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Sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone

SULT2A1, dehydroepiandrosterone sulfotransferase, hydroxysteroid sulfotransferase, DHEA-ST
This gene encodes a member of the sulfotransferase family. Sulfotransferases aid in the metabolism of drugs and endogenous compounds by converting these substances into more hydrophilic water-soluble sulfate conjugates that can be easily excreted. This protein catalyzes the sulfation of steroids and bile acids in the liver and adrenal glands, and may have a role in the inherited adrenal androgen excess in women with polycystic ovary syndrome. [provided by RefSeq, Mar 2010] (from NCBI)
Top mentioned proteins: ACID, HAD, CAN, PstI, estrogen sulfotransferase
Papers on SULT2A1
Identification of Human Sulfotransferases involved in Lorcaserin N-Sulfamate Formation.
Chen et al., Nieder-Ingelheim, Germany. In Drug Metab Dispos, Feb 2016
Human sulfotransferases (SULTs) SULT1A1, SULT1A2, SULT1E1 and SULT2A1 are involved in the formation of lorcaserin N-sulfamate.
Fast and sensitive quantification of human liver cytosolic lithocholic acid sulfation using ultra-high performance liquid chromatography-tandem mass spectrometry.
Lau et al., Singapore, Singapore. In J Chromatogr B Analyt Technol Biomed Life Sci, Feb 2016
UNASSIGNED: Detoxification of lithocholic acid (LCA) to lithocholic acid sulfate (LCA-S) is catalyzed by sulfotransferases, mainly SULT2A1.
Human liver cytosolic sulfotransferase 2A1-dependent dehydroepiandrosterone sulfation assay by ultra-high performance liquid chromatography-tandem mass spectrometry.
Lau et al., Singapore, Singapore. In J Pharm Biomed Anal, Jan 2016
UNASSIGNED: Sulfotransferase 2A1 (SULT2A1) is a major catalyst of the sulfation of dehydroepiandrosterone (DHEA) to dehydroepiandrosterone sulfate (DHEA-S) in human liver cytosol.
Preliminary evidence of altered steroidogenesis in women with Alzheimer's disease: Have the patients "OLDER" adrenal zona reticularis?
Stárka et al., Praha, Czech Republic. In J Steroid Biochem Mol Biol, Jan 2016
The steroid levels (47 steroids and steroid polar conjugates) and their ratios in AD female patients indicated increased CYP11A1 activity, weakened activity of the CYP17A1C17,20 lyase metabolic step and attenuated sulfotransferase SULT2A1 activity at higher activity of the CYP17A1 17-hydroxylase step.
Human sulfotransferases enhance the cytotoxicity of tolvaptan.
Beland et al., United States. In Toxicol Sci, Jan 2016
The affinity of individual SULT isozymes, as determined by Km analysis, was SULT1C3 ≫ SULT2A1 > SULT2B1 ~ SULT1B1 > SULT1E1.
The Design and Interpretation of Human SULT1A1 Assays.
Leyh et al., In Drug Metab Dispos, Jan 2016
The basic kinetic mechanism of these enzymes, previously thought to be ordered, has been redefined as random for SULT2A1, a representative member of the superfamily.
The First-in-Class Potassium-Competitive Acid Blocker, Vonoprazan Fumarate: Pharmacokinetic and Pharmacodynamic Considerations.
Echizen, Tokyo, Japan. In Clin Pharmacokinet, Oct 2015
Vonoprazan is metabolized to inactive metabolites mainly by cytochrome P450 (CYP)3A4 and to some extent by CYP2B6, CYP2C19, CYP2D6, and SULT2A1.
Fibrates and cholestasis.
Boyer et al., New Haven, United States. In Hepatology, Aug 2015
One of these NRs is peroxisome proliferator-activated receptor alpha (PPARα), which plays a central role in maintaining cholesterol, lipid, and bile acid homeostasis by regulating genes responsible for bile acid synthesis and transport in humans, including cytochrome P450 (CYP) isoform 7A1 (CYP7A1), CYP27A1, CYP8B1, uridine 5'-diphospho-glucuronosyltransferase 1A1, 1A3, 1A4, 1A6, hydroxysteroid sulfotransferase enzyme 2A1, multidrug resistance protein 3, and apical sodium-dependent bile salt transporter.
Genetics of neuroendocrine factors in rheumatoid arthritis.
Imrich et al., Bratislava, Slovakia. In Horm Metab Res, Jun 2015
Recently, several new gene variants have been identified in association with serum DHEAS concentrations, such as in SULT2A1 and HHEX genes.
[In vitro characterization of glucuronosyl- and sulfotransferases involved in the conjugation of ethanol].
Skopp et al., In Arch Kriminol, 2015
Inhibition was reversible and competitive for most enzymes; mechanism-based inhibition was evident for UGT2B7 and SULT2A1 with regard to quercetin and for SULT1E1 with regard to kaempferol.
Reduced sulfotransferase SULT2A1 activity in patients with Alzheimer´s disease.
Bendlová et al., Praha, Czech Republic. In Physiol Res, 2014
In the present study we evaluate the role of steroid sulfotransferase SULT2A1 in the pathophysiology of AD on the basis of circulating steroids (measured by GC-MS), in which the sulfation catalyzed by SULT2A1 dominates over glucuronidation (pregnenolone/sulfate, DHEA/sulfate, androstenediol/sulfate and 5alpha-reduced pregnane and androstane catabolites).
Liver Expression of Sulphotransferase 2A1 Enzyme Is Impaired in Patients with Primary Sclerosing Cholangitis: Lack of the Response to Enhanced Expression of PXR.
Milkiewicz et al., Szczecin, Poland. In J Immunol Res, 2014
BACKGROUND/AIM: Sulphotransferase 2A1 (SULT2A1) exerts hepatoprotective effects.
Interactions of cytosolic sulfotransferases with xenobiotics.
Ambadapadi et al., Gainesville, United States. In Drug Metab Rev, 2013
The human cytosolic sulfotransferases that have been most studied, namely SULT1A1, SULT1A3, SULT1B1, SULT1E1 and SULT2A1, are expressed in different tissues of the body, including liver, intestine, adrenal, brain and skin.
SULT2B1: unique properties and characteristics of a hydroxysteroid sulfotransferase family.
Rohn-Glowacki et al., Birmingham, United States. In Drug Metab Rev, 2013
Although human SULT2B1b displays significant substrate cross-reactivity with SULT2A1, the isoforms have different tissue expression patterns.
Polymorphisms of POR, SULT2A1 and HSD11B1 in children with premature adrenarche.
Voutilainen et al., Kuopio, Finland. In Metabolism, 2012
Common polymorphisms at POR, SULT2A1 or HSD11B1 were not associated with PA in a Finnish Caucasian population.
Estrogen-related receptor ERRα-mediated downregulation of human hydroxysteroid sulfotransferase (SULT2A1) in Hep G2 cells.
Chen et al., Stillwater, United States. In Chem Biol Interact, 2011
Hydroxysteroid sulfotransferase SULT2A1 is suppressed by the estrogen related receptor alpha
Serum dehydroepiandrosterone sulphate levels in patients with non-alcoholic fatty liver disease.
Kasayama et al., Itami, Japan. In Intern Med, 2010
Serum DHEAS levels are increased in patients with non-alcoholic fatty liver disease with elevated alanine aminotransferase levels.
Kinetic analysis of bile acid sulfation by stably expressed human sulfotransferase 2A1 (SULT2A1).
Alnouti et al., Omaha, United States. In Xenobiotica, 2010
The sulfation kinetics of dehydroepiandrosterone and 15 human bile acids by SULT2A1, was characterized.
Selective role of sulfotransferase 2A1 (SULT2A1) in the N-sulfoconjugation of quinolone drugs in humans.
Yamazoe et al., Sendai, Japan. In Drug Metab Dispos, 2009
Demonstrate that hSULT2A1 is responsible for the N-sulfation of quinolones and possibly other therapeutic drugs in humans.
Inactivating PAPSS2 mutations in a patient with premature pubarche.
Arlt et al., Nijmegen, Netherlands. In N Engl J Med, 2009
Dehydroepiandrosterone (DHEA) sulfotransferase, known as SULT2A1, converts the androgen precursor DHEA to its inactive sulfate ester, DHEAS [corrected], thereby preventing the conversion of DHEA to an active androgen.
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