PURIFICATION AND PROPERTIES OF SIALOADHESIN, A SIALIC ACID-BINDING RECEPTOR OF MURINE TISSUE MACROPHAGES
PURIFICATION AND PROPERTIES OF SIALOADHESIN, A SIALIC ACID-BINDING RECEPTOR OF MURINE TISSUE MACROPHAGES
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DOI：
10.1002/j.1460-2075.1991.tb07689.x
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发表时间：
1991-07-01
期刊：
影响因子：
11.4
通讯作者：
GORDON, S
中科院分区：
文献类型：
--
作者：
CROCKER, PR;KELM, S;GORDON, S
小鼠的巨噬细胞亚群表达一种凝集素样受体-唾液酸粘附素(最初被称为绵羊红细胞受体，SER)，它选择性地识别唾液糖结合物，并可能参与造血和淋巴组织中基质巨噬细胞的细胞相互作用。在这篇报道中，我们描述了从小鼠脾中分离的唾液酸粘附素的纯化和配基特异性。纯化的唾液酸粘附素是一种185kd的糖蛋白，表观M(R)，以唾液酸依赖的方式以纳摩尔浓度凝集绵羊或人的红细胞。小角度阴影和电子显微镜显示，唾液粘附素由大约9 nm的球形头部区域和大约35 nm的延伸尾部组成。为了研究唾液酸的特异性，我们研究了唾液酸粘附素与衍生的人红细胞、糖蛋白和糖脂的相互作用。综上所述，唾液酸粘附素能特异性识别唾液酸糖蛋白或神经节苷脂中的寡糖序列Neu5Ac-α-2-->；3Gal-beta-1-->；3GalNAc。这些发现表明，携带这种结构的特定唾液酸糖结合物可能参与基质巨噬细胞与造血细胞和淋巴细胞亚群之间的细胞相互作用。
Macrophage subpopulations in the mouse express a lectin-like receptor, sialoadhesin (originally named sheep erythrocyte receptor, SER), which selectively recognizes sialoglycoconjugates and is likely to be involved in cellular interactions of stromal macrophages in haematopoietic and lymphoid tissues. In this report we describe the purification and ligand specificity of sialoadhesin isolated from mouse spleen. Purified sialoadhesin, a glycoprotein of 185 kd apparent M(r), agglutinated sheep or human erythrocytes at nanomolar concentrations in a sialic acid-dependent manner. Low angle shadowing and electron microscopy showed that sialoadhesin consisted of a globular head region of approximately 9 nm and an extended tail of approximately 35 nm. To investigate the specificity for sialic acid, we studied the interaction of sialoadhesin with derivatized human erythrocytes, glycoproteins, and glycolipids. In conclusion, sialoadhesin specifically recognizes the oligosaccharide sequence Neu5Ac-alpha-2 --> 3Gal-beta-1 --> 3GalNAc in either sialoglycoproteins or gangliosides. These findings imply that specific sialoglycoconjugates carrying this structure may be involved in cellular interactions between stromal macrophages and subpopulations of haematopoietic cells and lymphocytes.