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Gene Review

SIGLEC1  -  sialic acid binding Ig-like lectin 1,...

Homo sapiens

Synonyms: CD169, FLJ00051, FLJ00055, FLJ00073, FLJ32150, ...
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Disease relevance of SIGLEC1


Psychiatry related information on SIGLEC1


High impact information on SIGLEC1


Biological context of SIGLEC1


Anatomical context of SIGLEC1


Associations of SIGLEC1 with chemical compounds

  • Using antibodies raised to the recombinant protein, sialoadhesin was immunoprecipitated from the THP-1 human monocytic cell line as an approximate 200-kd glycoprotein [16].
  • In conclusion, sialoadhesin specifically recognizes the oligosaccharide sequence Neu5Ac alpha 2----3Gal beta 1----3GalNAc in either sialoglycoproteins or gangliosides [17].
  • The past year has provided the X-ray crystal structures of both the N-terminal domain of sialoadhesin and the extracytoplasmic domain of the cation-dependent mannose 6-phosphate receptor [18].
  • In contrast, sialoadhesin had less exacting specificity, binding to gangliosides that bear either terminal alpha2,3- or alpha2,8-linked sialic acids with the following rank-order potency of binding: GQ1balpha > GD1a = GD1b = GT1b = GM3 = GM4 > GD3 = GQ1b >> GM1 (nonbinder) [19].
  • Thus, while siglecs may not interfere with selectin-mediated recognition, fucosylation could negatively regulate siglec binding [20].

Physical interactions of SIGLEC1

  • Finally, sialoadhesin bound different glycoforms of CD43 expressed in Chinese hamster ovary cells, including unbranched (core 1) and branched (core 2) O:-linked glycans, that are normally found on CD43 in resting and activated T cells, respectively [11].
  • Related immunoglobulin (Ig) superfamily members either failed to bind gangliosides (CD22) or bound with less stringent specificity (sialoadhesin), whereas a modified form of MAG (bearing three of its five extra-cellular Ig-like domains) bound only GQ1b alpha [21].
  • The CD33 antigen is a 67-kd glycosylated transmembrane protein of the sialic acid-binding immunoglobulinlike lectin (siglec) family with immunoreceptor tyrosine-based inhibitory motifs [22].
  • Binding specificities of the sialoadhesin family of I-type lectins. Sialic acid linkage and substructure requirements for binding of myelin-associated glycoprotein, Schwann cell myelin protein, and sialoadhesin [19].
  • Human Siglec-5 is a sialic acid binding immunoglobulin (Ig)-like lectin (Siglec), comprising one N-terminal IgV-SET domain followed by three IgC2-SET domains, and a cytoplasmic domain with ITIM and SAP motifs which regulate cell signalling [23].

Regulatory relationships of SIGLEC1


Other interactions of SIGLEC1


Analytical, diagnostic and therapeutic context of SIGLEC1


  1. Human rhinoviruses inhibit the accessory function of dendritic cells by inducing sialoadhesin and B7-H1 expression. Kirchberger, S., Majdic, O., Steinberger, P., Blüml, S., Pfistershammer, K., Zlabinger, G., Deszcz, L., Kuechler, E., Knapp, W., Stöckl, J. J. Immunol. (2005) [Pubmed]
  2. Macrophage-tumour cell interactions: identification of MUC1 on breast cancer cells as a potential counter-receptor for the macrophage-restricted receptor, sialoadhesin. Nath, D., Hartnell, A., Happerfield, L., Miles, D.W., Burchell, J., Taylor-Papadimitriou, J., Crocker, P.R. Immunology (1999) [Pubmed]
  3. Loss of Siglec expression on T lymphocytes during human evolution. Nguyen, D.H., Hurtado-Ziola, N., Gagneux, P., Varki, A. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  4. CD33 responses are blocked by SOCS3 through accelerated proteasomal-mediated turnover. Orr, S.J., Morgan, N.M., Elliott, J., Burrows, J.F., Scott, C.J., McVicar, D.W., Johnston, J.A. Blood (2007) [Pubmed]
  5. A macrophage marker, Siglec-1, is increased on circulating monocytes in patients with systemic sclerosis and induced by type I interferons and toll-like receptor agonists. York, M.R., Nagai, T., Mangini, A.J., Lemaire, R., van Seventer, J.M., Lafyatis, R. Arthritis Rheum. (2007) [Pubmed]
  6. Accumulation of insoluble alpha-synuclein in dementia with Lewy bodies. Campbell, B.C., Li, Q.X., Culvenor, J.G., Jäkälä, P., Cappai, R., Beyreuther, K., Masters, C.L., McLean, C.A. Neurobiol. Dis. (2000) [Pubmed]
  7. Crystal structure of the N-terminal domain of sialoadhesin in complex with 3' sialyllactose at 1.85 A resolution. May, A.P., Robinson, R.C., Vinson, M., Crocker, P.R., Jones, E.Y. Mol. Cell (1998) [Pubmed]
  8. Identification and molecular cloning of p75/AIRM1, a novel member of the sialoadhesin family that functions as an inhibitory receptor in human natural killer cells. Falco, M., Biassoni, R., Bottino, C., Vitale, M., Sivori, S., Augugliaro, R., Moretta, L., Moretta, A. J. Exp. Med. (1999) [Pubmed]
  9. The mannose receptor and other macrophage lectins. Stahl, P.D. Curr. Opin. Immunol. (1992) [Pubmed]
  10. Myelin-associated glycoprotein interacts with neurons via a sialic acid binding site at ARG118 and a distinct neurite inhibition site. Tang, S., Shen, Y.J., DeBellard, M.E., Mukhopadhyay, G., Salzer, J.L., Crocker, P.R., Filbin, M.T. J. Cell Biol. (1997) [Pubmed]
  11. Cutting edge: CD43 functions as a T cell counterreceptor for the macrophage adhesion receptor sialoadhesin (Siglec-1). van den Berg, T.K., Nath, D., Ziltener, H.J., Vestweber, D., Fukuda, M., van Die, I., Crocker, P.R. J. Immunol. (2001) [Pubmed]
  12. Sialoadhesin (Sn) maps to mouse chromosome 2 and human chromosome 20 and is not linked to the other members of the sialoadhesin family, CD22, MAG, and CD33. Mucklow, S., Hartnell, A., Mattei, M.G., Gordon, S., Crocker, P.R. Genomics (1995) [Pubmed]
  13. Sialoadhesin, a macrophage sialic acid binding receptor for haemopoietic cells with 17 immunoglobulin-like domains. Crocker, P.R., Mucklow, S., Bouckson, V., McWilliam, A., Willis, A.C., Gordon, S., Milon, G., Kelm, S., Bradfield, P. EMBO J. (1994) [Pubmed]
  14. Immunologic and functional evidence for anti-Siglec-9 autoantibodies in intravenous immunoglobulin preparations. von Gunten, S., Schaub, A., Vogel, M., Stadler, B.M., Miescher, S., Simon, H.U. Blood (2006) [Pubmed]
  15. Cloning, characterization, and phylogenetic analysis of siglec-9, a new member of the CD33-related group of siglecs. Evidence for co-evolution with sialic acid synthesis pathways. Angata, T., Varki, A. J. Biol. Chem. (2000) [Pubmed]
  16. Characterization of human sialoadhesin, a sialic acid binding receptor expressed by resident and inflammatory macrophage populations. Hartnell, A., Steel, J., Turley, H., Jones, M., Jackson, D.G., Crocker, P.R. Blood (2001) [Pubmed]
  17. Purification and properties of sialoadhesin, a sialic acid-binding receptor of murine tissue macrophages. Crocker, P.R., Kelm, S., Dubois, C., Martin, B., McWilliam, A.S., Shotton, D.M., Paulson, J.C., Gordon, S. EMBO J. (1991) [Pubmed]
  18. New animal lectin structures. Rini, J.M., Lobsanov, Y.D. Curr. Opin. Struct. Biol. (1999) [Pubmed]
  19. Binding specificities of the sialoadhesin family of I-type lectins. Sialic acid linkage and substructure requirements for binding of myelin-associated glycoprotein, Schwann cell myelin protein, and sialoadhesin. Collins, B.E., Kiso, M., Hasegawa, A., Tropak, M.B., Roder, J.C., Crocker, P.R., Schnaar, R.L. J. Biol. Chem. (1997) [Pubmed]
  20. New aspects of siglec binding specificities, including the significance of fucosylation and of the sialyl-Tn epitope. Sialic acid-binding immunoglobulin superfamily lectins. Brinkman-Van der Linden, E.C., Varki, A. J. Biol. Chem. (2000) [Pubmed]
  21. Myelin-associated glycoprotein binding to gangliosides. Structural specificity and functional implications. Schnaar, R.L., Collins, B.E., Wright, L.P., Kiso, M., Tropak, M.B., Roder, J.C., Crocker, P.R. Ann. N. Y. Acad. Sci. (1998) [Pubmed]
  22. CD33 as a target for selective ablation of acute myeloid leukemia. Bernstein, I.D. Clinical lymphoma. (2002) [Pubmed]
  23. Human Siglec-5: tissue distribution, novel isoforms and domain specificities for sialic acid-dependent ligand interactions. Connolly, N.P., Jones, M., Watt, S.M. Br. J. Haematol. (2002) [Pubmed]
  24. Sialylation of the sialic acid binding lectin sialoadhesin regulates its ability to mediate cell adhesion. Barnes, Y.C., Skelton, T.P., Stamenkovic, I., Sgroi, D.C. Blood (1999) [Pubmed]
  25. High resolution crystal structures of Siglec-7. Insights into ligand specificity in the Siglec family. Alphey, M.S., Attrill, H., Crocker, P.R., van Aalten, D.M. J. Biol. Chem. (2003) [Pubmed]
  26. Regulated expression of MUC1 epithelial antigen in erythropoiesis. Rughetti, A., Biffoni, M., Pierelli, L., Rahimi, H., Bonanno, G., Barachini, S., Pellicciotta, I., Napoletano, C., Pescarmona, E., Del Nero, A., Pignoloni, P., Frati, L., Nuti, M. Br. J. Haematol. (2003) [Pubmed]
  27. Negative regulation of leucocyte functions by CD33-related siglecs. Avril, T., Attrill, H., Zhang, J., Raper, A., Crocker, P.R. Biochem. Soc. Trans. (2006) [Pubmed]
  28. Characterization of CD33 as a new member of the sialoadhesin family of cellular interaction molecules. Freeman, S.D., Kelm, S., Barber, E.K., Crocker, P.R. Blood (1995) [Pubmed]
  29. OB-BP1/Siglec-6. a leptin- and sialic acid-binding protein of the immunoglobulin superfamily. Patel, N., Brinkman-Van der Linden, E.C., Altmann, S.W., Gish, K., Balasubramanian, S., Timans, J.C., Peterson, D., Bell, M.P., Bazan, J.F., Varki, A., Kastelein, R.A. J. Biol. Chem. (1999) [Pubmed]
  30. CD83 is a sialic acid-binding Ig-like lectin (Siglec) adhesion receptor that binds monocytes and a subset of activated CD8+ T cells. Scholler, N., Hayden-Ledbetter, M., Hellström, K.E., Hellström, I., Ledbetter, J.A. J. Immunol. (2001) [Pubmed]
  31. Characterization of the sialic acid-binding site in sialoadhesin by site-directed mutagenesis. Vinson, M., van der Merwe, P.A., Kelm, S., May, A., Jones, E.Y., Crocker, P.R. J. Biol. Chem. (1996) [Pubmed]
  32. CD150 association with either the SH2-containing inositol phosphatase or the SH2-containing protein tyrosine phosphatase is regulated by the adaptor protein SH2D1A. Shlapatska, L.M., Mikhalap, S.V., Berdova, A.G., Zelensky, O.M., Yun, T.J., Nichols, K.E., Clark, E.A., Sidorenko, S.P. J. Immunol. (2001) [Pubmed]
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