Disease relevance of Sulf1

• An unnamed sporeforming microorganism, termed Clostridium sp. strain S2, possessing bile salt sulfatase activity was isolated from rat intestinal microflora [1].
• Detection of breast cancer-associated estrone sulfatase in breast cancer biopsies and cell lines using polymerase chain reaction [2].
• Sulfatase- and beta-glucuronidase-treated, concentrated urine was bioassayed for urinary mutagens in a microsuspension modification of the Salmonella assay with and without metabolic activation [3].
• Because the blood pressures of SHR/y and SHR/a were also intermediate between SHR and WKY, the STS activity could be a secondary response to the hypertension [4].
• Based on these data, clinical studies with AHBS in acne patients are warranted, in order to verify the hypothesis on the importance of the sulfatase pathway in androgen-dependent skin diseases [5].

High impact information on Sulf1

• Some of the Lar-Fer-containing vesicles in Golgi-lysosome areas at 15 min after injection were found to contain aryl sulfatase reaction product, indicating fusion with lysosomes [6].
• The activity of iduronate sulfatase was completely inhibited in vitro by suramin at concentrations of 50 microM or higher [7].
• The activities of the lysosomal enzymes iduronate sulfatase, beta-glucuronidase, and hyaluronidase in the liver of the suramin-treated mature rats were consistently decreased, whereas those of alpha-L-iduronidase, heparan N-sulfatase, arylsulfatase B, and others were considerably increased [7].
• This was shown to be related to lysosomal enzyme activity rather than to specific phases of the cell cycle, there being a highly significant correlation (p smaller than 0.001) with aryl sulfatase activity [8].
• Active site serine promotes stabilization of the reactive glutathione thiolate in rat glutathione transferase T2-2. Evidence against proposed sulfatase activity of the corresponding human enzyme [9].

Chemical compound and disease context of Sulf1

• Enzymatic control of estrogen production in human breast cancer: relative significance of aromatase versus sulfatase pathways [10].
• To explain the absence of aryl sulfatase in areas of bone formation we suggest that different sulfate esters are mobilized from resorbing and mineralizing matrices, and that only the enzyme associated with bone resorption is histochemically detectable with the artificial substrates currently used [11].

Biological context of Sulf1

• Using the first two compounds, hydrolysis was detected after 3 min at 37 degrees C and still occurred, albeit to a reduced extent, at 16 and 4 degrees C. This indicates that aryl sulfatase and acid phosphatase are active prelysosomally [12].
• A sulfatase regulating the migratory potency of oligodendrocyte progenitor cells through tyrosine phosphorylation of beta-catenin [13].
• Urine concentrates were tested in Ames bacterial strains TA98 and TA100, with and without metabolic activation and with and without beta-glucuronidase/aryl sulfatase [14].
• An alternative hypotheses is that a regulatory locus in addition to the structural locus is responsible for STS activity levels, and this regulatory locus is on the rat Y chromosome [4].
• Only STS was present before sexual maturation [15].

Anatomical context of Sulf1

• An enzyme with sulfatase activity has been isolated from the granules of a rat NK leukemia cell line, CRNK-16 [16].
• Natural killer cell cytolytic granule-associated enzymes. I. Purification, characterization, and analysis of function of an enzyme with sulfatase activity [16].
• Enrichment of acid hydrolase activities (aryl sulfatase, N-acetyl-beta-glucosaminidase, tartrate-sensitive acid phosphatase, and cholesteryl ester acid hydrolase) and cathepsin D mass was also comparable in early and late endosomes but was considerably lower in the receptor-recycling fraction [17].
• Treatment of hepatocyte medium with beta-glucuronidase and sulfatase resulted in the loss of five putative conjugates and concomitant increases in 4'-, 6-, and 7-hydroxywarfarin and warfarin, suggesting that these metabolites and warfarin were conjugated [18].
• These data were supported by measuring aromatase, type I 17beta-HSD, and STS enzyme activities in chondrocytes collected from tibial growth plates at 1 and 7 wk of age [19].

Associations of Sulf1 with chemical compounds

• HRP did not bind to the luminal membrane and was not transferred across cells but was confined to apical lysosomes as identified by acid phosphatase and aryl sulfatase activities [20].
• Sulfatase action on released rLH reveals that sulfation may be related to release of rLH but that sulfate residues are not involved in the expression of rLH bioactivity [21].
• This is not due to the direct inhibition of the lysosomal exoglycosidase and sulfatase enzymes responsible for the complete depolymerization of HS chains, since pathway 1, while slowed, continued to completely depolymerize the HS chains in the presence of leupeptin [22].
• These were 4-methylumbelliferyl sulfate, 4-methylumbelliferyl phosphate, and 4-methylumbelliferyl-beta-D-glucosaminide, which are substrates for aryl sulfatase, acid phosphatase, and beta-hexosaminidase, respectively [12].
• Chondroitin sulfates, dermatan sulfate, heparan sulfate, heparin, keratan sulfate, and oligosaccharides derived from these sulfated glycosaminoglycans have been used for the measurement of sulfatase activity of rat skin extracts [23].

Other interactions of Sulf1

• In the second experiment, the activities of all three enzymes were elevated both 3 and 6 weeks after sub-tx, and the activities of cathepsin D and aryl sulfatase A in the postnuclear homogenate (S2) were significantly elevated [24].
• The enzymes include acid phosphatase, aryl sulfatase, N-acetyl-beta-glucosaminidase, and esterase activities [25].
• Finally, 1 day after the injection of poly-D-glutamic acid, the activities of several lysosomal enzymes (hexosaminidase, cathepsin B, acid sphingomyelinase, and sulfatase B), but not of all of them (eg, acid phosphatase), were increased in the kidney cortex [26].
• The different products of degradation, identified by fast protein liquid chromatography (FPLC) gel filtration chromatography, were indicative of protease, endoglycosidase (heparanase) and exoglycosidase and/or sulfatase activity [27].
• A purified myelin preparation containing [35S]-labeled cerebroside sulfate (CS) was biosynthesized in developing rat brain and tested as a model of a physiological substrate for CS hydrolysis by arylsulfatase A. Particular attention was directed to the involvement of the CS sulfatase activator protein in facilitating the catabolic process [28].

Analytical, diagnostic and therapeutic context of Sulf1

• The identity of the peak eluted as 3,3'T2-S was ascertained by its hydrolysis with sulfatase and the generation of 3,3'T2 identified by HPLC [29].
• Rat liver homogenates (S10) fortified with either uridine diphosphoglucuronic acid or phosphoadenosine phosphosulfate produced 180 +/- 56 and 95 +/- 31 pmoles of conjugates respectively, which were recovered as B[a]P-diol after treatment of the aqueous phase with either beta-glucuronidase or aryl sulfatase [30].
• Acid phosphatase and aryl sulfatase activities are also demonstrable by electron microscopy [25].
• The activities of various classes of lysosomal enzymes (cathepsin D, beta-glucuronidase, and aryl sulfatase A) were studied in thyroid tissue remaining in situ at various time intervals after subtotal thyroidectomy (sub-tx) [24].
• High-performance liquid chromatography of the sulfate conjugates showed one major sulfatase-sensitive peak with all tissues [31].

References