MOLECULAR-CLONING OF A HUMAN MACROPHAGE LECTIN SPECIFIC FOR GALACTOSE
MOLECULAR-CLONING OF A HUMAN MACROPHAGE LECTIN SPECIFIC FOR GALACTOSE
复制标题
DOI：
10.1073/pnas.87.18.7324
复制
发表时间：
1990-09-01
影响因子：
11.1
通讯作者：
PILLAI, S
中科院分区：
文献类型：
--
作者：
CHERAYIL, BJ;CHAITOVITZ, S;PILLAI, S
小鼠Mac-2蛋白是一种半乳糖和IgE结合的凝集素，由炎症巨噬细胞分泌。我们在这里描述了一个代表人的Mac-2同源基因(HMAC-2)的cDNA的克隆和鉴定。来自HMAC-2基因的氨基酸序列表明，该蛋白在进化上高度保守，其85%的氨基酸残基与小鼠的同源物相似。这种保守性在羧基末端的凝集素结构域中尤其明显。该蛋白的氨基末端部分不太保守，但仍然含有在小鼠蛋白中看到的重复的富含脯氨酸-甘氨酸的基序。体外合成的HMAC-2可被抗Mac-2的M3/38单抗识别，并与所需的糖蛋白asialofetuin和基底膜的主要成分层粘连蛋白结合。这些发现是在HMAC-2的潜在功能的背景下讨论的。
The murine Mac-2 protein is a galactose- and IgE-binding lectin secreted by inflammatory macrophages. We described here the cloning and characterization of a cDNA representing a human homolog of Mac-2 (hMac-2). The amino acid sequence derived from the hMac-2 cDNA indicates that the protein is evolutionarily highly conserved, with 85% of its amino acid residue being similar to those in the murine homolog. This conservation is especially marked in the carboxy-terminal lectin domain. The amino-terminal half of the protein is less conserved but stil contains the repetitive proline-glycine-rich motif seen in the mouse protein. hMac-2 synthesized in vitro is recognized by the M3/38 monoclonal antibody to Mac-2 and binds to the desialylated glycoprotein asialofetuin and to laminin, a major component of basement membranes. These findings are discussed in the context of the potentiaal functions of hMac-2.