Two categories of mammalian galactose-binding receptors distinguished by glycan array profiling.

Two categories of mammalian galactose-binding receptors distinguished by glycan array profiling.
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DOI:
10.1093/glycob/cwj126
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发表时间:
2006-08
期刊:
影响因子:
4.3
通讯作者:
Drickamer K
Drickamer K
中科院分区:
生物学3区
文献类型:
--
作者:
Coombs PJ;Taylor ME;Drickamer K

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Profiling of the four known galactose-binding receptors in the C-type lectin family has been undertaken in parallel on a glycan array. The results are generally consistent with previous assays using various different formats, but they provide a direct comparison of the properties of the four receptors, revealing that they fall into two distinct groups. The major subunit of the rat asialoglycoprotein receptor and the rat Kupffer cell receptor show similar broad preference for GalNAc-terminated glycans, while the rat macrophage galactose lectin and the human scavenger receptor C-type lectin bind more restricted sets of glycans. Both of these receptors bind to Lewisx-type structures, but the macrophage galactose lectin also interacts strongly with bi-antennary galactose- and GalNAc-terminated glycans. Although the similar glycan-binding profiles for the asialoglycoprotein receptor and the Kupffer cell receptor might suggest that these receptors are functionally redundant, analysis of fibroblasts transfected with full-length Kupffer cell receptor reveals that they fail to endocytose glycosylated ligand.
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