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首页> 外文期刊>Infection and immunity >Binding of lipopolysaccharide (LPS) to an 80-kilodalton membrane protein of human cells is mediated by soluble CD14 and LPS-binding protein.
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Binding of lipopolysaccharide (LPS) to an 80-kilodalton membrane protein of human cells is mediated by soluble CD14 and LPS-binding protein.

机译：脂多糖（LPS）与人细胞的80千膜蛋白的结合是由可溶性CD14和LPS结合蛋白介导的。

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Activation of cells by bacterial lipopolysaccharide (LPS) plays a key role in the pathogenesis of gram-negative septic shock. The 55-kDa glycoprotein CD14 is known to bind LPS and initiate cell activation. However, there must be additional LPS receptors because CD14 is linked by a glycosylphosphatidyl inositol anchor to the cell membrane and therefore unable to perform transmembrane signalling. Searching for potential LPS receptors, we investigated the binding of LPS to membrane proteins of the human monocytic cell line Mono-Mac-6. Membrane proteins were electrophoretically separated under reducing conditions, transferred to nitrocellulose, and exposed to LPS, which was visualized with anti-LPS antibody. Smooth- and rough-type LPS, as well as free lipid A, bound to a variety of proteins in the absence of serum. However, in the presence of serum, additional or preferential binding to a protein of approximately 80-kDa was observed. Experiments with differently acylated lipid A structures showed that the synthetic tetraacyl compound 406 was still able to bind, whereas no binding was detected with the bisacyl compound 606. The 80-kDa membrane protein was also detected on human peripheral blood monocytes and endothelial cells. The serum factors mediating the binding of lipid A to the 80-kDa membrane protein were identified as soluble CD14 and LPS-binding protein. From these results, we conclude that this 80-kDa protein is a candidate for the hypothetical molecule for LPS and/or LPS-CD14 recognition and signal transduction.
机译：细菌脂多糖（LPS）激活细胞在革兰氏阴性败血性休克的发病机理中起关键作用。已知55kDa糖蛋白CD14结合LPS并启动细胞活化。但是，必须有其他LPS受体，因为CD14通过糖基磷脂酰肌醇锚固剂连接到细胞膜上，因此无法执行跨膜信号传导。为了寻找潜在的LPS受体，我们研究了LPS与人单核细胞系Mono-Mac-6的膜蛋白的结合。在还原条件下电泳分离膜蛋白，将其转移到硝酸纤维素膜上，然后暴露于LPS，用抗LPS抗体将其可视化。在没有血清的情况下，平滑型和粗糙型LPS以及游离脂质A与多种蛋白质结合。然而，在血清存在下，观察到与约80kDa的蛋白质的额外或优先结合。用不同的酰化脂质A结构进行的实验表明，合成的四酰基化合物406仍然能够结合，而双酰基化合物606没有检测到结合。在人外周血单核细胞和内皮细胞上也检测到80 kDa的膜蛋白。介导脂质A与80 kDa膜蛋白结合的血清因子被鉴定为可溶性CD14和LPS结合蛋白。根据这些结果，我们得出结论，该80 kDa蛋白是LPS和/或LPS-CD14识别和信号转导的假设分子的候选者。

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