a [[glycoprotein]] found on [[white blood cells]] and [[endothelium|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 molecule]]s. PSGL-1 can bind to all three members of the family but binds best (with the highest affinity) to P-selectin.<br />
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==Posttranslational modification==<br />
PSGL-1 protein requires two distinct [[posttranslational modification]]s to gain its selectin binding activity:<ref name=Li1996>{{cite journal |vauthors=Li F, Wilkins PP, Crawley S, etal |title=Post-translational modifications of recombinant P-selectin glycoprotein ligand-1 required for binding to P- and E-selectin. |journal=J. Biol. Chem. |volume=271 |issue= 6 |pages= 3255–64 |year= 1996 |pmid= 8621728 |doi=10.1074/jbc.271.6.3255 }}</ref><ref>{{cite journal | vauthors=Wilkins PP, Moore KL, McEver RP, Cummings RD |title=Tyrosine sulfation of P-selectin glycoprotein ligand-1 is required for high affinity binding to P-selectin. |journal=J. Biol. Chem. |volume=270 |issue= 39 |pages= 22677–80 |year= 1995 |pmid= 7559387 |doi=10.1074/jbc.270.39.22677 }}<br />
</ref><ref>{{cite journal |vauthors=Sako D, Comess KM, Barone KM, etal |title=A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding. |journal=Cell |volume=83 |issue= 2 |pages= 323–31 |year= 1995 |pmid= 7585949 |doi=10.1016/0092-8674(95)90173-6 }}<br />
</ref><ref>{{cite journal | vauthors=Pouyani T, Seed B |title=PSGL-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus. |journal=Cell |volume=83 |issue= 2 |pages= 333–43 |year= 1995 |pmid= 7585950 |doi=10.1016/0092-8674(95)90174-4 }}</ref> <br />
* [[sulfation]] of [[tyrosine]]s <br />
* the addition of the [[sialyl Lewis x]] tetrasaccharide (sLex) to its O-linked [[glycan]]s<br />
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==Function==<br />
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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|date=June 2016}}<br />
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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.<ref>[http://immuno-oncologynews.com/2016/06/01/discovery-of-immune-factor-controlling-t-cell-checkpoints-explored-by-clinical-developers/ Immune Factor Seen to Control T-Cell Checkpoints Involved in Spread of Cancers and Infections. June 2016 ]</ref><br />
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==References==<br />
{{reflist}}<br />
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==Further reading==<br />
{{refbegin | 2}}<br />
{{PBB_Further_reading <br />
| citations = <br />
*{{cite journal | vauthors=Furie B, Furie BC |title=Role of platelet P-selectin and microparticle PSGL-1 in thrombus formation. |journal=Trends in Molecular Medicine |volume=10 |issue= 4 |pages= 171–8 |year= 2004 |pmid= 15059608 |doi= 10.1016/j.molmed.2004.02.008 }}<br />
*{{cite journal |vauthors=Sako D, Chang XJ, Barone KM, etal |title=Expression cloning of a functional glycoprotein ligand for P-selectin. |journal=Cell |volume=75 |issue= 6 |pages= 1179–86 |year= 1993 |pmid= 7505206 |doi=10.1016/0092-8674(93)90327-M }}<br />
*{{cite journal |vauthors=Moore KL, Eaton SF, Lyons DE, etal |title=The P-selectin glycoprotein ligand from human neutrophils displays sialylated, fucosylated, O-linked poly-N-acetyllactosamine. |journal=J. Biol. Chem. |volume=269 |issue= 37 |pages= 23318–27 |year= 1994 |pmid= 7521878 |doi= }}<br />
*{{cite journal |vauthors=Veldman GM, Bean KM, Cumming DA, etal |title=Genomic organization and chromosomal localization of the gene encoding human P-selectin glycoprotein ligand. |journal=J. Biol. Chem. |volume=270 |issue= 27 |pages= 16470–5 |year= 1995 |pmid= 7541799 |doi=10.1074/jbc.270.27.16470 }}<br />
*{{cite journal | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}<br />
*{{cite journal |vauthors=Guyer DA, Moore KL, Lynam EB, etal |title=P-selectin glycoprotein ligand-1 (PSGL-1) is a ligand for L-selectin in neutrophil aggregation. |journal=Blood |volume=88 |issue= 7 |pages= 2415–21 |year= 1996 |pmid= 8839831 |doi= }}<br />
*{{cite journal |vauthors=Goetz DJ, Greif DM, Ding H, etal |title=Isolated P-selectin glycoprotein ligand-1 dynamic adhesion to P- and E-selectin. |journal=J. Cell Biol. |volume=137 |issue= 2 |pages= 509–19 |year= 1997 |pmid= 9128259 |doi=10.1083/jcb.137.2.509 | pmc=2139768 }}<br />
*{{cite journal | vauthors=Fuhlbrigge RC, Kieffer JD, Armerding D, Kupper TS |title=Cutaneous lymphocyte antigen is a specialized form of PSGL-1 expressed on skin-homing T cells. |journal=Nature |volume=389 |issue= 6654 |pages= 978–81 |year= 1997 |pmid= 9353122 |doi= 10.1038/40166 }}<br />
*{{cite journal |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 }}<br />
*{{cite journal |vauthors=Snapp KR, Ding H, Atkins K, etal |title=A novel P-selectin glycoprotein ligand-1 monoclonal antibody recognizes an epitope within the tyrosine sulfate motif of human PSGL-1 and blocks recognition of both P- and L-selectin. |journal=Blood |volume=91 |issue= 1 |pages= 154–64 |year= 1998 |pmid= 9414280 |doi= }}<br />
*{{cite journal |vauthors=Bennett EP, Hassan H, Mandel U, etal |title=Cloning of a human UDP-N-acetyl-alpha-D-Galactosamine:polypeptide N-acetylgalactosaminyltransferase that complements other GalNAc-transferases in complete O-glycosylation of the MUC1 tandem repeat. |journal=J. Biol. Chem. |volume=273 |issue= 46 |pages= 30472–81 |year= 1998 |pmid= 9804815 |doi=10.1074/jbc.273.46.30472 }}<br />
*{{cite journal |vauthors=Wimazal F, Ghannadan M, Müller MR, etal |title=Expression of homing receptors and related molecules on human mast cells and basophils: a comparative analysis using multi-color flow cytometry and toluidine blue/immunofluorescence staining techniques. |journal=Tissue Antigens |volume=54 |issue= 5 |pages= 499–507 |year= 2000 |pmid= 10599889 |doi=10.1034/j.1399-0039.1999.540507.x }}<br />
*{{cite journal | vauthors=Epperson TK, Patel KD, McEver RP, Cummings RD |title=Noncovalent association of P-selectin glycoprotein ligand-1 and minimal determinants for binding to P-selectin. |journal=J. Biol. Chem. |volume=275 |issue= 11 |pages= 7839–53 |year= 2000 |pmid= 10713099 |doi=10.1074/jbc.275.11.7839 }}<br />
*{{cite journal |vauthors=André P, Spertini O, Guia S, etal |title=Modification of P-selectin glycoprotein ligand-1 with a natural killer cell-restricted sulfated lactosamine creates an alternate ligand for L-selectin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3400–5 |year= 2000 |pmid= 10725346 |doi= 10.1073/pnas.040569797 | pmc=16251 }}<br />
*{{cite journal |vauthors=Frenette PS, Denis CV, Weiss L, etal |title=P-Selectin glycoprotein ligand 1 (PSGL-1) is expressed on platelets and can mediate platelet-endothelial interactions in vivo. |journal=J. Exp. Med. |volume=191 |issue= 8 |pages= 1413–22 |year= 2000 |pmid= 10770806 |doi=10.1084/jem.191.8.1413 | pmc=2193129 }}<br />
*{{cite journal |vauthors=Woltmann G, McNulty CA, Dewson G, etal |title=Interleukin-13 induces PSGL-1/P-selectin-dependent adhesion of eosinophils, but not neutrophils, to human umbilical vein endothelial cells under flow. |journal=Blood |volume=95 |issue= 10 |pages= 3146–52 |year= 2000 |pmid= 10807781 |doi= }}<br />
*{{cite journal |vauthors=Tsuchihashi S, Fondevila C, Shaw GD, etal |title=Molecular characterization of rat leukocyte P-selectin glycoprotein ligand-1 and effect of its blockade: protection from ischemia-reperfusion injury in liver transplantation. |journal=J Immunol |volume=176 |issue= 1 |pages= 616–24 |year= 2006 |pmid= 16365457 |doi= 10.4049/jimmunol.176.1.616}}<br />
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==External links==<br />
* {{MeshName|P-selectin+glycoprotein+ligand-1}}<br />
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{{Clusters of differentiation}}<br />
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[[Category:Clusters of differentiation]]<br />
[[Category:Receptors]]</div>en>JCW-CleanerBot