cDNA cloning and primary structure analysis of C1qR(p), the human C1q/MBL/SPA receptor that mediates enhanced phagocytosis in vitro
cDNA cloning and primary structure analysis of C1qR(p), the human C1q/MBL/SPA receptor that mediates enhanced phagocytosis in vitro
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DOI：
10.1016/s1074-7613(00)80419-7
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发表时间：
1997-02-01
期刊：
影响因子：
32.4
通讯作者：
Tenner, AJ
中科院分区：
文献类型：
--
作者：
Nepomuceno, RR;HenschenEdman, AH;Tenner, AJ
补体蛋白C1 q、甘露糖结合凝集素（MEL）和肺表面活性蛋白A（SPA）是结构相似的分子，可增强体外吞噬功能。单克隆抗体R3和R139抑制由这三种配体引发的增强，用于纯化126，000 M-r细胞表面蛋白，命名为C1 qR（p）。获得氨基酸序列并克隆相应的cDNA。C1 qR（p）是一种新型的I型膜蛋白，具有以下结构元件：一个C型糖识别结构域、五个EGF样结构域、一个跨膜结构域和一个短的胞质尾区。通过氨基酸测序鉴定的所有肽均由cDNA编码。此外，产生了抗肽抗血清，其与C1 qR（p）反应。这些数据表明，克隆的cDNA编码的受体，在C1 q/MBL/SPA介导的清除或破坏的病原体和免疫复合物的吞噬作用中发挥作用。
The complement protein C1q, mannose-binding lectin (MEL), and pulmonary surfactant protein A (SPA) are structurally similar molecules that enhance phagocytic function in vitro. Monoclonal antibodies R3 and R139, which inhibit the enhancement triggered by these three ligands, were used to purify a 126,000 M-r cell surface protein designated C1qR(p). Amino acid sequence was obtained and the corresponding cDNA was cloned. C1qR(p) is a novel type I membrane protein with the following putative structural elements: a C-type carbohydrate recognition domain, five EGF-like domains, a transmembrane domain, and a short cytoplasmic tail. All peptides identified by amino acid sequencing are encoded by the cDNA. Additionally, an anti-peptide antiserum was generated, which is reactive with C1qR(p). The data indicate that the cloned cDNA encodes the receptor that plays a role in C1q/MBL/SPA-mediated removal or destruction of pathogens and immune complexes by phagocytosis.