The macrophage endothelial cell mannose receptor cDNA encodes a protein that binds oligosaccharides terminating with SO4-4-GalNAc beta 1,4GlcNAc beta or Man at independent sites
The macrophage endothelial cell mannose receptor cDNA encodes a protein that binds oligosaccharides terminating with SO4-4-GalNAc beta 1,4GlcNAc beta or Man at independent sites
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DOI：
10.1073/pnas.94.21.11256
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发表时间：
1997-10-14
影响因子：
11.1
通讯作者：
Baenziger, JU
中科院分区：
文献类型：
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作者：
Fiete, D;Beranek, MC;Baenziger, JU
促黄体生成素（LH）和其他带有末端序列为SO 4 -4-GalNAc β 1，4GlcNAc β 1，4 Man-（S4 GGnM）的寡糖的糖蛋白通过S4 GGnM特异性受体从循环中迅速清除（S4 GGnM-R）在肝内皮细胞表面表达，从大鼠肝脏分离的S4 GGnM-R在抗原性和结构上与从大鼠肺分离的巨噬细胞甘露糖特异性受体（Man-R）密切相关，然而，从这些组织中分离的S4 GGnM-R和Man-R在它们结合带有末端GalNAc-3-SO 4或Man的配体的能力上是不同的。我们通过检测重组Man-1的性质，探索了Man-R和S4 GGnM-R之间的结构关系。R以跨膜蛋白和可溶性嵌合融合蛋白的形式存在，其中跨膜和胞质结构域已被人IgG 1的Fc区取代。与从肝脏分离的S4 GGnM-R一样，嵌合融合蛋白能够在独立位点结合以GalNAc-4-SO 4和Man终止的配体。当在CHO细胞中表达的重组Man-R是能够介导的终端GalNAc-4-SO 4或终端的人轴承配体的摄取。我们建议，Man-R被重命名为Man/S4 GGnM受体的基础上，其多个和独立的特异性。
Lutropin (LH) and other glycoproteins bearing oligosaccharides with the terminal sequence SO4-4-GalNAc beta 1,4GlcNAc beta 1,4Man- (S4GGnM) are rapidly removed from the circulation by an S4GGnM-specific receptor (S4GGnM-R) expressed at the surface of hepatic endothelial cells, The S4GGnM-R isolated from rat liver is closely related to the macrophage mannose-specific receptor (Man-R) isolated from rat lung both antigenically and structurally, The S4GGnM-R and Man-R isolated from these tissues nonetheless differ in their ability to bind ligands bearing terminal GalNAc-3-SO4 or Man. In this paper, we have explored the structural relationship between the Man-R and the S4GGnM-R by examining the properties of the recombinant Man-R in the form of a transmembrane protein and a soluble chimeric fusion protein in which the transmembrane and cytosolic domains have been replaced by the Fc region of human IgG1. Like the S4GGnM-R isolated from liver, the chimeric fusion protein is able to bind ligands terminating with GalNAc-4-SO4 and Man at independent sites. When expressed in CHO cells the recombinant Man-R is able to mediate the uptake of ligands bearing either terminal GalNAc-4-SO4 or terminal Man. We propose that the Man-R be renamed the Man/S4GGnM receptor on the basis of its multiple and independent specificities.