Highly conserved mouse and human brain sulfotransferases: molecular cloning, expression, and functional characterization

Sakakibara, Yoichi; Suiko, Masahito; Pai, Tongkun; Nakayama, Tatsuo; Yasuda, Takami; Katafuchi, Junko; Liu, Ming Cheh

doi:10.1016/s0378-1119(02)00431-6

Cited by 57 publications

(47 citation statements)

References 25 publications

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“…Figure 4 shows the regulation of Sult4a1 and 5a1 mRNA in male mice by MEIs. The basal expression of Sult4a1 mRNA was very low in livers of male mice, which is known (Sakakibara et al, 2002), and was not affected by any of the inducers. In contrast, Sult5a1 mRNA expression was induced by all AhR ligands (TCDD, PCB126, and BNF), one PXR ligand (PCN), and two Nrf2 activators (OPZ, EXQ).…”

Section: Resultsmentioning

confidence: 89%

Regulation of Sulfotransferase Enzymes by Prototypical Microsomal Enzyme Inducers in Mice

Alnouti

Klaassen

2007

J Pharmacol Exp Ther

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Section: Resultsmentioning

confidence: 89%

Regulation of Sulfotransferase Enzymes by Prototypical Microsomal Enzyme Inducers in Mice

Alnouti

Klaassen

2007

J Pharmacol Exp Ther

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“…Subfamily SULT2B is localized in human prostate, placenta, adrenal gland, ovary, lung, kidney and colon 49,50,52 . Human SULT4A1 has been identified in brain 54,55 and SULT6B1 in testis and kidney 56 .…”

mentioning

confidence: 99%

Phase Ii Drug Metabolizing Enzymes

Jančová¹,

Anzenbacher²,

Anzenbacherová³

2010

Biomed Pap Med Fac Univ Palacky Olomouc Czech Repub

467

347

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“…Three that belong to the SULT2 gene family are SULT2A1 (dehydroepiandrosterone sulfotransferase) (26,27), SULT2B1a (pregnenolone sulfotransferase) (28,29) and SULT2B1b (cholesterol sulfotransferase) (28,29). Finally, neuronal/brain sulfotransferase belongs to the SULT4 gene family (30,31).…”

mentioning

confidence: 99%

Sulfation of ractopamine and salbutamol by the human cytosolic sulfotransferases

Kurogi

Davidson

et al. 2012

Journal of Biochemistry

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-Cheh Liu *These two authors contributed equally to this study.Feed additives such as ractopamine and salbutamol are pharmacologically active compounds, acting primarily as b-adrenergic agonists. This study was designed to investigate whether the sulfation of ractopamine and salbutamol may occur under the metabolic conditions and to identify the human cytosolic sulfotransferases (SULTs) that are capable of sulfating two major feed additive compounds, ractopamine and salbutamol. A metabolic labelling study showed the generation and release of [ 35 S]sulfated ractopamine and salbutamol by HepG2 human hepatoma cells labelled with [ 35 S]sulfate in the presence of these two compounds. A systematic analysis using 11 purified human SULTs revealed SULT1A3 as the major SULT responsible for the sulfation of ractopamine and salbutamol. The pH dependence and kinetic parameters were analyzed. Moreover, the inhibitory effects of ractopamine and salbutamol on SULT1A3-mediated dopamine sulfation were investigated. Cytosol or S9 fractions of human lung, liver, kidney and small intestine were examined to verify the presence of ractopamine-/ salbutamol-sulfating activity in vivo. Of the four human organs, the small intestine displayed the highest activity towards both compounds. Collectively, these results imply that the sulfation mediated by SULT1A3 may play an important role in the metabolism and detoxification of ractopamine and salbutamol.

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Highly conserved mouse and human brain sulfotransferases: molecular cloning, expression, and functional characterization

Cited by 57 publications

References 25 publications

Regulation of Sulfotransferase Enzymes by Prototypical Microsomal Enzyme Inducers in Mice

Regulation of Sulfotransferase Enzymes by Prototypical Microsomal Enzyme Inducers in Mice

Phase Ii Drug Metabolizing Enzymes

Sulfation of ractopamine and salbutamol by the human cytosolic sulfotransferases

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