Disease relevance of Sts

• Our hypothesis is that the steroid sulfatase gene (Sts) may indirectly contribute to the modulation of blood pressure (BP) in rats with genetic hypertension [1].
• The present investigation supports previous studies that demonstrate the unique features of perfluorocarboxylic acid toxicity, relative to classic peroxisome proliferators and endorses the continued use of 2D protein-mapping of Sts and other proteins as biomarkers of chemical toxicity [2].
• Trans-stimulation, both inward and outward, via System ASC is vigorous in the hepatoma cell [3].
• We conclude that, as in Ehrlich ascites tumor cells and in embryonic heart cells, the A, ASC, and L systems are operative in isolated hepatocytes for the transport of amino acids [4].
• In malignant fibrosarcomas, only system ASC was identifiable, and its Vmax was 15 times higher than that observed in fibroblasts [5].

Psychiatry related information on Sts

• Reversal of scopolamine induced amnesia in rats by the steroid sulfatase inhibitor estrone-3-O-sulfamate [6].

High impact information on Sts

• We investigated the activities of Na(+)-dependent transport systems A, ASC, and N in hepatic plasma membrane vesicles (HPMVs) prepared from rats treated with TNF in vivo [7].
• The presence of the tumor resulted in a generalized stimulation of concentrative (Na(+)-dependent) glucogenic (small neutral) amino acid uptake via System A (3.4-fold), System N (2.3-fold), and System ASC (1.7-fold), as well as in the facilitative (Na(+)-independent) uptake of arginine via System y+ (1.7-fold) [8].
• During liver regeneration, no changes were noted in the transport activities of system N and system ASC as measured by the uptake of glutamine and cysteine, respectively, in the presence of 2-(methylamino)isobutyric acid [9].
• These results demonstrate that glutamine transporters, with characteristics associated with hepatic Systems N, L, and A (or ASC), can be expressed in X. laevis oocytes injected with specific size fractions of rat liver mRNA [10].
• Exposure of vesicles to p-bromophenacyl bromide and methyl p-nitrobenzenesulfonate, which share with DEPC reactivity against histidine residues, also led to inhibition of alanine transport through systems A and ASC [11].

Chemical compound and disease context of Sts

• Furthermore, threonine uptake by the hepatoma cell undergoes no stimulation when Li+ is substituted for choline in a Na+-free medium, whereas ASC uptake by the ordinary rat hepatocyte is stimulated much as is System A uptake [3].
• As in other occurrences, and in contrast to System A, ASC transport in the hepatoma cell is stimulated neither by amino acid deprivation nor by insulin, glucagon, or dexamethasone [3].
• Steroid sulfatase in brain: comparison of sulfohydrolase activities for various steroid sulfates in normal and pathological brains, including the various forms of metachromatic leukodystrophy [12].
• In postmenopausal breast cancer tissue, steroid sulfatase (STS) activity is high and much estrone sulfate also exists; these facts reveal that estrone sulfate may be involved in the growth of breast cancer as an estrogen source [13].
• Steroid sulfatase is an enzyme, which catalyzes hydrolysis from estrone sulfate to estrone, and the development of steroid sulfatase inhibitors is expected as novel therapeutic drugs for postmenopausal breast cancer [13].

Biological context of Sts

• Cloning of the rat steroid sulfatase gene (Sts), a non-pseudoautosomal X-linked gene that undergoes X inactivation [14].
• Further study is needed to discriminate between these possibilities, and until the second hypothesis can be eliminated, the Sts locus or its modifier loci remain a potential component of the Y chromosome hypertensive locus [15].
• In some mammals the steroid sulfatase locus (Sts) is on the Y chromosome, although the rat Sts is on the X chromosome [15].
• An especially broad substrate specificity for systems L and ASC is therefore suggested for the rat pancreatic islet cells [16].
• Epidermal steroid sulfatase and cholesterol sulfotransferase are regulated during late gestation in the fetal rat [17].

Anatomical context of Sts

• In the present study, transport by Systems A, ASC, and N was shown to be elevated in hepatocytes isolated from diabetic rats [18].
• We find that the two wide-range Na+-dependent transport systems A and ASC for various neutral amino acid can be discriminated more sharply in the hepatoma cell line HTC than in any cell yet studied by us in which the two systems co-exist [3].
• Cholesterol sulfate was metabolized to pregnenolone sulfate by a mitochondrial side-chain cleavage system, but proved to be a relatively poor substrate for an extramitochondrial steroid sulfatase activity present in adrenal cortex [19].
• In fibroblasts, glutamine transport was mediated by systems ASC and A [5].
• System ASC (alanine-serine-cysteine) appeared to be of primary importance for the transport of these amino acids in isolated brain capillaries [20].

Associations of Sts with chemical compounds

• The presence of Na+ (100 mM NaCl) and L-alanine (10 mM) during exposure to vesicles to DEPC protected against inactivation of system A (but not system ASC) transport activity [11].
• In the rat hepatocyte, whether freshly separated or in primary culture, we do not find L-glutamine entry by Systems A and ASC as seen in cells previously studied [21].
• The increased amino acid transport activity in diabetic rat hepatocytes was due mainly to an increased transport through system A (alanine-preferring) and, to a much lesser extent, through system ASC (alanine, serine, cysteine) [22].
• This overall pattern of protection is opposite to that previously found against specific sulfhydryl reagents (i.e. N-ethylmaleimide), where protection of system ASC was nearly maximal [11].
• In contrast, the activity of System ASC measured by the Na+-dependent uptake of MeAIB-insensitive threonine uptake increased after day 14 and was optimal between days 16 and 18 [23].

Other interactions of Sts

• Additionally, protein and mRNA levels of loricrin and filaggrin, two structural proteins of stratum corneum, were increased in treated epidermis, as were the activities of two lipid catabolic enzymes critical to stratum corneum function, beta-glucocerebrosidase and steroid sulfatase [24].
• The LG fraction was enriched in certain acid hydrolases including glucosidase, acid phosphatase, phospholipases A, and sphingomyelinase; other acid hydrolases, i.e., amino-glycosidases, glactosidase and aryl sulfatase (pH 5.5), and steroid sulfatase were not preferentially localized in this fraction [25].
• Using in situ hybridization, mRNAs of aromatase p450, type I and II 17beta-hydroxysteroid dehydrogenase (HSD), steroid sulfatase (STS), and 5alpha-reductase were detected in proliferating and hypertrophic chondrocytes of the growth plate [26].
• The treatment of solubilized and microsome-bound arylsulfatase C with transglutaminase indicated two susceptible glutamine residues per subunit of the enzyme molecule [27].

Analytical, diagnostic and therapeutic context of Sts

• Activities of beta-glucocerebrosidase and steroid sulfatase, enzymes previously linked to barrier maturation, also increased after treatment with PPARalpha and FXR activators [28].
• Antibody secreting cell probes (ASC-probes) were generated from the hepatic lymph node (HLN), mesenteric lymph node (MLN) and spleen of rats after infection with the liver fluke, Fasciola hepatica, and used to probe Western blots of parasite antigens [29].
• The expression of sulfotransferase and steroid sulfatase was studied in rat liver using the most promising culture models of hepatocytes, including monolayer culture with a pyruvate (30 mM) enriched medium, co-culture with rat epithelial cells from primitive biliary origin and collagengel sandwich culture [30].
• A monoclonal antibody to rat liver arylsulfatase C and its application in immunohistochemistry [31].
• By electron microscopy, arylsulfatase C was found localized on the membranes of the endoplasmic reticulum and nuclear envelopes in these cells [31].

References