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These results suggest that the availability of estrogens in the boar epididymis may be locally controlled also by steroid sulphatase and estrogen sulphotransferase.
SULTE1 expression in the ovaries of the cyclic cows.
These results resolve the conflicting results on the localization of SULT1E1 from earlier studies and suggest that posttranscriptional mechanisms play an important role in the control of SULT1E1 expression during TGC differentiation.
the activities of free estrogens produced in bovine TGC are curtailed by SULT1E1 expressed in UTC and in fetal liver
Our study shows that estrogen sulfotransferase is present in both the intracellular and intraluminal compartments of the epididymis, suggesting that this enzyme plays different roles along the excurrent duct.
results suggest that bmST1 plays a role in detoxification of xanthurenic acid in the silkworm
Increased expression of SULT1E1 is associated with obstructive cholestasis.
A crucial adipose- and male-specific role of Est in maintaining the whole-body energy homeostasis.
Gene profiling identifies sulfotransferase family 1E (Sult1e1), which encodes a sulfotransferase E1 responsible for inactivation of estrogen, as a gene upregulated in non-alcoholic steatohepatitis in both genders and most conspicuously in male IkbkbDeltahep mice having worst non-alcoholic steatohepatitis and lowest plasma estradiol levels.
The role of estrogen sulfotransferase, a conjugating enzyme that sulfonates and deactivates estrogens, in sepsis response is reported.
Liver ischemia and reperfusion (I/R) induced the expression of EST and comprised estrogen activity in an Nrf2-dependent manner. EST ablation gender-specifically affected I/R sensitivity.
EST functions as a negative regulator of adipogenesis.
Murine SULT1E1 inhibition in vitro and in silico was investigated and compared this to data for the human enzyme.
maintaining the functional integrity of the epididymis by regulating luminal estrogen homeostasis.
results suggest that estrogen sulfotransferase plays a physiologic role in protecting Leydig cells from estrogen-induced biochemical lesions
Data show that ablation of the mouse estrogen sulfotransferase gene Sult1e1 causes placental thrombosis and spontaneous fetal loss.
estrogen sulfotransferase, the enzyme that inactivates estrogen, has been found selectively expressed in male tissues, thus suggesting a role for this enzyme to protect male-specific tissues against estrogenic activity
Elevated SULT1E1 levels and associated alterations in estrogen-regulated hepatic protein expression may play an important role in cystic fibrosis liver disease
The role of SULT1E1 in ovulation is suggested by the substantially low ovulatory response in hCG-treated SULT1E1 KO mice
EST is expressed in adipose tissues in a sexually dimorphic manner, is regulated by testosterone, and plays a physiological role in regulating adipose tissue accumulation in male mice.
The enhanced SULT1E1 activity may have a role in inhibiting GH-stimulated STAT5b phosphorylation and IGF-1 synthesis via the sulfation and inactivation of E2.
Data show that SULT1E1 expression in HepG2 cells is inducible by sterol mediated liver-X-receptor (LXR) activation.
CYP19A1 mRNA levels were lower in endometrial cancer (EC) than in controls. A novel highly sensitive and accurate protocol to assess SULT1E1 activity is presented. STS enzyme activity and the STS:SULT1E1 activity ratio seem to be lower in ECs than in controls. STS is an important route for estrogen supply in endometrial cells.
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).
Single nucleotide polymorphisms in SULT1E1 were significantly associated with time to treatment failure in men on abiraterone acetate therapy. The single nucleotide polymorphisms may serve as predictive markers for treatment with abiraterone acetate.
Resveratrol and all its derivatives reduced also SULT1E1 mRNA transcript level. The reduced expression of AhR, CYP1A1, and 1B1 was also found as a result of treatment with these compounds.
Data show that both estrogen sulfatase (STS) and estrogen sulfotransferase (EST) were highly expressed in the human umbilical vein
Effects of steroid hormone on estrogen sulfotransferase and on steroid sulfatase expression in endometriosis tissue and stromal cells
a model that enables prediction of substrates and inhibitors of SULT1E1, is reported.
It metabolizes breast cancer drugs like afimoxifene and endoxifen by sulfation.
Data suggest that the substrate specificities of SULT1E1 and SULT1A1*1 include metabolites of tamoxifen (endoxifen, 4-hydroxytamoxifen, and N-desmethyltamoxifen); these metabolites are weak inhibitors of sulfation of estradiol by SULT1E1/SULT1A1*1.
Authors propose that the formation of this DNA loop and protein-bound complex prevents additional binding of ETS1 and p53 R273H proteins to other proximal binding sites.
Data indicate that protein-ligand interaction energy by using docking Quantitative Structure-Activity Relationships(QSAR) models showed accuracy of 67.28%, 78.00% and 75.46%, for the isoforms SULT1A1, SULT1A3 and SULT1E1, respectively.
Overexpression of EST promoted adipogenesis.
Report diterpenoid extracts from Leonurus sibiricus L. with estrogen sulfotransferase inhibitory activity.
Knock-down of SULT1E1 in HUVECs resulted in regulation of genes involved in inflammation and lipid metabolism.
Decrease or deletion of EST in the mammary gland may be related to the development of hypertrophic breast, especially gland-associated hypertrophic breast.
study showed expression patterns of SULT1E1 and PAPSS in breast and endometrial tissues; the estrogen sulfation enzymes were comparatively higher in the tumorous tissues than adjacent normal tissues; overexpression of SULT1E1 and PAPSS1 retarded MCF-7 cells growth in vivo and in vitro by arresting cell cycles and inducing apoptosis
Using two iterative rounds of evolution, we generated SULT1E1 mutants with increased thermostability.
results demonstrate that SULT1E1 expression in MCF10A breast epithelial cells cells is transcriptionally regulated by confluence through a suppressive action of the AhR, which is not mediated through a dioxin response element at nt -3476
Identification of the upstream enhancer of the SULT1E1 promoter that plays a crucial role in regulating the activity of SULT1E1 transcription.
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 encodes a protein that transfers a sulfo moiety to and from estrone, which may control levels of estrogen receptors.
, estrone sulfotransferase
, ste2 gene for estrogen sulfotransferase
, sulfotransferase, estrogen-preferring
, estrogen sulfotransferase
, sulfotransferase 1E1
, estrogen sulfotransferase, testis isoform
, sulfotransferase, estrogen preferring
, adrenocortical estrogen sulfotransferase
, sulfotransferase family 1E, estrogen-preferring, member 1
, sulfotransferase family 1E member 1 L homeolog
, sulfotransferase family 1E member 1 S homeolog