Article ; Online: The Uptake and Deconjugation of Androstenone Sulfate in the Adipose Tissue of the Boar
Animals, Vol 11, Iss 3158, p
2021 Volume 3158
Abstract: Boars express high testicular levels of sulfotransferase enzymes, and consequently, the boar taint causing compound androstenone predominantly circulates as a steroid sulfate. Androstenone sulfate is suspected to function as a steroid reservoir that can ... ...
Abstract | Boars express high testicular levels of sulfotransferase enzymes, and consequently, the boar taint causing compound androstenone predominantly circulates as a steroid sulfate. Androstenone sulfate is suspected to function as a steroid reservoir that can be deconjugated to provide a source of free androstenone for accumulation. Therefore, the purpose of this study was to characterize the uptake and deconjugation of androstenone sulfate in the adipose tissue of the boar. Real-time PCR was used to quantify the expression of steroid sulfatase (STS) and several organic anion transporting polypeptides (OATPs) in the adipose tissue. Additionally, [ 3 H]-androstenone sulfate was incubated with adipocytes or supernatant from homogenized fat to assess steroid uptake and conversion, respectively. A positive correlation existed between OATP-B expression and androstenone sulfate uptake (r = 0.86, p = 0.03), as well as between STS expression and androstenone sulfate conversion (r = 0.76, p < 0.001). Moreover, fat androstenone concentrations were positively correlated (r = 0.85, p < 0.001) with androstenone sulfate conversion and tended to increase with STS expression in early maturing boars. This suggests that androstenone sulfate uptake and deconjugation are mediated by OATP-B and STS, respectively, which may influence the development of boar taint in early maturing animals. |
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Keywords | pig ; boar taint ; androstenone ; androstenone sulfate ; steroid uptake ; deconjugation ; Veterinary medicine ; SF600-1100 ; Zoology ; QL1-991 |
Subject code | 630 |
Language | English |
Publishing date | 2021-11-01T00:00:00Z |
Publisher | MDPI AG |
Document type | Article ; Online |
Database | BASE - Bielefeld Academic Search Engine (life sciences selection) |
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