Sialoadhesin
From Wikipedia, the free encyclopedia
Sialic acid binding Ig-like lectin 1, sialoadhesin
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Identifiers | |
Symbol | SIGLEC1 |
Alt. Symbols | SN, CD169 |
Entrez | 6614 |
HUGO | 11127 |
OMIM | 600751 |
RefSeq | NM_023068 |
UniProt | Q9BZZ2 |
Other data | |
Locus | Chr. 20 p13 |
Sialoadhesin is a cell adhesion molecule found on the surface of certain cells of the immune system called macrophages. 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). 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).[1]
Sialoadhesin predomiantly 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.[2]
[edit] References
- ^ Ajit Varki. PROW Guide: Sialoadhesin, Siglec-1 (CD169). Retrieved on 2008-02-23.
- ^ 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: . PMID 7533044.
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