Sulphation requirement for GlyCAM-1, an endothelial ligand for L-selectin
Sulphation requirement for GlyCAM-1, an endothelial ligand for L-selectin
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DOI：
10.1038/361555a0
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发表时间：
1993-02
期刊：
影响因子：
64.8
通讯作者：
Y. Lmai;L. Lasky;S. Rosen
中科院分区：
文献类型：
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作者：
Y. Lmai;L. Lasky;S. Rosen
L-选择素参与白细胞与血管内皮的初始附着1 -3。在淋巴细胞上，介导与淋巴结高内皮微静脉的结合。作为一种选择素4 - 6，它作为一种钙依赖性凝集素7，8识别内皮细胞上的碳水化合物配体9 -11。L-选择素的两种淋巴结配体已被鉴定为Mr 50 K和Mr 90 K的硫酸化糖蛋白，称为SgpSO和Sgp 90（参考文献10）。最近克隆的SgpSO（参考文献12），现在命名为GlyCAM-1，是一种高内皮微静脉相关的粘蛋白样糖蛋白，主要含有O-连接的糖链。GlyCAM-1的唾液酸化是其配体活性所必需的9，10，13，并且怀疑岩藻糖基化的作用13。我们使用氯酸盐作为硫酸化的代谢抑制剂，并在这里报告GlyCAM-1对硫酸盐有额外的需求。
L-SELECTIN participates in the initial attachment of leukocytes to the vascular endothelium1–3. On lymphocytes, it mediates binding to high endothelial venules of lymph nodes. As a selectin4–6it functions as a calcium-dependent lectin7,8recognizing carbohydrate-bearing ligands on endothelial cells9–11. Two lymph node ligands for L-selectin have been identified as sulphated glycoproteins of Mr∼50K and ∼90K, called SgpSO and Sgp90 (ref. 10). The recently cloned SgpSO (ref. 12), now designated GlyCAM-1, is a high endothelial venule-associated, mucin-like glycoprotein containing predominantly O-linked carbohydrate chains. Sialylation of GlyCAM-1 is necessary for its ligand activity9,10,13and a role for fucosylation is suspected13. We have used chlorate as a metabolic inhibitor of sulphation, and report here that GlyCAM-1 has an additional requirement for sulphate.