Prolectin, a glycan-binding receptor on dividing B cells in germinal centers.
Prolectin, a glycan-binding receptor on dividing B cells in germinal centers.
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DOI：
10.1074/jbc.m109.012807
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发表时间：
2009-07-03
期刊：
影响因子：
--
通讯作者：
Drickamer K
中科院分区：
文献类型：
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作者：
Graham SA;Jégouzo SA;Yan S;Powlesland AS;Brady JP;Taylor ME;Drickamer K
蛋白凝集素是一种以前未描述的聚糖结合受体，已通过重新筛选人类基因组中编码含有潜在C型碳水化合物识别结构域的蛋白质的基因而鉴定。聚糖阵列分析显示，受体胞外结构域中的碳水化合物识别结构域与末端α-连接甘露糖或岩藻糖残基的聚糖结合。在成纤维细胞中表达的蛋白凝集素存在于细胞表面，但与许多聚糖结合受体不同，它不介导新糖蛋白配体的内吞作用。然而，与其他已知的聚糖结合受体相比，该受体包含一个异常大的细胞内结构域，该结构域由多个序列基序组成，包括磷酸化酪氨酸残基，使其能够与信号分子如Grb 2相互作用。免疫组织化学已被用于证明，在生殖中心的增殖B细胞的一个专门的人口上表达的前凝集素。因此，这种新的受体具有在生发中心的细胞之间的碳水化合物介导的通信中发挥作用的潜力。
Prolectin, a previously undescribed glycan-binding receptor, has been identified by re-screening of the human genome for genes encoding proteins containing potential C-type carbohydrate-recognition domains. Glycan array analysis revealed that the carbohydrate-recognition domain in the extracellular domain of the receptor binds glycans with terminal α-linked mannose or fucose residues. Prolectin expressed in fibroblasts is found at the cell surface, but unlike many glycan-binding receptors it does not mediate endocytosis of a neoglycoprotein ligand. However, compared with other known glycan-binding receptors, the receptor contains an unusually large intracellular domain that consists of multiple sequence motifs, including phosphorylated tyrosine residues, that allow it to interact with signaling molecules such as Grb2. Immunohistochemistry has been used to demonstrate that prolectin is expressed on a specialized population of proliferating B cells in germinal centers. Thus, this novel receptor has the potential to function in carbohydrate-mediated communication between cells in the germinal center.