J. Anim Sci.
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J. Anim. Sci. 2005. 83:358-365
© 2005 American Society of Animal Science


ANIMAL GROWTH, PHYSIOLOGY, AND REPRODUCTION

Testicular sulfoconjugation of the 16-androstene steroids by hydroxysteroid sulfotransferase: Its effect on the concentrations of 5{alpha}-androstenone in plasma and fat of the mature domestic boar1

P. A. Sinclair and E. J. Squires2

Department of Animal and Poultry Science, University of Guelph, Guelph, Ontario, Canada, N1G 2W1

2 Correspondence—phone: 519-824-4120 (ext. 53928); fax: 519-836-9873; e-mail: jsquires{at}uoguelph.ca.

This study examined the relationship between sulfoconjugation and the degree to which 5{alpha}-androstenone can accumulate in fat. Analysis of the unconjugated and sulfoconjugated fractions of peripheral plasma from 25 mature Yorkshire boars and testicular vein plasma from an additional 20 mature Yorkshire boars revealed that the majority of 5{alpha}-androsten-one is present as a sulfoconjugate, reaching levels up to 69 ± 4.3 and 72 ± 6.2%, respectively, relative to its unconjugated form. The presence of this steroid in the sulfoconjugate fraction was confirmed by gas chromatography-mass spectrometry. Plasma concentrations of 5{alpha}-androstenone in the sulfoconjugate fraction were negatively correlated (r = –0.36; P < 0.01) with the concentrations of 5{alpha}-androstenone in fat. High concentrations of 5{alpha}-androstenone in the sulfate fraction were only associated with animals that had fat androstenone concentrations < 0.5 µg/g. In addition, there was a positive correlation (r = 0.31; P < 0.01) between the concentrations of unconjugated 5{alpha}-androstenone in plasma and 5{alpha}-androstenone in fat. These findings indicate that the levels of the sulfoconjugated form present in the peripheral plasma influence the accumulation of 5{alpha}-androstenone in fat. The specific sulfotransferase enzyme involved in sulfoconjugating these steroids was identified by incubating Leydig cells with specific sulfotransferase inhibitors for 8 h. It was discovered that the enzyme responsible for the sulfoconjugation of the 16-androstene steroids is hydroxysteroid sulfotransferase. Hydroxysteroid sulfotransferase may play a significant role in determining the levels of sulfated 16-androstene steroids present in plasma. The results of this study indicate that sulfoconjugation may serve to regulate the quantity of unconjugated 5{alpha}-androstenone present in the circulation and thus available for accumulation. Animals with a decreased ability to sulfoconjugate 5{alpha}-androstenone would have a subsequent increase in the levels of unconjugated 5{alpha}-androstenone in circulation, allowing for the accumulation of high levels in fat and thereby potentially leading to the development of boar taint.

Key Words: Androstenone • Boar Taint • Sulfoconjugation • Sulfotransferase




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J ANIM SCIHome page
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