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Gene Review

SELPLG  -  selectin P ligand

Homo sapiens

Synonyms: CD162, CLA, P-selectin glycoprotein ligand 1, PSGL-1, PSGL1, ...
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Disease relevance of SELPLG


High impact information on SELPLG

  • Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1 [6].
  • The selectins bind weakly to sialyl Lewisx (SLe(X))-like glycans, but with high-affinity to specific glycoprotein counterreceptors, including PSGL-1 [6].
  • We also present the crystal structure of P-selectin LE co-complexed with the N-terminal domain of human PSGL-1 modified by both tyrosine sulfation and SLe(X) [6].
  • P-selectin binding to neutrophils requires a specific protein, P-selectin glycoprotein ligand 1 (PSGL-1), as well as sialyl-Lewis X (sLex) glycan determinants [7].
  • P-selectin glycoprotein ligand 1 (PSGL-1) is a mucin-like glycoprotein expressed on the surface of myeloid cells and serves as the high affinity counterreceptor for P-selectin [8].

Chemical compound and disease context of SELPLG

  • P-Selectin (SELP) and P-selectin glycoprotein ligand-1 (SELPLG) constitute a receptor/ligand complex involved in the recruitment of activated lymphocytes, a critical event in the pathogenesis of multiple sclerosis (MS) [1].
  • Here we postulated that blockade of the earliest steps in leukocyte adhesion (ie, leukocyte rolling) via administration of a recombinant soluble form of P-selectin glycoprotein ligand-1 (PSGL-1; the recombinant soluble form is rsPSGL.Ig) would attenuate selectin-mediated events observed in the rat during traumatic shock [9].

Biological context of SELPLG


Anatomical context of SELPLG


Associations of SELPLG with chemical compounds

  • The interaction of PSGL-1 with P-selectin (CD62P) mediates tethering, rolling, and weak adhesion of leukocytes, during which they become sufficiently activated in situ by locally released or displayed cytokines and chemoattractants for integrin-mediated firm adhesion [11].
  • The organization of the PSGL-1 gene closely resembles those of CD43 and human platelet glycoprotein GPIb alpha, both of which have an intron in the 5'-noncoding region, a long second exon containing the complete coding region, and TATA-less promoters [12].
  • The loss of CD162 and CD62L expression was inhibited by EDTA, which suggests that neutrophil activation and sheddase cleavage occurred [14].
  • CONCLUSION: G-CSF, but not dexamethasone, down regulates PSGL-1 expression on the surface of neutrophils in humans [15].
  • The remaining eosinophils in the allergen challenged asthmatics were not activated as defined by cell density or change of expression of VLA-4, Mac-1 and PSGL-1 [16].

Physical interactions of SELPLG

  • Interaction of PSGL-1 with moesin was shown in HL-60 cell lysates by isolating a complex with glutathione S-transferase fusions of the cytoplasmic domain of PSGL-1 [17].
  • Exogenous eosinophil activation converts PSGL-1-dependent binding to CD18-dependent stable adhesion to platelets in shear flow [18].
  • Crystals of the radixin FERM domain bound to PSGL-1 belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 80.74, b = 85.73, c = 117.75 A, and contain two complexes in the crystallographic asymmetric unit [19].
  • These data show that P-selectin requires only the lectin and EGF domains to bind to PSGL-1 [20].
  • Simultaneous expression of core-2 beta1,6-N-acetylglucosaminyltransferase and fucosyltransferase VII was required for optimal L-selectin binding to PSGL-1 [21].

Enzymatic interactions of SELPLG


Regulatory relationships of SELPLG

  • In contrast, G-CSF rapidly down regulated PSGL-1 expression on neutrophils within 90 minutes, whereas neither dexamethasone nor placebo had an effect [15].
  • Similar to G-CSF, GM-CSF down regulated PSGL-1 in vitro [15].
  • Anti-P-selectin glycoprotein ligand-1 (PSGL-1) antibodies dramatically block the recruitment of CD8+ cells in brain vessels of patients with MS, suggesting that PSGL-1 represents a novel pharmaceutical target that may be exploited to block the selective entrance of CD8+ cells during early inflammation [23].
  • This study shows that binding of P-selectin to PSGL-1 triggers tyrosine kinase-dependent mechanisms that lead to CD11b/CD18 activation in PMN [24].
  • Pharmacologic disruption of interactions between moesin and F-actin in cells expressing PSGL-1 resulted in a dose-dependent inhibition of rolling on P-selectin [25].

Other interactions of SELPLG


Analytical, diagnostic and therapeutic context of SELPLG


  1. SELPLG and SELP single-nucleotide polymorphisms in multiple sclerosis. Fenoglio, C., Galimberti, D., Ban, M., Maranian, M., Scalabrini, D., Venturelli, E., Piccio, L., De Riz, M., Yeo, T.W., Goris, A., Gray, J., Bresolin, N., Scarpini, E., Compston, A., Sawcer, S. Neurosci. Lett. (2006) [Pubmed]
  2. Intracellular parasitism by the human granulocytic ehrlichiosis bacterium through the P-selectin ligand, PSGL-1. Herron, M.J., Nelson, C.M., Larson, J., Snapp, K.R., Kansas, G.S., Goodman, J.L. Science (2000) [Pubmed]
  3. Increased platelet-monocyte aggregates and cardiovascular disease in end-stage renal failure patients. Ashman, N., Macey, M.G., Fan, S.L., Azam, U., Yaqoob, M.M. Nephrol. Dial. Transplant. (2003) [Pubmed]
  4. Polymorphisms in the P-selectin (CD62P) and P-selectin glycoprotein ligand-1 (PSGL-1) genes and coronary heart disease. Bugert, P., Vosberg, M., Entelmann, M., Jahn, J., Katus, H.A., Klüter, H. Clin. Chem. Lab. Med. (2004) [Pubmed]
  5. Role of platelet P-selectin and microparticle PSGL-1 in thrombus formation. Furie, B., Furie, B.C. Trends in molecular medicine. (2004) [Pubmed]
  6. Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1. Somers, W.S., Tang, J., Shaw, G.D., Camphausen, R.T. Cell (2000) [Pubmed]
  7. PSGL-1 recognition of P-selectin is controlled by a tyrosine sulfation consensus at the PSGL-1 amino terminus. Pouyani, T., Seed, B. Cell (1995) [Pubmed]
  8. A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding. Sako, D., Comess, K.M., Barone, K.M., Camphausen, R.T., Cumming, D.A., Shaw, G.D. Cell (1995) [Pubmed]
  9. Effect of recombinant soluble P-selectin glycoprotein ligand-1 on leukocyte-endothelium interaction in vivo. Role in rat traumatic shock. Scalia, R., Hayward, R., Armstead, V.E., Minchenko, A.G., Lefer, A.M. Circ. Res. (1999) [Pubmed]
  10. ITAM-based interaction of ERM proteins with Syk mediates signaling by the leukocyte adhesion receptor PSGL-1. Urzainqui, A., Serrador, J.M., Viedma, F., Yáñez-Mó, M., Rodríguez, A., Corbí, A.L., Alonso-Lebrero, J.L., Luque, A., Deckert, M., Vázquez, J., Sánchez-Madrid, F. Immunity (2002) [Pubmed]
  11. P-selectin binding to P-selectin glycoprotein ligand-1 induces an intermediate state of alphaMbeta2 activation and acts cooperatively with extracellular stimuli to support maximal adhesion of human neutrophils. Ma, Y.Q., Plow, E.F., Geng, J.G. Blood (2004) [Pubmed]
  12. Genomic organization and chromosomal localization of the gene encoding human P-selectin glycoprotein ligand. Veldman, G.M., Bean, K.M., Cumming, D.A., Eddy, R.L., Sait, S.N., Shows, T.B. J. Biol. Chem. (1995) [Pubmed]
  13. Human mast cell progenitors use alpha4-integrin, VCAM-1, and PSGL-1 E-selectin for adhesive interactions with human vascular endothelium under flow conditions. Boyce, J.A., Mellor, E.A., Perkins, B., Lim, Y.C., Luscinskas, F.W. Blood (2002) [Pubmed]
  14. Diminished adhesion of Anaplasma phagocytophilum-infected neutrophils to endothelial cells is associated with reduced expression of leukocyte surface selectin. Choi, K.S., Garyu, J., Park, J., Dumler, J.S. Infect. Immun. (2003) [Pubmed]
  15. Rapid down modulation of P-selectin glycoprotein ligand-1 (PSGL-1, CD162) by G-CSF in humans. Jilma, B., Hergovich, N., Homoncik, M., Marsik, C., Kreuzer, C., Jilma-Stohlawetz, P. Transfusion (2002) [Pubmed]
  16. Eosinophil traffic in the circulation following allergen challenge. Sklar, L.A., Tsuji, H., Edwards, B.S., Larson, R.S., Schuyler, M. Allergy (2004) [Pubmed]
  17. Polarization and interaction of adhesion molecules P-selectin glycoprotein ligand 1 and intercellular adhesion molecule 3 with moesin and ezrin in myeloid cells. Alonso-Lebrero, J.L., Serrador, J.M., Domínguez-Jiménez, C., Barreiro, O., Luque, A., del Pozo, M.A., Snapp, K., Kansas, G., Schwartz-Albiez, R., Furthmayr, H., Lozano, F., Sánchez-Madrid, F. Blood (2000) [Pubmed]
  18. Exogenous eosinophil activation converts PSGL-1-dependent binding to CD18-dependent stable adhesion to platelets in shear flow. McCarty, O.J., Tien, N., Bochner, B.S., Konstantopoulos, K. Am. J. Physiol., Cell Physiol. (2003) [Pubmed]
  19. Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tails of adhesion molecules CD43 and PSGL-1. Takai, Y., Kitano, K., Terawaki, S., Maesaki, R., Hakoshima, T. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. (2007) [Pubmed]
  20. Soluble monomeric P-selectin containing only the lectin and epidermal growth factor domains binds to P-selectin glycoprotein ligand-1 on leukocytes. Mehta, P., Patel, K.D., Laue, T.M., Erickson, H.P., McEver, R.P. Blood (1997) [Pubmed]
  21. Molecular basis of leukocyte rolling on PSGL-1. Predominant role of core-2 O-glycans and of tyrosine sulfate residue 51. Bernimoulin, M.P., Zeng, X.L., Abbal, C., Giraud, S., Martinez, M., Michielin, O., Schapira, M., Spertini, O. J. Biol. Chem. (2003) [Pubmed]
  22. Regulation of P-selectin binding to the neutrophil P-selectin counter-receptor P-selectin glycoprotein ligand-1 by neutrophil elastase and cathepsin G. Gardiner, E.E., De Luca, M., McNally, T., Michelson, A.D., Andrews, R.K., Berndt, M.C. Blood (2001) [Pubmed]
  23. CD8+ T cells from patients with acute multiple sclerosis display selective increase of adhesiveness in brain venules: a critical role for P-selectin glycoprotein ligand-1. Battistini, L., Piccio, L., Rossi, B., Bach, S., Galgani, S., Gasperini, C., Ottoboni, L., Ciabini, D., Caramia, M.D., Bernardi, G., Laudanna, C., Scarpini, E., McEver, R.P., Butcher, E.C., Borsellino, G., Constantin, G. Blood (2003) [Pubmed]
  24. Platelet/polymorphonuclear leukocyte interaction: P-selectin triggers protein-tyrosine phosphorylation-dependent CD11b/CD18 adhesion: role of PSGL-1 as a signaling molecule. Evangelista, V., Manarini, S., Sideri, R., Rotondo, S., Martelli, N., Piccoli, A., Totani, L., Piccardoni, P., Vestweber, D., de Gaetano, G., Cerletti, C. Blood (1999) [Pubmed]
  25. Attachment of the PSGL-1 cytoplasmic domain to the actin cytoskeleton is essential for leukocyte rolling on P-selectin. Snapp, K.R., Heitzig, C.E., Kansas, G.S. Blood (2002) [Pubmed]
  26. Lipid raft adhesion receptors and Syk regulate selectin-dependent rolling under flow conditions. Abbal, C., Lambelet, M., Bertaggia, D., Gerbex, C., Martinez, M., Arcaro, A., Schapira, M., Spertini, O. Blood (2006) [Pubmed]
  27. Noncovalent association of P-selectin glycoprotein ligand-1 and minimal determinants for binding to P-selectin. Epperson, T.K., Patel, K.D., McEver, R.P., Cummings, R.D. J. Biol. Chem. (2000) [Pubmed]
  28. Binding of ADAM28 to P-selectin glycoprotein ligand-1 enhances P-selectin-mediated leukocyte adhesion to endothelial cells. Shimoda, M., Hashimoto, G., Mochizuki, S., Ikeda, E., Nagai, N., Ishida, S., Okada, Y. J. Biol. Chem. (2007) [Pubmed]
  29. Increased PSGL-1 expression on granulocytes from allergic-asthmatic subjects results in enhanced leukocyte recruitment under flow conditions. Dang, B., Wiehler, S., Patel, K.D. J. Leukoc. Biol. (2002) [Pubmed]
  30. Isolated P-selectin glycoprotein ligand-1 dynamic adhesion to P- and E-selectin. Goetz, D.J., Greif, D.M., Ding, H., Camphausen, R.T., Howes, S., Comess, K.M., Snapp, K.R., Kansas, G.S., Luscinskas, F.W. J. Cell Biol. (1997) [Pubmed]
  31. Shear-dependent capping of L-selectin and P-selectin glycoprotein ligand 1 by E-selectin signals activation of high-avidity beta2-integrin on neutrophils. Green, C.E., Pearson, D.N., Camphausen, R.T., Staunton, D.E., Simon, S.I. J. Immunol. (2004) [Pubmed]
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