Sialoadhesin and related cellular recognition molecules of the immunoglobulin superfamily
Sialoadhesin and related cellular recognition molecules of the immunoglobulin superfamily
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DOI:
10.1042/bst0240150
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发表时间:
1996-02-01
影响因子:
3.9
通讯作者:
Mucklow, S
中科院分区:
文献类型:
--
作者:
Crocker, PR;Kelm, S;Mucklow, S
Cell-cell interactions play a crucial role in a broad range of biological and pathological processes encompassing cell migration and differentiation, inflammation, immune function, development and embryogenesis. The majority of cell interaction molecules fall into discrete families based on their primary structure and domain organization. These include the immunoglobulin superfamily, integrins, cadherins and selectins. The largest of these families is the immunoglobulin superfamily (IgSF) which contains over 100 members. These proteins are generally considered to mediate intercellular communication through specific protein-protein interactions. However, the recent characterization of the sialoadhesin family of lectin-like cell adhesion molecules of the IgSF [1, 2] has shown that protein-carbohydrate interactions are also important. All members of this family can mediate sialic acid (sia)-dependent adhesion. To date, it includes the eponymous member, sialoadhesin (Sn), expressed uniquely by subpopulations of macrophages [3], CD33 expressed by cells of the myelomonocytic lineage [2, 4], CD22 expressed by B-lymphocytes [5, 6], the myelin associated glycoprotein (MAG) expressed by myelinating glial cells [1, 7] and the Schwann cell myelin protein (SMP) expressed by glial cells of the chick and quail [8, 9]. SMP will not be considered further in this article because it is the least characterized of the family and as yet no mammalian homologue has been identified. All members of the sialoadhesin family have a simi-