SIALOADHESIN, A MACROPHAGE SIALIC-ACID BINDING-RECEPTOR FOR HEMATOPOIETIC-CELLS WITH 17 IMMUNOGLOBULIN-LIKE DOMAINS

SIALOADHESIN, A MACROPHAGE SIALIC-ACID BINDING-RECEPTOR FOR HEMATOPOIETIC-CELLS WITH 17 IMMUNOGLOBULIN-LIKE DOMAINS
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DOI:
10.1002/j.1460-2075.1994.tb06771.x
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发表时间:
1994-10-03
期刊:
影响因子:
11.4
通讯作者:
BRADFIELD, P
BRADFIELD, P
中科院分区:
生物学1区
文献类型:
--
作者:
CROCKER, PR;MUCKLOW, S;BRADFIELD, P

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Sialoadhesin is a macrophage-restricted adhesion molecule of 185 kDa that mediates sialic acid-dependent binding to cells. It is expressed strongly by macrophages in lymphoid and haemopoietic tissues where it is likely to mediate cell-cell interactions. Here we report the molecular cloning of murine sialoadhesin and show that it is a new member of the immunoglobulin (Ig) superfamily with 17 Ig-like domains. COS cells transfected with a cDNA encoding full-length sialoadhesin bound mouse bone marrow cells in a sialic acid-dependent manner. Alternatively spliced cDNAs, predicting soluble forms of sialoadhesin containing the first three or 16 Ig-like domains of sialoadhesin, were expressed in COS cells and the respective proteins purified. When immobilized on plastic, the 16-domain form bound cells in a sialic acid-dependent manner, suggesting that sialoadhesin can function in both secreted and membrane-bound forms. The most similar proteins in the database were CD22, myelin-associated glycoprotein, Schwann cell myelin protein and CD33. Like sialoadhesin, CD22 mediates sialic acid-dependent cell adhesion. The sequence similarity of sialoadhesin to CD22 and related members of the Ig superfamily indicates the existence of a novel family of sialic acid binding proteins involved in cell-cell interactions.