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Zebrafish 17β-hydroxysteroid dehydrogenases: An evolutionary perspective.
Mol. Cell. Endocrinol. 301, (Sp. Iss. SI), 20-26 (2009)
The term 17beta-hydroxysteroid dehydrogenase (17beta-HSD) describes an enzyme that stereospeciflcally reduces or oxidizes a keto- or hydroxy group at C17 of the steroid scaffold, respectively. Fourteen mammalian 17beta-HSDs have been identified so far and nine sequence homologs are found in zebrafish. 17beta-HSDs additionally active in fatty acid metabolism display high sequence conservation and widespread tissue expression. Homologs of these multifunctional 17beta-HSDs have been identified in flies, worms and yeast, and steroid-converting activity was demonstrated in some cases. The "classical" 17beta-HSDs, types 1, 2 and 3, are steroid-specific enzymes expressed in few tissues. They may have arisen at the beginning of vertebrate evolution allowing new, differently controlled modes of steroid hormone action. These findings reflect on two aspects: (1) the evolutionary origin of steroid-specific enzymes and (2) a possible conservation of steroid hormone function in invertebrates through currently unknown mechanisms.
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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
17beta-hydroxysteroid dehydrogenase (17beta-HSD); Steroids; Fatty acids; Zebrafish; Evolution; human 17-beta-hydroxysteroid dehydrogenases; major histocompatibility complex; coenzyme-a dehydrogenase; fatty-acid elongase; breast-cancer; 3-ketosteroid reductase; caenorhabditis-elegans; tissue distribution; estrogen-receptor; molecular-cloning
ISSN (print) / ISBN
0303-7207
e-ISSN
1872-8057
Zeitschrift
Molecular and Cellular Endocrinology
Quellenangaben
Band: 301,
Heft: 1-2,
Seiten: 20-26,
Supplement: (Sp. Iss. SI)
Verlag
Elsevier
Verlagsort
Shannon
Begutachtungsstatus
Peer reviewed
Institut(e)
Molekulare Endokrinologie und Metabolismus (MEM)