Identification and characterization of a novel human collectin CL-K1
Identification and characterization of a novel human collectin CL-K1
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DOI：
10.1111/j.1348-0421.2006.tb03868.x
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发表时间：
2006-01-01
影响因子：
2.6
通讯作者：
Wakamiya, Nobutaka
中科院分区：
文献类型：
--
作者：
Keshi, Hiroyuki;Sakamoto, Takashi;Wakamiya, Nobutaka
凝集素是C型凝集素家族的一员，具有两种特征性结构，胶原样结构域和碳水化合物识别结构域。它们识别微生物上的碳水化合物抗原并作为宿主防御。在这里，我们报告了一个新的聚集素CL-K1的克隆和表征。RT-PCR分析表明，CL-K1 mRNA存在于所有器官中。推导的氨基酸序列和来自表达CL-K1 cDNA的CHO细胞的免疫染色的数据揭示CL-K1作为分泌蛋白表达。通过免疫印迹和部分氨基酸分析在血液中发现CL-K1。CL-K1显示了岩藻糖和弱甘露糖的Ca 2+依赖性糖结合活性，但不显示N-乙酰半乳糖胺、N-乙酰葡萄糖胺或麦芽糖，尽管甘露糖结合凝集素（MBL）含有类似的氨基酸基序。由于CL-K1具有特异的糖结合特性，它能特异性地识别多种细菌。阐明CL-K1和CL-L1两个祖先聚集蛋白的作用有助于了解聚集蛋白家族的生物学功能。
Collectins are a family of C-type lectins with two characteristic structures, collagen like domains and carbohydrate recognition domains. They recognize carbohydrate antigens on microorganisms and act as host-defense. Here we report the cloning and characterization of a novel collectin CL-K1. RT-PCR analyses showed CL-K1 mRNA is present in all organs. The deduced amino acid sequence and the data from immunostaining of CL-K1 cDNA expressing CHO cells revealed that CL-K1 is expressed as a secreted protein. CL-K1 is found in blood by immunoblotting and partial amino acid analyses. CL-K1 showed Ca2+-dependent sugar binding activity of fucose and weakly mannose but not N-acetyl-galactosamine, N-acetyl-glucosamine, or maltose, though mannose-binding lectin (MBL) containing similar amino acid motif. CL-K1 can recognize specially several bacterial saccharides due to specific sugar-binding, character. Elucidation of the role of two ancestor collectins of CL-K1 and CL-L1 could lead to see the biological function of collectin family.