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hyposulfatemia leads to hepatic phosphoadenosine-5'-phosphosulfate depletion, which causes loss of SULT2A1 activity and results in accumulation of nonsulfated bile acids and activated farnesoid X receptor (show xpr1 Proteins) activation.
activation of PXR (show NR1I2 Proteins) increases the activity and gene expression of the phase II conjugating enzyme dehydroepiandrosterone sulfotransferase (STD)
hydroxysteroid sulfotransferase has a protective role in lithocholic acid-induced liver toxicity
and Sult2a1 participate in an integrated pathway mediating elimination of sulfated (show SULF1 Proteins) steroid and bile acid metabolites from the liver
decreased levels or activities of farnesoid X receptor (show xpr1 Proteins), pregnane X receptor (show NR1I2 Proteins), and constitutive androstane receptor (show NR1I3 Proteins) during the acute-phase response could contribute to decreases in Sult2A1, resulting in decreased sulfation of DHEA
Increased Sult2A1 expression appears to be an adaptive response to ensure optimal metabolism of Sult2A1 substrates at old age.
Sult2A1 converts bile acids, steroids and a number of drugs to the corresponding sulfated (show SULF1 Proteins) metabolites in the livers of 4-month- and 20-month-old mice.
Polymorphisms of SULT2A1 gene is not associated with attention-deficit/hyperactivity disorder.
Galeterone and abiraterone are novel inhibitors of DHEA sulfonation, as determined in enzymatic incubations containing human tissue cytosol (liver or intestinal) or human recombinant SULT enzyme (SULT2A1, SULT2B1b, or SULT1E1).
nine human SULT2A1 allozymes plus the wild-type SULT2A1 were found to display differential sulfating activity toward DHEA and tibolone. Kinetic analysis revealed that different SULT2A1 allozymes exhibited differential substrate affinity and catalytic efficiency toward the two substrates tested.
Mass spectrometry analysis and structural modeling supported a reaction mechanism which involves the isomerization of Delta(4)-3-ketosteroids from the keto form to an enol form, prior to being subjected to sulfation. Results derived from this study suggested a potential role of SULT2A1 as a Delta(4)-3-ketosteroid sulfotransferase in steroid metabolism
Decreased SULT2A1 activity was found in the adrenal zona reticularis in Alzheimer's disease patients.
PSC is characterized by disease-specific impairment of SULT2A1 expression following PXR (show NR1I2 Proteins) activation, a phenomenon which is not noted in PBC (show DLAT Proteins), and may account for the impaired hepatoprotection in PSC.
The substrate, such as lithocholic acid (LCA), participated in regulating the structure and flexibility of sulfotransferase actively rather than merely being selected passively.
Our results show that SULT2A1 is important in the first trimester; particularly in the adrenals
results established human SULT2A1 as a novel LXRalpha (show NR1H3 Proteins) target gene; the expression of LXRalpha (show NR1H3 Proteins) is a potential predictor for the expression of SULT2A1 in human liver
It turns out the protective effect of DHEA was significantly decreased when Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) signaling was activated, while inactivating Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) signaling enhanced the effects of DHEA
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.
sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone-preferring, member 1
, sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA)-preferring, member 1
, alcohol sulfotransferase
, bile salt sulfotransferase 1
, hydroxysteroid sulfotransferase
, sulfotransferase 2A1
, sulfotransferase, DHEA preferring
, sulfotransferase, hydroxysteroid preferring 1
, bile salt sulfotransferase
, bile-salt sulfotransferase 2A1
, hydroxysteroid sulfotransferase a
, sulfotransferase family, cytosolic, 2A, dehydroepiandrosterone (DHEA) -preferring, member 1
, sulfotransferase hydroxysteroid gene 2
, sulfotransferase, hydroxysteroid preferring 2
, alcohol/hydroxysteroid sulfotransferase
, bile-salt sulfotranasferase 2A1