The hepcidin-binding site on ferroportin is evolutionarily conserved.
The hepcidin-binding site on ferroportin is evolutionarily conserved.
复制标题
铁蛋白上的肝素结合位点在进化上是保守的。
DOI：
10.1016/j.cmet.2008.07.002
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发表时间：
2008-08
期刊：
影响因子：
29
通讯作者：
Kaplan J
中科院分区：
文献类型：
--
作者：
De Domenico I;Nemeth E;Nelson JM;Phillips JD;Ajioka RS;Kay MS;Kushner JP;Ganz T;Ward DM;Kaplan J
Mammalian iron homeostasis is regulated by the interaction of the liver-produced peptide hepcidin and its receptor, the iron transporter ferroportin. Hepcidin binds to ferroportin resulting in degradation of ferroportin and decreased cellular iron export. We identify the hepcidin-binding domain (HBD) on ferroportin and show that a synthetic 19 amino acid peptide corresponding to the HBD recapitulates the characteristics and specificity of hepcidin binding to cell surface ferroportin. The binding of mammalian hepcidin to ferroportin or the HBD shows an unusual temperature dependency with an increased rate of dissociation at temperatures below 15°C. The increased rate of dissociation is due to temperature dependent changes in hepcidin structure. In contrast, hepcidin from poikilothermic vertebrates, such as fish or frogs, binds the HBD in a temperature independent fashion. The affinity of hepcidin for the HBD permits a rapid, sensitive assay of hepcidin from all species and yields insights into the evolution of hepcidin.
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影响因子：
4.8
作者：
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通讯作者：
Westerman, ME
影响因子：
20.3
作者：
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Townsend, ARM
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2.3
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29
作者：
Donovan, A;Lima, CA;Andrews, NC
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作者：
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通讯作者：
Verghese, Bindhu