Siglec-8 - A novel eosinophil-specific member of the immunoglobulin superfamily
Siglec-8 - A novel eosinophil-specific member of the immunoglobulin superfamily
复制标题
DOI：
10.1074/jbc.275.2.861
复制
发表时间：
2000-01-14
影响因子：
4.8
通讯作者：
Crocker, PR
中科院分区：
文献类型：
--
作者：
Floyd, H;Ni, J;Crocker, PR
我们描述了siglec-8，一种新的唾液酸结合免疫球蛋白样凝集素，是由嗜酸性粒细胞特异性表达的表征。从人嗜酸性粒细胞cDNA文库中分离出编码siglec-8的全长cDNA。预测Siglec-8含有三个细胞外免疫球蛋白样结构域、跨膜区和47个氨基酸的胞质尾区。siglec-8基因定位于染色体19q13.33-41，与编码CD 33（siglec-3）、siglec-5、siglec-6和siglec-7的基因紧密连锁。当siglec-8在COS细胞上表达或作为与人IgG Fc区融合的重组蛋白表达时（1），它能够介导与人红细胞和可溶性唾液酸糖缀合物的唾液酸依赖性结合。使用特异性单克隆抗体，siglec-8只能在嗜酸性粒细胞上检测到，因此似乎是嗜酸性粒细胞特异性跨膜受体的第一个例子。
We describe the characterization of siglec-8, a novel sialic acid-binding immunoglobulin-like lectin that is expressed specifically by eosinophils. A full-length cDNA encoding siglec-8 was isolated from a human eosinophil cDNA library. Siglec-8 is predicted to contain three extracellular immunoglobulin-like domains, a transmembrane region, and a cytoplasmic tail of 47 amino acids. The siglec-8 gene mapped on chromosome 19q13.33-41, closely linked to genes encoding CD33 (siglec-3), siglec-5, siglec-6, and siglec-7. When siglec-8 was expressed on COS cells or as a recombinant protein fused to the Fc region of human IgG(1), it was able to mediate sialic acid-dependent binding to human erythrocytes and to soluble sialoglycoconjugates. Using specific monoclonal antibodies, siglec-8 could be detected only on eosinophils and hence appears to be the first example of an eosinophil-specific transmembrane receptor.