A functional soluble form of the murine mannose receptor is produced by macrophages in vitro and is present in mouse serum
A functional soluble form of the murine mannose receptor is produced by macrophages in vitro and is present in mouse serum
复制标题
DOI：
10.1074/jbc.273.36.23376
复制
发表时间：
1998-09-04
影响因子：
4.8
通讯作者：
Gordon, S
中科院分区：
文献类型：
--
作者：
Martínez-Pomares, L;Mahoney, JA;Gordon, S
在体外原代巨噬细胞的条件培养基和小鼠血清中发现了甘露糖受体（sMR）的可溶性形式，sMR作为单一物质释放，具有比细胞相关形式更小的尺寸，并以甘氨酸调节的方式在巨噬细胞条件培养基中积累至与细胞相关甘露糖受体相当的水平。脉冲追踪实验表明，sMR生产在文化中发生的组成性切割预先存在的全长蛋白质。开发了一种结合测定法，以确定sMR的糖特异性及其与病原体和颗粒抗原（即白色念珠菌和酵母聚糖）相互作用的能力。蛋白酶抑制剂的研究表明，sMR是由一个完整的甘露糖受体的基质金属蛋白酶或ADAM金属蛋白酶切割。sMR在免疫应答中的作用是基于其结合特性、细胞因子的调节以及先前在淋巴结和脾脏中甘露糖受体的富含半胱氨酸结构域的推定配体的发现而提出的。
A soluble form of the mannose receptor (sMR) has been found in conditioned medium of primary macrophages in vitro and in mouse serum, sMR was released as a single species, had a smaller size than the cell-associated form, and accumulated in macrophage-conditioned medium, in a cytokine-regulated manner, to levels comparable with those found for cell-associated mannose receptor. Pulse-chase experiments showed that sMR production in culture occurred by constitutive cleavage of pre-existing full-length protein. A binding assay was developed to determine the sugar specificity of sMR and its ability to interact with pathogens and particulate antigens (i.e. Candida albicans and zymosan). Protease inhibitor studies suggested that sMR was produced by cleavage of an intact mannose receptor by a matrix metalloprotease or ADAM metalloprotease. A role for sMR in the immune response is proposed based on its binding properties, regulation by cytokines, and the previous discovery of putative ligands for the cysteine-rich domain of the mannose receptor in lymph nodes and spleen.