Document Detail

Regulation of the cytosolic sulfotransferases by nuclear receptors.
MedLine Citation:
PMID:  23330539     Owner:  NLM     Status:  MEDLINE    
The cytosolic sulfotransferases (SULTs) are a multigene family of enzymes that catalyze the transfer of a sulfonate group from the physiologic sulfate donor, 3'-phosphoadenosine-5'-phosphosulfate, to a nucleophilic substrate to generate a polar product that is more amenable to elimination from the body. As catalysts of both xenobiotic and endogenous metabolism, the SULTs are major points of contact between the external and physiological environments, and modulation of SULT-catalyzed metabolism can not only affect xenobiotic disposition, but it can also alter endogenous metabolic processes. Therefore, it is not surprising that SULT expression is regulated by numerous members of the nuclear receptor (NR) superfamily that function as sensors of xenobiotics as well as endogenous molecules, such as fatty acids, bile acids, and oxysterols. These NRs include the peroxisome proliferator-activated receptors, pregnane X receptor, constitutive androstane receptor, vitamin D receptor, liver X receptors, farnesoid X receptor, retinoid-related orphan receptors, and estrogen-related receptors. This review summarizes current information about NR regulation of SULT expression. Because species differences in SULT subfamily composition and tissue-, sex-, development-, and inducer-dependent regulation are prominent, these differences will be emphasized throughout the review. In addition, because of the central role of the SULTs in cellular physiology, the effect of NR-mediated SULT regulation on physiological and pathophysiological processes will be discussed. Gaps in current knowledge that require further investigation are also highlighted.
Melissa Runge-Morris; Thomas A Kocarek; Charles N Falany
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Publication Detail:
Type:  Journal Article; Review    
Journal Detail:
Title:  Drug metabolism reviews     Volume:  45     ISSN:  1097-9883     ISO Abbreviation:  Drug Metab. Rev.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-01-21     Completed Date:  2013-07-16     Revised Date:  2013-12-04    
Medline Journal Info:
Nlm Unique ID:  0322067     Medline TA:  Drug Metab Rev     Country:  England    
Other Details:
Languages:  eng     Pagination:  15-33     Citation Subset:  IM    
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MeSH Terms
Cytosol / enzymology,  metabolism*
Receptors, Cytoplasmic and Nuclear / genetics,  metabolism*
Sulfotransferases / genetics,  metabolism*
Xenobiotics / pharmacokinetics
Grant Support
Reg. No./Substance:
0/Receptors, Cytoplasmic and Nuclear; 0/Xenobiotics; EC 2.8.2.-/Sulfotransferases

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