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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Activation of erythropoietin receptor in the absence of hormone by a peptide that binds to a domain different from the hormone binding site
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Activation of erythropoietin receptor in the absence of hormone by a peptide that binds to a domain different from the hormone binding site

机译:在不存在激素的情况下,结合与不同于激素结合位点的域的肽激活促红细胞生成素受体

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摘要

Applying a homology search method previ- ously described, we identified a sequeuce in the extracellular dimerization site of the erythropoietin receptor, distant from the hormone binding site. A peptide identical to that sequence was synthesized. Remarkably, it activated receptor signaling in the absence of erythropoietin. Neither the peptide nor the hormone altered the affinity of the other for the receptor; thus, the peptide does not bind to the hormone binding site. The combined activation of signal transduction by hormone and peptide was strongly synergistic. In mice, the peptide acted like the hormone, protecting against the decrease in hemat- ocrit caused by carboplatin.
机译:应用先前描述的同源搜索方法,我们发现了促红细胞生成素受体的细胞外二聚化位点中离激素结合位点较远的一个隔离区。合成与该序列相同的肽。显着地,它在不存在促红细胞生成素的情况下激活受体信号传导。肽和激素都不会改变彼此对受体的亲和力。因此,该肽不结合激素结合位点。激素和肽对信号转导的联合激活具有强烈的协同作用。在小鼠中,该肽的作用类似于激素,可防止卡铂引起的血细胞比容降低。

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