Ecdysteroid 7,9(11)-dien-6-ones as potential photoaffinity labels for ecdysteroid binding proteins

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Abstract

Three ecdysteroid 7,9(11)-dien-7-ones (dacryhainansterone, 25-hydroxydacryhainansterone and kaladasterone) were prepared by dehydration of the corresponding 11a-hydroxy ecdysteroids (ajugasterone C, turkesterone and muristerone A, respectively). The biological activities of the dienones in the Drosophila melanogaster B _II cell bioassay, which reflect the affinity for the ecdysteroid receptor complex, showed that the dienones retain high biological activity. Irradiation at 350 nm of the ecdysteroid dienones (100 nM) with bacterially-expressed dipteran and lepidopteran ecdysteroid receptor proteins (DmEcR/DmUSP or CfEcR/CfUSP), followed by loading with [ ³H]ponasterone A revealed that irradiation of dacryhainansterone or kaladasterone resulted in blocking of >70% of the specific binding sites. Thus, ecdysteroid dienones show considerable potential as photoaffinity analogues for ecdysteroid binding proteins.

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Most cited references 44

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Functional ecdysone receptor is the product of EcR and Ultraspiracle genes.

J. Jiang, P Cherbas, T Yao … (1993)

Although the biological activity of the insect moulting hormone ecdysone, is manifested through a hormonally regulated transcriptional cascade associated with chromosomal puffing, a direct association of the receptor with the puff has yet to be established. The cloned ecdysone receptor (EcR) is by itself incapable of high-affinity DNA binding or transcriptional activation. Rather, these activities are dependent on heterodimer formation with Ultraspiracle (USP) the insect homologue of vertebrate retinoid X receptor. Here we report that native EcR and USP are co-localized on ecdysone-responsive loci of polytene chromosomes. Moreover, we show that natural ecdysones selectively promote physical association between EcR and USP, and conversely, that high-affinity hormone binding requires both EcR and USP. Replacement of USP with retinoid X receptor produces heterodimers with distinct pharmacological and functional properties. These results redefine the ecdysone receptor as a dynamic complex whose activity may be altered by combinatorial interactions among subunits and ligand.

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New insecticides with ecdysteroidal and juvenile hormone activity.

T S Dhadialla, G. Carlson, D Le (1998)

Agrochemical research over the last two decades has resulted in the discovery of chemically novel insecticides that mimic the action of the two insect growth and developmental hormones, the steroidal 20-hydroxyecdysone (20E) and the sesquiterpenoid juvenile hormone (JH). Bisacylhydrazines are non-steroidal agonists of 20E and exhibit their insecticidal activity via interaction with the ecdysteroid receptor proteins. Interestingly, two of the bisacylhydrazine (tebufenozide and RH-2485) insecticides are very selectively toxic to lepidopteran pests. These insecticides are safe to beneficial insects and have a benign ecotoxicological profile. Aromatic non-terpenoidal insecticides (fenoxycarb and pyriproxyfen) mimic the action of JHs. However, like the JHs, their exact mode of action is not well understood. These insecticides are toxic to a broad spectrum of insects during their embryonic, last larval, or reproductive stages. The insecticidal, ecotoxicological properties and the mode of action of the two groups of insecticides are reviewed in this article.

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The Drosophila EcR gene encodes an ecdysone receptor, a new member of the steroid receptor superfamily.

M. Koelle, W. S. Talbot, W Segraves … (1991)

The steroid hormone ecdysone triggers coordinate changes in Drosophila tissue development that result in metamorphosis. To advance our understanding of the genetic regulatory hierarchies controlling this tissue response, we have isolated and characterized a gene, EcR, for a new steroid receptor homolog and have shown that it encodes an ecdysone receptor. First, EcR protein binds active ecdysteroids and is antigenically indistinguishable from the ecdysone-binding protein previously observed in extracts of Drosophila cell lines and tissues. Second, EcR protein binds DNA with high specificity at ecdysone response elements. Third, ecdysone-responsive cultured cells express EcR, whereas ecdysone-resistant cells derived from them are deficient in EcR. Expression of EcR in such resistant cells by transfection restores their ability to respond to the hormone. As expected, EcR is nuclear and found in all ecdysone target tissues examined. Furthermore, the EcR gene is expressed at each developmental stage marked by a pulse of ecdysone.

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Author and article information

Journal

Journal ID (nlm-ta): J Insect Sci

Title: Journal of Insect Science

Publisher: University of Arizona Library

ISSN (Electronic): 1536-2442

Publication date Collection: 2002

Publication date (Electronic): 28 June 2002

Volume: 2

Electronic Location Identifier: 11

Affiliations

[1 ]Department of Biological Sciences, University of Exeter, Hatherly Laboratories, Prince of Wales Road, Exeter, Devon, EX4 4PS, U.K.

[2 ]Rohm & Haas Co., Research Laboratories, 727 Norristown Road, Spring House, PA 19477-0904, U.S.A

[3 ]Equipe de RMN et Modélisation Moléculaire, Université René Descartes, Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques, Unité Mixte de Recherche CNRS, UMR 8601, 45 rue des Saints-Pères, 75270 Paris Cedex 06, France

[4 ]Institute of Organic Chemistry and Biochemistry, Academy of Sciences, Flemingovo nám. 2, 166 10 Prague, Czech Republic.

[5 ]Laboratoire d'Endocrinolgie Moléculaire et Evolution, Université Pierre et Marie Curie, 7 Quai St. Bernard, 75252 Paris 05, France

[6 ]Current address: Biochemistry, Dow AgroSciences LLC, 9330 Zionsville Road, Indianapolis, IN 46268, U.S.A.

[7 ]Current address: RHeogene Inc., Research Labs., 727, Norristown Road, PO Box 949, Spring House, PA 19477-0904, U.S.A.

[8 ] L.N.Dinan@ 123456exeter.ac.uk

Article

PMC ID: 355911

PubMed ID: 15455045

SO-VID: e646c405-bdde-46bf-8542-4e686d6b8a37

History

Date received : 2 March 2002

Date accepted : 10 June 2002

Ecdysteroid 7,9(11)-dien-6-ones as potential photoaffinity labels for ecdysteroid binding proteins

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Abstract

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Vector Biology

Most cited references 44

Functional ecdysone receptor is the product of EcR and Ultraspiracle genes.

New insecticides with ecdysteroidal and juvenile hormone activity.

The Drosophila EcR gene encodes an ecdysone receptor, a new member of the steroid receptor superfamily.

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