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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 activation.
activation of PXR 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
during embryonic development, SULT2B1a produces pregnenolone sulfate, an essential neurosteroid during development of the central nervous system.
and Sult2a1 participate in an integrated pathway mediating elimination of sulfated steroid and bile acid metabolites from the liver
decreased levels or activities of farnesoid X receptor, pregnane X receptor, and constitutive androstane receptor 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 metabolites in the livers of 4-month- and 20-month-old mice.
Energy-dependent scoring of docking solutions identified the interaction as specific for the PAPSS2 and SULT2A1 isoforms
Kinetic analyses showed further differential catalytic efficiency and substrate affinity of the SULT2A1 allozymes, in comparison with wild-type SULT2A1. These findings provided useful information concerning the effects of genetic polymorphisms on the sulfating activity of SULT2A1 allozymes.
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
A theoretical study at the level of density functional theory (DFT) was performed to characterize noncovalent intermolecular interactions, especially hydrogen bond interactions, in the active site of enzyme human androsterone sulphotransferase.
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 activation, a phenomenon which is not noted in PBC, and may account for the impaired hepatoprotection in PSC.
It metabolizes breast cancer drugs like afinoxifene and endoxifen by sulfation.
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
molecular dynamic simulations were used to investigate the effect of ligands (cofactor and substrate) on the thermo-denaturation process of hSULT2A1
results established human SULT2A1 as a novel LXRalpha target gene; the expression of LXRalpha 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/beta-catenin signaling was activated, while inactivating Wnt/beta-catenin signaling enhanced the effects of DHEA
The complete kinetic mechanism of human SULT2A1.
Fetal inflammatory response syndrome and funisitis are associated with an elevation of umbilical cord plasma concentrations of soluble sulfotransferase (ST)2.
Depression following hip fracture with poor long term recovery is associated with a higher serum cortisol:DHEAS ratio.
Genetic variants in SULT2A1 do not predispose to polycystic ovary syndrome. Although a variant in SULT2A1 decreased the DHEAS to DHEA ratio, no changes in other androgenic hormone levels were observed.
formation of disulfide bonds in hSULT2A1 is a potentially important reversible mechanism for alterations in the rates of sulfation of both endogenous and xenobiotic substrates
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