1976
DOI: 10.1016/0005-2744(76)90287-4
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Studies on a 3β3-hydroxysteroid sulphotransferase from rat liver

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Cited by 32 publications
(4 citation statements)
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“…The developmental pattern of 3f3-hydroxy-5cholenoate sulfotransferase activity was similar to hepatic phenol and hydroxysteroid sulfotransferase activities in the rat (30)(31)(32). The sex-related differences in activities in mature rats were more pronounced for 3f3-hydroxy-5-cholenoate than glycolithocholate in this study, because of the differences in relative activities of BSS I and II.…”
Section: Discussionsupporting
confidence: 67%
“…The developmental pattern of 3f3-hydroxy-5cholenoate sulfotransferase activity was similar to hepatic phenol and hydroxysteroid sulfotransferase activities in the rat (30)(31)(32). The sex-related differences in activities in mature rats were more pronounced for 3f3-hydroxy-5-cholenoate than glycolithocholate in this study, because of the differences in relative activities of BSS I and II.…”
Section: Discussionsupporting
confidence: 67%
“…The enzyme hydroxysteroid sulfotransferase (HST) mediates the conversion of DHEA to DHEA-S and it is dependent upon sulfation and glutathione and is inhibited by inflammation Carrol 1976, Kim et al 2004). In addition, neurotoxicant exposures were revealed to significantly reduce HST function and in-crease androgen and testosterone levels (Ryan and Carrol 1976, Freeman et al 1977, Veltman et al 1986, Barregard et al 1994. The end result is that a cyclical pattern of continuous interaction between the androgen and transsulfuration pathways can be set into motion following neurotoxicant exposures that may increase susceptibility to neurotoxicity, particularly among developing males (Geier and Geier 2005).…”
Section: Why Males Might Be More Vulnerablementioning
confidence: 99%
“…It is at the DHEA location in the androgen synthesis pathway that, DHEA can either be converted further down the androgen pathway towards testosterone by being converted to androstenedione or androstenediol, or towards the normally favored storage molecule of DHEA-sulfate (DHEA-S). In examining the conversion step of DHEA to DHEA-S by the enzyme, hydroxysteroid sulfotransferase, this enzyme requires glutathione as a co-factor [9]. Since, some children with ASDs have significant decreases in their total glutathione levels and active reduced glutathione, and a significant increase in their inactive oxidized glutathione, there may be a marked shift toward DHEA, and subsequent metabolites in the androgen synthesis pathway.…”
Section: Discussionmentioning
confidence: 99%