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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).
findings showed clearly the impact of genetic polymorphisms on the cholesterol-sulphating activity of SULT2B1b allozymes, which may underscore the differential metabolism of cholesterol in individuals with different SULT2B1b genotypes
Mutation in SULT2B1 leads to an autosomal-recessive congenital ichthyosis phenotype via increased proliferation of human keratinocytes, thickening of epithelial layers, and altered epidermal cholesterol metabolism.
Since 1'-hydroxyestragole exposure readily produced DNA injury in B-13/H cells, these data suggest that cholangiocarcinomas generated in rats fed estragole may be dependent, in part, on SULT2B1 activation of the 1'-hydroxyestragole metabolite.
It metabolizes breast cancer drugs like afimoxifene and endoxifen by sulfation.
Overexpression of SULT2B1b is an independent prognostic indicator and promotes cell growth and invasion in colorectal carcinoma.
This study identified specific germline variations in estradiol metabolism-related pathways, namely CYP1B1, SULT2B1, and HSD17B2, as novel prognostic markers that are cumulatively associated with increased risk of prostate cancer progression
The SULT2B1 isoforms have a unique 50 amino acid carboxy-terminal sequence that is not present in the other human SULT isoforms (review).
Data indicate that cholesterol sulfate (CS) and SULT2B1b inhibited gluconeogenesis by targeting the gluconeogenic factor hepatocyte nuclear factor 4alpha (HNF4alpha) in both cell cultures and human SULT2B1b transgenic mice.
SULT2B1 is induced by calcitriol activated vitamin D receptor in human prostate cancer cells.
SULT2B1b expression promotes proliferation of hepatocellular carcinoma cells in vitro and in vivo, which may contribute to the progression of HCC.
In HT29 cells expression of SULT2B1 was enhanced by probiotic fermentation supernatants without aleurone.
Sulfation of 25-hydroxycholesterol by SULT2B1b plays an important role in the maintenance of intracellular lipid homeostasis via the LXR/SREBP-1c signaling pathway in endothelial cells.
The Ca(2+)-bound form may be physiologically relevant for stressed cells with an elevated free calcium level.
The expression of SULT2B1b mRNA in endometrial stromal cells is induced by progesterone and that in endometrial epithelial cells is induced by relaxin via the cAMP pathway.
alternative splicing of SULT2B1 results in cholesterol sulfotransferase or pregnenolone sulfotransferase
crystal structure of hydroxysteroid sulfotransferases SULT2B1a and SULT2B1b bound to the substrate donor product 3'-phosphoadenosine 5'-phosphate and acceptor substrate pregnenolone revealed a different catalytic binding orientation
We have documented the presence of the enzyme (SULT2B1b) that sulfonates cholesterol in human platelets and examined the influence of plasma lipoproteins on the expression and activity of this enzyme
Differential subcellular localization of SULT2B1b in prostate and placenta suggests that SULT2B1b may be differentially regulated and have different physiological functions in these two hormonally responsive human tissues
confinement of SULT2B1b to the granular layer coincides with this being the area with the highest cholesterol sulfate content suggesting that the physiologic action of cholesterol sulfate is likely carried out in this region of the living epidermis
Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. The gene structure (number and length of exons) is similar among family members. This gene sulfates dehydroepiandrosterone but not 4-nitrophenol, a typical substrate for the phenol and estrogen sulfotransferase subfamilies. Two alternatively spliced variants that encode different isoforms have been described.
, alcohol sulfotransferase
, hydroxysteroid sulfotransferase 2
, sulfotransferase 2B1
, sulfotransferase family cytosolic 2B member 1
, sulfotransferase 2B
, sulfotransferase family, cytosolic, 2B, member 1
, cytosolic hydroxysteroid sulfotransferase 2b member 1