Molecular cloning and functions of rat liver hydroxysteroid sulfotransferases catalysing covalent binding of carcinogenic polycyclic arylmethanols to DNA
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Oxysterol sulfation by cytosolic sulfotransferase suppresses liver X receptor/sterol regulatory element binding protein-1c signaling pathway and reduces serum and hepatic lipids in mouse models of nonalcoholic fatty liver disease
2012, Metabolism: Clinical and ExperimentalCitation Excerpt :Whether these patients have lower expression of SULT2B1b or lower sulfated oxysterol levels is unknown and merits further investigation. Three SULT isoenzymes in human and 4 in rat have been cloned and identified [33-36]. He et al [37] reported that SULT2B1b has been localized to the cytosol and nuclei of both human cells and tissues.
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2004, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Additive effects of either stressor on DHEA sulfation activity were observed. The Western blot results of (rat)SULT1A1 (major protein for 2-naphthol sulfation in rat [50]) and (rat)SULT2A1 (major protein for DHEA sulfation [51,52]) and their densitometry analysis data are presented in Fig. 3. The densitometry data on (rat)SULT1A1 protein suggest that this protein amount did not change following treatment with either physical or chemical stress alone or in combination (Fig. 3A).
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