HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in ISI Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via ISI Web of Science (11) Citing Articles via Google Scholar Google Scholar Articles by Mindnich, R Articles by Adamski, J Search for Related Content PubMed PubMed Citation Articles by Mindnich, R Articles by Adamski, J

GSF-National Research Center for Environment and Health, Institute of Experimental Genetics, Genome Analysis Center, Ingolstaedter Landstr. 1, 85764 Neuherberg, Germany

(Requests for offprints should be addressed to J Adamski; Email: adamski{at}gsf.de)

Formation and inactivation of testosterone is performed by various members of the 17ß-hydroxysteroid dehydrogenase (17ß-HSD) family. The main player in testosterone formation is considered to be 17ß-HSD type 3, which catalyzes the reduction of androstenedione to testosterone with high efficiency and is almost exclusively expressed in testis. So far, only the mammalian homologs have been characterized but nothing is known about the role of 17ß-HSD type 3 in other vertebrates. In this study, we describe the identification and characterization of the zebrafish homolog. We found zebrafish 17ß-HSD type 3 to be expressed in embryogenesis from sphere to 84 h post-fertilization. Expression was also detected in various tissues of both male and female adults, but displayed sexual dimorphism. Interestingly, expression was not highest in male testis but in male liver. In female adults, strongest expression was observed in ovaries. At the subcellular level, both human and zebrafish 17ß-HSD type 3 localize to the endoplasmic reticulum. The zebrafish enzyme in vitro effectively catalyzed the conversion of androstenedione to testosterone by use of NADPH as cofactor. Among further tested androgens epiandrosterone and dehydroepiandrosterone were accepted as substrates and reduced at C-17 by the human and the zebrafish enzyme. Androsterone and androstanedione though, were only substrates of human 17ß-HSD type 3, not the zebrafish enzyme. Furthermore, we found that both enzymes can reduce 11-ketoandrostenedione as well as 11ß-hydroxyandrostenedione at C-17 to the respective testosterone forms. Our results suggest that 17ß-HSD type 3 might play slightly different roles in zebrafish compared with human although testosterone itself is likely to have similar functions in both organisms.

This article has been cited by other articles:

				J. L. Vingren, W. J. Kraemer, D. L. Hatfield, J. M. Anderson, J. S. Volek, N. A. Ratamess, G. A. Thomas, J.-Y. Ho, M. S. Fragala, and C. M. Maresh Effect of resistance exercise on muscle steroidogenesis J Appl Physiol, December 1, 2008; 105(6): 1754 - 1760. [Abstract] [Full Text] [PDF]

				P P de Waal, D S Wang, W A Nijenhuis, R W Schulz, and J Bogerd Functional characterization and expression analysis of the androgen receptor in zebrafish (Danio rerio) testis Reproduction, August 1, 2008; 136(2): 225 - 234. [Abstract] [Full Text] [PDF]