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Regulation of 3β-Hydroxysteroid Dehydrogenase/∆5-∆4 Isomerase: A Review

Rasmussen, Martin Krøyer; Ekstrand, Bo and Zamaratskaia, Galia (2013) Regulation of 3β-Hydroxysteroid Dehydrogenase/∆5-∆4 Isomerase: A Review. International Journal of Molecular Sciences, 14, pp. 17926-17942.

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Summary

This review focuses on the expression and regulation of 3β-hydroxysteroi ddehydrogenase/Δ5-Δ4 isomerase (3β-HSD), with emphasis on the porcine version. 3β-HSD is often associated with steroidogenesis, but its function in the metabolism of both steroids and xenobiotics is more obscure. Based on currently available literature covering humans,rodents and pigs, this review provides an overview of the present knowledge concerning the regulatory mechanisms for 3β-HSD at all omic levels. The HSD isoenzymes are essential in steroid hormone metabolism, both in the synthesis and degradation of steroids.
They display tissue-specific expression and factors influencing their activity, which therefore indicates their tissue-specific responses. 3β-HSD is involved in the synthesis of a number of natural steroid hormones, including progesterone and testosterone, and the hepatic degradation of the pheromone androstenone. In general, a number of signaling and regulatory pathways have been demonstrated to influence 3β-HSD transcription and activity, e.g., JAK-STAT, LH/hCG, ERα, AR, SF-1 and PPARα. The expression and enzymic activity of 3β-HSD are also influenced by external factors, such as dietary composition. Much of the research conducted on porcine 3β-HSD is motivated by its importance for the occurrence of the boar taint phenomenon that results from high concentrations of steroids such as androstenone. This topic is also examined in this review.


EPrint Type:Journal paper
Keywords:hydroxysteroid dehydrogenase, pig, boar taint, expression, steroid hormones metabolism
Subjects: Animal husbandry > Feeding and growth
Animal husbandry > Breeding and genetics
Research affiliation: Denmark > Organic RDD 1 > NO-CAST
DOI:10.3390/ijms140917926
Deposited By: Madsen, Academic employee Mette Graves
ID Code:24792
Deposited On:04 Dec 2013 13:28
Last Modified:09 Apr 2015 10:17
Document Language:English
Status:Published
Refereed:Peer-reviewed and accepted

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