High-affinity binding of putative moult-inhibiting hormone (MIH) and crustacean hyperglycaemic hormone (CHH) to membrane-bound receptors on the Y-organ of the shore crab Carcinus maenus
High-affinity binding of putative moult-inhibiting hormone (MIH) and crustacean hyperglycaemic hormone (CHH) to membrane-bound receptors on the Y-organ of the shore crab Carcinus maenus
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DOI：
10.1098/rspb.1993.0008
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发表时间：
1993-01
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影响因子：
--
通讯作者：
S. Webster
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文献类型：
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作者：
S. Webster
应用受体结合分析法研究了蜕皮抑制激素（MIH）和甲壳类高血激素（CHH）受体在真鲷（Carcinus maenus）组织膜上的分布和特征。在Y器官制备物上观察到高亲和力、特异性、可置换和可饱和的[125 I]MIH结合，表明受体-配体相互作用。检查的所有组织，包括Y器官特异性结合的[125 I]CHH，并且对于该组织，通过Scatchard分析确定高亲和力结合特征。由于以前的研究表明，CHH是积极的抑制蜕皮激素的生物合成的Y-器官在体外，有人认为，这种神经肽具有生理作用，在蜕皮控制，进一步加强了新兴的情况下，一个复杂的，多激素控制蜕皮。使用来自Necora和Cancer的异源MIHs的受体结合实验显示，所有这些MIHs在置换同源（Carcinus）放射性配体方面同样有效，这一特征反映在它们有点相似的生物活性中。然而，所有三个MIH可以区分色谱和免疫化学行为和氨基酸分析的方式与进化关系内的短尾亚目。因此，这表明MIHs的结合结构域是高度保守的。
Receptor-binding assays for putative moult-inhibiting hormone (MIH) and crustacean hyperglycaemic hormone (CHH) were developed to determine the distribution and characteristics of their receptors on crude membrane preparations of Carcinus maenus tissues. High-affinity, specific, displaceable and saturable binding of [125I]MIH indicative of receptor—ligand interaction was observed on Y-organ preparations. All tissues examined including the Y-organ specifically bound [125I]CHH, and, for this tissue, high-affinity binding characteristics were determined by Scatchard analysis. As previous studies had shown that CHH is active in repressing ecdysteroid biosynthesis by Y-organs in vitro, it is argued that this neuropeptide has a physiological role in moult control, further strengthening the emerging scenario of a complex, multihormonal control of moulting. Receptor binding experiments using heterologous MIHs from Necora and Cancer revealed that all these MIHs were similarly effective at displacing homologous (Carcinus) radioligand, a feature reflected in their somewhat similar biological activities. Nevertheless, all three MIHs could be distinguished in terms of chromatographic and immunochemical behaviour and in terms of amino acid analysis in a manner correlated with evolutionary relationships within the Brachyura. It is therefore suggested that binding domains of MIHs have been highly conserved.