Molecular characterization of the human macrophage mannose receptor: demonstration of multiple carbohydrate recognition-like domains and phagocytosis of yeasts in Cos-1 cells.
Molecular characterization of the human macrophage mannose receptor: demonstration of multiple carbohydrate recognition-like domains and phagocytosis of yeasts in Cos-1 cells.
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DOI：
10.1084/jem.172.6.1785
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发表时间：
1990-12-01
期刊：
影响因子：
--
通讯作者：
Warner A
中科院分区：
文献类型：
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作者：
Ezekowitz RA;Sastry K;Bailly P;Warner A
巨噬细胞甘露糖受体是一种表达于组织巨噬细胞表面的整体膜蛋白。在连接富含甘露糖的糖缀合物或病原体后，受体介导巨噬细胞对结合的配体的内吞和吞噬。甘露糖受体的dna衍生初级结构预测了富含半胱氨酸的nh2末端结构域，随后是纤维连接蛋白II型区域。外结构域的其余部分由八个碳水化合物识别样结构域组成，随后是跨膜区域和细胞质尾部。将甘露糖受体cDNA转染到cos - 1细胞中是富含甘露糖缀合物的受体介导的内吞作用和酵母的吞噬作用所必需的。细胞质尾部的缺失导致受体突变，该受体能够结合但不能摄取结扎的病原体，这表明吞噬信号包含在细胞质尾部。
The macrophage mannose receptor is an integral membrane protein expressed on the surface of tissue macrophages. After ligation of mannose-rich glycoconjugates or pathogens, the receptor mediates endocytosis and phagocytosis of the bound ligands by macrophages. The cDNA-derived primary structure of the mannose receptor predicts a cysteine-rich NH2-terminal domain, followed by a fibronectin type II region. The remainder of the ectodomain is comprised of eight carbohydrate recognition-like domains, followed by a transmembrane region, and a cytoplasmic tail. Transfection of the mannose receptor cDNA into Cos-I cells is necessary for receptor-mediated endocytosis of mannose-rich glycoconjugate as well as phagocytosis of yeasts. Deletion of the cytoplasmic tail results in a mutant receptor that is able to bind but not ingest the ligated pathogens, suggesting that the signal for phagocytosis is contained in the cytoplasmic tail.