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'''Sialoadhesin''' is a [[cell adhesion molecule]] found on the surface of [[macrophage]]s. It is found in especially high amounts on macrophages of the spleen, liver, lymph node, bone marrow, colon, and lungs. Also, in patients suffering from rheumatoid arthritis, the protein has been found in great amounts on macrophages of the affected tissues.<ref name="Hartnell_2001">{{cite journal |vauthors=Hartnell A, Steel J, Turley H, Jones M, Jackson DG, Crocker PR | title = Characterization of human sialoadhesin, a sialic acid binding receptor expressed by resident and inflammatory macrophage populations | journal = Blood | volume = 97 | issue = 1 | pages = 288–96 |date=January 2001 | pmid = 11133773 | doi = 10.1182/blood.V97.1.288 }}</ref> It is defined as an I-type [[lectin]], since it contains 17 [[immunoglobulin domain|immunoglobulin (Ig) domains]] (one variable domain and 16 constant domains), and thus also belongs to the [[immunoglobulin superfamily]] (IgSF).  Sialoadhesin binds to certain molecules called [[sialic acid]]s. During this binding process a [[salt bridge (protein)]] is formed between a highly conserved [[arginine]] residue (from the v-set domain to the 3'-sialyllactose) and the carboxylate group of the sialic acid.<ref name="Hartnell_2001"/> Since sialoadhesin binds sialic acids with its [[N-terminal]] IgV-domain, it is also a member of the [[SIGLEC]] family. Alternate names for sialoadhesin include '''siglec-1''' and '''CD169''' ([[cluster of differentiation]] 169).<ref name="titlePROW Guide: Sialoadhesin, Siglec-1 (CD169)">{{cite web | url = http://mpr.nci.nih.gov/PROW/guide/985165905_g.htm | title = Sialoadhesin, Siglec-1 (CD169) | accessdate = 2011-04-15 | author = Varki A | date = 2001-09-10 | work = Protein Reviews on the Web (PROW) Guide | publisher = United States National Center for Biotechnology Information (NCBI) | pages = | language = | archiveurl = | archivedate = | quote = }}</ref>
'''Sialoadhesin''' is a [[cell adhesion molecule]] found on the surface of [[macrophage]]s. It is found in especially high amounts on macrophages of the spleen, liver, lymph node, bone marrow, colon, and lungs. Also, in patients suffering from rheumatoid arthritis, the protein has been found in great amounts on macrophages of the affected tissues.<ref name="Hartnell_2001">{{cite journal |vauthors=Hartnell A, Steel J, Turley H, Jones M, Jackson DG, Crocker PR | title = Characterization of human sialoadhesin, a sialic acid binding receptor expressed by resident and inflammatory macrophage populations | journal = Blood | volume = 97 | issue = 1 | pages = 288–96 |date=January 2001 | pmid = 11133773 | doi = 10.1182/blood.V97.1.288 }}</ref> It is defined as an I-type [[lectin]], since it contains 17 [[immunoglobulin domain|immunoglobulin (Ig) domains]] (one variable domain and 16 constant domains), and thus also belongs to the [[immunoglobulin superfamily]] (IgSF).  Sialoadhesin binds to certain molecules called [[sialic acid]]s. During this binding process a [[salt bridge (protein)]] is formed between a highly conserved [[arginine]] residue (from the v-set domain to the 3'-sialyllactose) and the carboxylate group of the sialic acid.<ref name="Hartnell_2001"/> Since sialoadhesin binds sialic acids with its [[N-terminal]] IgV-domain, it is also a member of the [[SIGLEC]] family. Alternate names for sialoadhesin include '''siglec-1''' and '''CD169''' ([[cluster of differentiation]] 169).<ref name="titlePROW Guide: Sialoadhesin, Siglec-1 (CD169)">{{cite web | url = http://mpr.nci.nih.gov/PROW/guide/985165905_g.htm | title = Sialoadhesin, Siglec-1 (CD169) | accessdate = 2011-04-15 | author = Varki A | date = 2001-09-10 | work = Protein Reviews on the Web (PROW) Guide | publisher = United States National Center for Biotechnology Information (NCBI) | pages = | language = | archiveurl = https://web.archive.org/web/20070701182416/http://mpr.nci.nih.gov/prow/guide/985165905_g.htm | archivedate = 2007-07-01 | quote = | deadurl = yes | df =  }}</ref>


Sialoadhesin predominantly binds [[neutrophil]]s, but can also bind [[monocyte]]s, [[natural killer cell]]s, [[B cell]]s and a subset of [[cytotoxic T cell]]s by interacting with sialic acid molecules in the [[ligand]]s on their surfaces.<ref>{{cite journal |vauthors=Kelm S, Pelz A, Schauer R, Filbin M, Tang S, de Bellard M, Schnaar R, Mahoney J, Hartnell A, Bradfield P |title=Sialoadhesin, myelin-associated glycoprotein and CD22 define a new family of sialic acid-dependent adhesion molecules of the immunoglobulin superfamily |journal=Curr Biol |volume=4 |issue=11 |pages=965–72 |year=1994 |pmid=7533044 |doi=10.1016/S0960-9822(00)00220-7}}</ref>
Sialoadhesin predominantly binds [[neutrophil]]s, but can also bind [[monocyte]]s, [[natural killer cell]]s, [[B cell]]s and a subset of [[cytotoxic T cell]]s by interacting with sialic acid molecules in the [[ligand]]s on their surfaces.<ref>{{cite journal |vauthors=Kelm S, Pelz A, Schauer R, Filbin M, Tang S, de Bellard M, Schnaar R, Mahoney J, Hartnell A, Bradfield P |title=Sialoadhesin, myelin-associated glycoprotein and CD22 define a new family of sialic acid-dependent adhesion molecules of the immunoglobulin superfamily |journal=Curr Biol |volume=4 |issue=11 |pages=965–72 |year=1994 |pmid=7533044 |doi=10.1016/S0960-9822(00)00220-7}}</ref>

Revision as of 04:00, 17 May 2018

Sialoadhesin
File:2BVE.pdb.jpg
Structure of the N-terimal domain of mouse sialoadhesin.[1]
Identifiers
SymbolSIGLEC1
Alt. symbolsSN, CD169
Entrez6614
HUGO11127
OMIM600751
PDB2BVE
RefSeqNM_023068
UniProtQ9BZZ2
Other data
LocusChr. 20 p13

Sialoadhesin is a cell adhesion molecule found on the surface of macrophages. It is found in especially high amounts on macrophages of the spleen, liver, lymph node, bone marrow, colon, and lungs. Also, in patients suffering from rheumatoid arthritis, the protein has been found in great amounts on macrophages of the affected tissues.[2] It is defined as an I-type lectin, since it contains 17 immunoglobulin (Ig) domains (one variable domain and 16 constant domains), and thus also belongs to the immunoglobulin superfamily (IgSF). Sialoadhesin binds to certain molecules called sialic acids. During this binding process a salt bridge (protein) is formed between a highly conserved arginine residue (from the v-set domain to the 3'-sialyllactose) and the carboxylate group of the sialic acid.[2] Since sialoadhesin binds sialic acids with its N-terminal IgV-domain, it is also a member of the SIGLEC family. Alternate names for sialoadhesin include siglec-1 and CD169 (cluster of differentiation 169).[3]

Sialoadhesin predominantly binds neutrophils, but can also bind monocytes, natural killer cells, B cells and a subset of cytotoxic T cells by interacting with sialic acid molecules in the ligands on their surfaces.[4]

Sialaodhesin (CD169) positive macrophages, along with mesenchymal stem cells and beta-adrenergic neurons, form the hematopoietic stem cell niche in the bone marrow. CD169+ macrophages mediate signaling between the various cells and seem to promote hematopoietic stem cell retention to the niche.

References

  1. PDB: 2BVE​; Zaccai NR, May AP, Robinson RC, Burtnick LD, Crocker PR, Brossmer R, Kelm S, Jones EY (February 2007). "Crystallographic and in silico analysis of the sialoside-binding characteristics of the Siglec sialoadhesin". J. Mol. Biol. 365 (5): 1469–79. doi:10.1016/j.jmb.2006.10.084. PMID 17137591.
  2. 2.0 2.1 Hartnell A, Steel J, Turley H, Jones M, Jackson DG, Crocker PR (January 2001). "Characterization of human sialoadhesin, a sialic acid binding receptor expressed by resident and inflammatory macrophage populations". Blood. 97 (1): 288–96. doi:10.1182/blood.V97.1.288. PMID 11133773.
  3. Varki A (2001-09-10). "Sialoadhesin, Siglec-1 (CD169)". Protein Reviews on the Web (PROW) Guide. United States National Center for Biotechnology Information (NCBI). Archived from the original on 2007-07-01. Retrieved 2011-04-15.
  4. Kelm S, Pelz A, Schauer R, Filbin M, Tang S, de Bellard M, Schnaar R, Mahoney J, Hartnell A, Bradfield P (1994). "Sialoadhesin, myelin-associated glycoprotein and CD22 define a new family of sialic acid-dependent adhesion molecules of the immunoglobulin superfamily". Curr Biol. 4 (11): 965–72. doi:10.1016/S0960-9822(00)00220-7. PMID 7533044.