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
1993; Royal Society; Volume: 251; Issue: 1330 Linguagem: Inglês
10.1098/rspb.1993.0008
ISSN1471-2954
Autores Tópico(s)Invertebrate Immune Response Mechanisms
ResumoRestricted accessMoreSectionsView PDF ToolsAdd to favoritesDownload CitationsTrack Citations ShareShare onFacebookTwitterLinked InRedditEmail Cite this article Webster S. G. 1993High-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 maenusProc. R. Soc. Lond. B.25153–59http://doi.org/10.1098/rspb.1993.0008SectionRestricted accessArticleHigh-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 S. G. Webster Google Scholar Find this author on PubMed Search for more papers by this author S. G. Webster Google Scholar Find this author on PubMed Published:22 January 1993https://doi.org/10.1098/rspb.1993.0008AbstractReceptor-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.FootnotesThis text was harvested from a scanned image of the original document using optical character recognition (OCR) software. As such, it may contain errors. Please contact the Royal Society if you find an error you would like to see corrected. Mathematical notations produced through Infty OCR. 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