{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T17:17:07Z","timestamp":1790788627218,"version":"4.1.0"},"reference-count":0,"publisher":"Bioscientifica","issue":"3","content-domain":{"domain":["journals.bioscientifica.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1999,6,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Six types of human 17beta-hydroxysteroid dehydrogenases catalyzing the conversion of estrogens and androgens at position C17 have been identified so far. The peroxisomal 17beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD 4, gene name HSD17B4) catalyzes the oxidation of estradiol with high preference over the reduction of estrone. The highest levels of 17beta-HSD 4 mRNA transcription and specific activity are found in liver and kidney followed by ovary and testes. A 3 kb mRNA codes for an 80 kDa (737 amino acids) protein featuring domains which are not present in the other 17beta-HSDs. The N-terminal domain of 17beta-HSD 4 reveals only 25% amino acid similarity with the other types of 17beta-HSDs. The 80 kDa protein is N-terminally cleaved to a 32 kDa enzymatically active fragment. Both the 80 kDa and the N-terminal 32 kDa (amino acids 1-323) protein are able to perform the dehydrogenase reaction not only with steroids at the C17 position but also with D-3-hydroxyacyl-coenzyme A (CoA). The enzyme is not active with L-stereoisomers. The central part of the 80 kDa protein (amino acids 324-596) catalyzes the 2-enoyl-acyl-CoA hydratase reaction with high efficiency. The C-terminal part of the 80 kDa protein (amino acids 597-737) facilitates the transfer of 7-dehydrocholesterol and phosphatidylcholine between membranes in vitro. The HSD17B4 gene is stimulated by progesterone, and ligands of PPARalpha (peroxisomal proliferator activated receptor alpha) such as clofibrate, and is down-regulated by phorbol esters. Mutations in the HSD17B4 lead to a fatal form of Zellweger syndrome.<\/jats:p>","DOI":"10.1677\/jme.0.0220227","type":"journal-article","created":{"date-parts":[[2004,12,2]],"date-time":"2004-12-02T18:43:59Z","timestamp":1102013039000},"page":"227-240","update-policy":"https:\/\/doi.org\/10.1530\/crossmarkpolicy-6","source":"Crossref","is-referenced-by-count":69,"title":["Unique multifunctional HSD17B4 gene product: 17beta-hydroxysteroid dehydrogenase 4 and D-3-hydroxyacyl-coenzyme A dehydrogenase\/hydratase involved in Zellweger syndrome"],"prefix":"10.1530","volume":"22","author":[{"given":"Y","family":"de Launoit","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J","family":"Adamski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"416","container-title":["Journal of Molecular Endocrinology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/jme.bioscientifica.com\/view\/journals\/jme\/22\/3\/227.xml","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/journals.bioscientifica.com\/jme\/article-pdf\/22\/3\/227\/188940\/227.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/journals.bioscientifica.com\/jme\/article-pdf\/22\/3\/227\/188940\/227.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,7,8]],"date-time":"2026-07-08T15:39:47Z","timestamp":1783525187000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.bioscientifica.com\/jme\/article\/22\/3\/227\/34170\/Unique-multifunctional-HSD17B4-gene-product-17beta"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1999,6,1]]},"references-count":0,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1999,6,1]]}},"URL":"https:\/\/doi.org\/10.1677\/jme.0.0220227","relation":{},"ISSN":["1479-6813","0952-5041"],"issn-type":[{"value":"1479-6813","type":"electronic"},{"value":"0952-5041","type":"print"}],"subject":[],"published":{"date-parts":[[1999,6,1]]}}}