A novel, high endothelial venule-specific sulfotransferase expresses 6-sulfo sialyl Lewisx, an L-selectin ligand displayed by CD34
A novel, high endothelial venule-specific sulfotransferase expresses 6-sulfo sialyl Lewisx, an L-selectin ligand displayed by CD34
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DOI：
10.1016/s1074-7613(00)80083-7
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发表时间：
1999-07-01
期刊：
影响因子：
32.4
通讯作者：
Fukuda, M
中科院分区：
文献类型：
--
作者：
Hiraoka, N;Petryniak, B;Fukuda, M
L-选择素通过促进淋巴细胞与表达在次级淋巴器官高内皮微静脉上的独特碳水化合物配体-硫酸唾液酸路易斯(X)的黏附来介导淋巴细胞归巢。促成这种L-选择素受体硫酸盐化的磺基转移酶(S)的性质一直不确定。在这里，我们描述了一种新的L-选择素配体磺基转移酶，称为LSST，它指导L-选择素受体CD34，GlyCAM-1和MAdCAM-1上6-磺基唾液酸基Lewis(X)的合成。LSST主要在HEV中表达，与天然的L-选择素受体一样，LSST对核心2分支粘蛋白O-糖链具有明显的催化选择性。与非硫酸盐对照相比，LSST可增强剪切条件下L-选择素介导的粘附性。因此，LSST对应于HEV特异性的磺基转移酶，该酶有助于淋巴细胞归巢所需的L-选择素配体的生物合成。
L-selectin mediates lymphocyte homing by facilitating lymphocyte adhesion to unique carbohydrate ligands, sulfated sialyl Lewis(x), which are expressed on high endothelial venules (HEV) in secondary lymphoid organs. The nature of the sulfotransferase(s) that contribute to sulfation of such L-selectin counterreceptors has been uncertain. We herein describe a novel L-selectin ligand sulfotransferase, termed LSST, that directs the synthesis of the 6-sulfo sialyl Lewis(x) on L-selectin counterreceptors CD34, GlyCAM-1, and MAdCAM-1. LSST is predominantly expressed in HEV and exhibits striking catalytic preference for core 2-branched mucin-type O-glycans as found in natural L-selectin counterreceptors. LSST enhances L-selectin-mediated adhesion under shear compared to nonsulfated controls. LSST therefore corresponds to an HEV-specific sulfotransferase that contributes to the biosynthesis of L-selectin ligands required for lymphocyte homing.