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Gene Review

SELP  -  selectin P (granule membrane protein...

Homo sapiens

Synonyms: CD62, CD62 antigen-like family member P, CD62P, GMP-140, GMP140, ...
 
 
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Disease relevance of SELP

 

Psychiatry related information on SELP

  • There was no difference between subjects with PTSD and healthy control subjects in proportions of circulating lymphocyte subsets or in expression of the lymphocyte markers CD62, CD25, and CD45RO/CD45RA [5].
  • To assess whether platelets are activated in transient global amnesia (TGA) and TIA, blood samples were analyzed by fluorescence-activated cytoscan using antibodies specific for platelet fibrinogen receptor (PAC1) and P-selectin (CD62P) [6].
 

High impact information on SELP

  • This network of interactions includes three genes in the TGF-beta pathway and SELP, which is associated with stroke in the general population [7].
  • The neutrophil selectin LECAM-1 presents carbohydrate ligands to the vascular selectins ELAM-1 and GMP-140 [8].
  • Adhesion of resting or activated neutrophils through the integrins LFA-1 and Mac-1 to ICAM-1 in a lipid bilayer does not occur at physiologic shear stresses; however, static incubation of activated neutrophils allows development of adhesion that is greater than 100-fold more shear resistant than found on CD62 [9].
  • Data presented to date suggest that one ligand of CD62 includes CD15 (Lewis x determinant) and sialic acid [10].
  • Addition of a chemoattractant to activate LFA-1 and Mac-1 results in the arrest of neutrophils rolling on bilayers containing both CD62 and ICAM-1 [9].
 

Chemical compound and disease context of SELP

 

Biological context of SELP

  • No significant differences in both SELP SNPs were found between patients and controls, whereas a decreased frequency of the Met62Ile SNP was found in patients versus controls in the Italian population (P = 0.025) [1].
  • Cloning of GMP-140, a granule membrane protein of platelets and endothelium: sequence similarity to proteins involved in cell adhesion and inflammation [16].
  • In situ hybridization mapped GMP-140 to human chromosome 1 bands 21-24 consistent with chromosomal localization of LHR [17].
  • These data suggest that LHR, ELAM-1, and GMP-140 comprise an adhesion protein family, the selectins, that arose by multiple gene duplication events before divergence of mouse and human [17].
  • PADGEM protein (PADGEM), also known as GMP140, is a platelet alpha-granule membrane protein that is translocated to the external membrane after platelet activation [18].
 

Anatomical context of SELP

 

Associations of SELP with chemical compounds

  • Within minutes after stimulation with phorbol esters or histamine, human endothelial cells become adhesive for neutrophils; this interaction is inhibited by antibodies to GMP-140 [20].
  • Recognition requires sialic acid, because cells expressing large amounts of Lewis x, but not sialyl Lewis x, do not interact with GMP-140 [21].
  • Thus, the sialyl Lewis x tetrasaccharide may require additional structural modifications or specific presentations in order for leukocytes in flowing blood to interact rapidly and with high affinity to GMP-140 on activated platelets or endothelium [21].
  • 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 [22].
  • These observations led to the hypothesis that sulfatide may play a role in facilitating the disengagement of CD62, allowing the efficient exit of granulocytes from the blood stream at sites of inflammation [23].
 

Physical interactions of SELP

  • In adults, after in vitro activation of platelets with thrombin and ADP, VWF binding to platelets increased and correlated significantly with CD62P expression (r = 0.71, p < 0.001) [24].
  • EMP were analyzed by fluorescent activated cell sorting (FACS), detecting the particels via expression of CD62 (E-selectin) and anionic phospholipids binding to annexin V [25].
 

Regulatory relationships of SELP

  • In wheals of > or = 6 h duration, GMP-140 was only weakly expressed whereas ELAM-1 and ICAM-1 were markedly up-regulated in lesional and less so in nonlesional skin of acute, chronic recurrent and delayed pressure urticaria [26].
  • GPVI-deficient platelets showed some fibrinogen binding in response to collagen but failed to aggregate and to express CD62 and CD63 [27].
  • In vitro studies of anticoagulated whole blood inoculated with Neisseria meningitidis supported these clinical findings with marked increases in PMNL CD11b/CD18 expression and activation but no detectable changes in platelet-activated alphaIIbbeta3 or CD62P expression [28].
  • However, Serratia treatment almost completely abolished the increase in platelet surface GMP-140 induced by low concentrations of alpha-thrombin (0.5 nmol/L) and diminished the downregulation of platelet surface GPIX by 60.9% +/- 5.6% (mean +/- SEM, n = 3) [29].
  • To detect only the activated form of PMPs, a new ELISA needs to be developed, and it will likely use a combination of antibodies that detect platelet activation markers such as P-selectin (CD62P) or activated GPIIb/IIIa [30].
 

Other interactions of SELP

  • In endothelial cells treated with secretagogues that stimulate vWf release the elongated structures positive for PADGEM disappeared, further identifying these structures as Weibel-Palade bodies [18].
  • Platelet activation was characterized by flow cytometric measurement of GPIIb/IIIa and GMP-140 in whole blood and washed platelets suspensions, with antihuman fluorescent monoclonal antibodies [31].
  • The estimation of platelet adhesion and activation was performed with two enzyme immunoassays (EIAs) using monoclonal antibodies directed against CD42b (GP lb) and CD 62 (GMP 140 or P-Selectin) [32].
  • Agreeing with previous data, less than 2% of platelets from peripheral blood of normal individuals expressed the activation markers CD62P or CD63 [33].
  • Platelet GMP-140, along with ELAM-1 and gp90MEL, comprise the LEC-CAM family of cell-cell adhesion proteins [34].
 

Analytical, diagnostic and therapeutic context of SELP

References

  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. Monocyte-endothelial adhesion in chronic rheumatoid arthritis. In situ detection of selectin and integrin-dependent interactions. Grober, J.S., Bowen, B.L., Ebling, H., Athey, B., Thompson, C.B., Fox, D.A., Stoolman, L.M. J. Clin. Invest. (1993) [Pubmed]
  3. Granule membrane protein 140 (GMP140) binds to carcinomas and carcinoma-derived cell lines. Aruffo, A., Dietsch, M.T., Wan, H., Hellström, K.E., Hellström, I. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  4. Adhesion molecule expression in Graves' thyroid glands; potential relevance of granule membrane protein (GMP-140) and intercellular adhesion molecule-1 (ICAM-1) in the homing and antigen presentation processes. Miyazaki, A., Mirakian, R., Bottazzo, G.F. Clin. Exp. Immunol. (1992) [Pubmed]
  5. Immune function in PTSD. Altemus, M., Dhabhar, F.S., Yang, R. Ann. N. Y. Acad. Sci. (2006) [Pubmed]
  6. Activated platelets in transient global amnesia and TIA. Hirabayashi, H., Shimizu, M., Kohara, S., Shinohara, Y. Neurology (2004) [Pubmed]
  7. Genetic dissection and prognostic modeling of overt stroke in sickle cell anemia. Sebastiani, P., Ramoni, M.F., Nolan, V., Baldwin, C.T., Steinberg, M.H. Nat. Genet. (2005) [Pubmed]
  8. The neutrophil selectin LECAM-1 presents carbohydrate ligands to the vascular selectins ELAM-1 and GMP-140. Picker, L.J., Warnock, R.A., Burns, A.R., Doerschuk, C.M., Berg, E.L., Butcher, E.C. Cell (1991) [Pubmed]
  9. Leukocytes roll on a selectin at physiologic flow rates: distinction from and prerequisite for adhesion through integrins. Lawrence, M.B., Springer, T.A. Cell (1991) [Pubmed]
  10. CD62/P-selectin recognition of myeloid and tumor cell sulfatides. Aruffo, A., Kolanus, W., Walz, G., Fredman, P., Seed, B. Cell (1991) [Pubmed]
  11. Adenoviral gene delivery to solid tumors by recombinant silk-elastinlike protein polymers. Hatefi, A., Cappello, J., Ghandehari, H. Pharm. Res. (2007) [Pubmed]
  12. Lipopolysaccharide from enterohemorrhagic Escherichia coli binds to platelets through TLR4 and CD62 and is detected on circulating platelets in patients with hemolytic uremic syndrome. Ståhl, A.L., Svensson, M., Mörgelin, M., Svanborg, C., Tarr, P.I., Mooney, J.C., Watkins, S.L., Johnson, R., Karpman, D. Blood (2006) [Pubmed]
  13. Different levels of platelet activation in preeclamptic, normotensive pregnant, and nonpregnant women. Holthe, M.R., Staff, A.C., Berge, L.N., Lyberg, T. Am. J. Obstet. Gynecol. (2004) [Pubmed]
  14. Platelet activation with unfractionated heparin at therapeutic concentrations and comparisons with a low-molecular-weight heparin and with a direct thrombin inhibitor. Xiao, Z., Théroux, P. Circulation (1998) [Pubmed]
  15. Reversible inhibition of human platelet activation by hypothermia in vivo and in vitro. Michelson, A.D., MacGregor, H., Barnard, M.R., Kestin, A.S., Rohrer, M.J., Valeri, C.R. Thromb. Haemost. (1994) [Pubmed]
  16. Cloning of GMP-140, a granule membrane protein of platelets and endothelium: sequence similarity to proteins involved in cell adhesion and inflammation. Johnston, G.I., Cook, R.G., McEver, R.P. Cell (1989) [Pubmed]
  17. Genomic organization of the selectin family of leukocyte adhesion molecules on human and mouse chromosome 1. Watson, M.L., Kingsmore, S.F., Johnston, G.I., Siegelman, M.H., Le Beau, M.M., Lemons, R.S., Bora, N.S., Howard, T.A., Weissman, I.L., McEver, R.P. J. Exp. Med. (1990) [Pubmed]
  18. PADGEM (GMP140) is a component of Weibel-Palade bodies of human endothelial cells. Bonfanti, R., Furie, B.C., Furie, B., Wagner, D.D. Blood (1989) [Pubmed]
  19. The genes encoding E-selectin (SELE) and lymphotactin (SCYC1) lie on separate chicken chromosomes although they are closely linked in human and mouse. Morroll, S., Goodchild, M., Salmon, N., Copeland, N.G., Gilbert, D.J., Jenkins, N.A., Bumstead, N., Boyd, Y. Immunogenetics (2001) [Pubmed]
  20. Rapid neutrophil adhesion to activated endothelium mediated by GMP-140. Geng, J.G., Bevilacqua, M.P., Moore, K.L., McIntyre, T.M., Prescott, S.M., Kim, J.M., Bliss, G.A., Zimmerman, G.A., McEver, R.P. Nature (1990) [Pubmed]
  21. The selectin GMP-140 binds to sialylated, fucosylated lactosaminoglycans on both myeloid and nonmyeloid cells. Zhou, Q., Moore, K.L., Smith, D.F., Varki, A., McEver, R.P., Cummings, R.D. J. Cell Biol. (1991) [Pubmed]
  22. 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]
  23. CD62/P-selectin binding sites for myeloid cells and sulfatides are overlapping. Bajorath, J., Hollenbaugh, D., King, G., Harte, W., Eustice, D.C., Darveau, R.P., Aruffo, A. Biochemistry (1994) [Pubmed]
  24. The relationship of von Willebrand factor binding to activated platelets from healthy neonates and adults. Schmugge, M., Rand, M.L., Bang, K.W., Mody, M., Dunn, M.S., Amankwah, K.S., Blanchette, V.S., Freedman, J. Pediatr. Res. (2003) [Pubmed]
  25. Endothelial cell-derived microparticles in allogeneic hematopoietic stem cell recipients. Pihusch, V., Rank, A., Steber, R., Pihusch, M., Pihusch, R., Toth, B., Hiller, E., Kolb, H.J. Transplantation (2006) [Pubmed]
  26. Differential endothelial adhesion molecule expression in early and late whealing reactions. Haas, N., Schadendorf, D., Henz, B.M. Int. Arch. Allergy Immunol. (1998) [Pubmed]
  27. Glycoprotein VI is a major collagen receptor for platelet activation: it recognizes the platelet-activating quaternary structure of collagen, whereas CD36, glycoprotein IIb/IIIa, and von Willebrand factor do not. Kehrel, B., Wierwille, S., Clemetson, K.J., Anders, O., Steiner, M., Knight, C.G., Farndale, R.W., Okuma, M., Barnes, M.J. Blood (1998) [Pubmed]
  28. Severe meningococcal disease is characterized by early neutrophil but not platelet activation and increased formation and consumption of platelet-neutrophil complexes. Peters, M.J., Heyderman, R.S., Faust, S., Dixon, G.L., Inwald, D.P., Klein, N.J. J. Leukoc. Biol. (2003) [Pubmed]
  29. Glycoprotein Ib (GPIb)-dependent and GPIb-independent pathways of thrombin-induced platelet activation. Yamamoto, N., Greco, N.J., Barnard, M.R., Tanoue, K., Yamazaki, H., Jamieson, G.A., Michelson, A.D. Blood (1991) [Pubmed]
  30. Development and assessment of enzyme immunoassay for platelet-derived microparticles. Osumi, K., Ozeki, Y., Saito, S., Nagamura, Y., Ito, H., Kimura, Y., Ogura, H., Nomura, S. Thromb. Haemost. (2001) [Pubmed]
  31. Study of platelet adhesion in patients with uncomplicated hypertension. Andrioli, G., Ortolani, R., Fontana, L., Gaino, S., Bellavite, P., Lechi, C., Minuz, P., Manzato, F., Tridente, G., Lechi, A. J. Hypertens. (1996) [Pubmed]
  32. Application of enzyme immunoassays for testing haemocompatibility of biomedical polymers. Groth, T., Campbell, E.J., Herrmann, K., Seifert, B. Biomaterials (1995) [Pubmed]
  33. Whole blood microvolume laser scanning cytometry for monitoring resting and activated platelets. Wyant, T.L., Smith, P.C., Brown, B., Kantor, A.B. Platelets (2001) [Pubmed]
  34. Requirement for sialic acid on neutrophils in a GMP-140 (PADGEM) mediated adhesive interaction with activated platelets. Corral, L., Singer, M.S., Macher, B.A., Rosen, S.D. Biochem. Biophys. Res. Commun. (1990) [Pubmed]
  35. Redistribution of membrane glycoproteins in platelets activated under flow conditions. Lozano, M., Escolar, G., White, J.G., Tàssies, D., Ordinas, A., Díaz-Ricart, M. Blood Coagul. Fibrinolysis (1996) [Pubmed]
  36. Lectin binding to chronic inflammatory gingival tissue: possible adhesion mechanisms based on lectin-carbohydrate interactions. Krugluger, W., Lill, W., Nell, A., Katzensteiner, S., Sperr, W., Förster, O. J. Periodont. Res. (1993) [Pubmed]
  37. Increased plasma thrombomodulin as a vascular endothelial cell marker in patients with thrombotic thrombocytopenic purpura and hemolytic uremic syndrome. Mori, Y., Wada, H., Okugawa, Y., Tamaki, S., Nakasaki, T., Watanabe, R., Gabazza, E.C., Nishikawa, M., Minami, N., Shiku, H. Clin. Appl. Thromb. Hemost. (2001) [Pubmed]
 
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