{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,3]],"date-time":"2026-08-03T10:10:28Z","timestamp":1785751828785,"version":"3.56.0"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1996,12,1]]},"abstract":"<jats:p>Although the involvement of 3-oxo-\u03944 compounds as intermediates in arthropod ecdysteroid biosynthesis has been postulated for a long time, it has not yet been directly demonstrated. In the present study, 3-oxo-\u03944-steroids have been synthesized and incubated in vitro with dissociated moulting gland cells from the crab Carcinus maenas. The tritiated compounds were converted into 3-dehydroecdysone, ecdysone and\/or 25-deoxyecdysone, i.e. final ecdysteroids. This means that the 3-oxo-\u03944 compounds had undergone a 5\u03b2-reduction, to give the 5\u03b2-conformation of ecdysteroids. Our results suggest that the 3-oxo-\u03944-steroid 4,7-cholestadien-14\u03b1-ol-3,6-dione may be an intermediate in the biosynthetic pathway. The 5\u03b2-reduction reaction involves a cytosolic enzyme which requires NADPH as electron donor and seems specific for 3-oxo-\u03944 substrates. This reaction was the most active in crab Y-organs, as compared with other tissues. The characteristics of the 5\u03b2-reductase (subcellular localization, substrate and cofactor requirements) appear similar to those of the vertebrate 3-oxo-\u03944-steroid 5\u03b2-reductase involved in steroid hormone catabolism and bile acid biosynthesis.<\/jats:p>","DOI":"10.1042\/bj3200413","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T21:51:59Z","timestamp":1439243519000},"page":"413-419","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":35,"title":["Evidence for the involvement of 3-oxo-\u03944 intermediates in ecdysteroid biosynthesis"],"prefix":"10.1042","volume":"320","author":[{"given":"Catherine","family":"BLAIS","sequence":"first","affiliation":[{"name":"Ecole Normale Sup\u00e9rieure, Laboratoire de Biochimie, CNRS EP 119, 46 rue d'Ulm, F-75230 Paris cedex 05, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chantal","family":"DAUPHIN-VILLEMANT","sequence":"additional","affiliation":[{"name":"Ecole Normale Sup\u00e9rieure, Laboratoire de Biochimie, CNRS EP 119, 46 rue d'Ulm, F-75230 Paris cedex 05, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nikolay","family":"KOVGANKO","sequence":"additional","affiliation":[{"name":"Ecole Normale Sup\u00e9rieure, Laboratoire de Biochimie, CNRS EP 119, 46 rue d'Ulm, F-75230 Paris cedex 05, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean-Pierre","family":"GIRAULT","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Ren\u00e9 Descartes, Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques, CNRS URA 400, 45 rue des Saints-P\u00e8res, F-75006 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"suffix":"Jr.","given":"Charles","family":"DESCOINS","sequence":"additional","affiliation":[{"name":"Ecole Normale Sup\u00e9rieure, Laboratoire de Biochimie, CNRS EP 119, 46 rue d'Ulm, F-75230 Paris cedex 05, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ren\u00e9","family":"LAFONT","sequence":"additional","affiliation":[{"name":"Ecole Normale Sup\u00e9rieure, Laboratoire de Biochimie, CNRS EP 119, 46 rue d'Ulm, F-75230 Paris cedex 05, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/320\/2\/413\/623119\/bj3200413.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/320\/2\/413\/623119\/bj3200413.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,24]],"date-time":"2021-11-24T01:06:42Z","timestamp":1637716002000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/320\/2\/413\/37935\/Evidence-for-the-involvement-of-3-oxo-4"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1996,12,1]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1996,12,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj3200413","relation":{},"ISSN":["0264-6021","1470-8728"],"issn-type":[{"value":"0264-6021","type":"print"},{"value":"1470-8728","type":"electronic"}],"subject":[],"published":{"date-parts":[[1996,12,1]]}}}