Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.6.1 (sulfatase)
 3,205 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

To investigate the modifying role of intestinal microflora in the metabolism of chemical carcinogens in vivo, we subjected bile from Fischer rats treated per os with chemical carcinogens and related compounds to a mutagenicity assay in the presence and absence of a cell-free extract from human feces. A mixture of the bile sample and potassium phosphate buffer was incubated in the presence or absence of human cell-free fecal extract and then further incubated with a bacterial suspension of Salmonella typhimurium tester strains TA98 or TA100. Bile from rats treated with 1-nitropyrene (1-NP) produced about 2700 and 400 revertants per plate in strain TA98 in the presence and absence of the fecal extract, respectively. There was a drug dose- and bile volume-related response. Treatment of 1-NP-bile with beta-glucuronidase, but not aryl sulfatase, enhanced its mutagenicity. Cell-free extracts of some strains of intestinal bacteria (Bacteroides fragilis ATCC 12044, B. vulgatus ATCC 8482, B. thetaiotaomicron ATCC 12290, Bacteroides sp. strain 524, Eubacterium eligens VPI C15-48, Peptostreptococcus sp. strain 204 and Escherichia coli A-5-18) also enhanced the mutagenicity of 1-NP-bile. These bacterial cell-free extracts hydrolyzed the synthetic beta-D-glucuronides of phenolphthalein and/or p-nitrophenol. These data indicate that the glucuronide(s) of 1-NP-metabolite(s) secreted into bile can be hydrolyzed in the intestine by bacterial beta-glucuronidases to potent mutagenic aglycone(s).
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PMID:Mutagenic activation of biliary metabolites of 1-nitropyrene by intestinal microflora. 398 38

Expression of the arylsulfatase (HpArs) gene in the sea urchin, Hemicentrotus pulcherrimus, is regulated in spatially, as well as temporally, during development. To address the cis-regulatory elements involved in this regulation, we performed reporter assays using variously deleted or mutated promoter and regulatory elements of the HpArs gene, accompanied by gel mobility shift assay and foot printing. Results show that two regions, PU1 (-72 b.p. to -56 b.p.), which is similar to SpZ12-1 and/or Oct-1 motif, and the PD1 site (+133 b.p. to +142 b.p.), which is homologous to the binding sites of Rel family transcription factors and/or AGIE-BP1, are related to the regulation of expression of the HpArs gene. Furthermore, an HpArs enhancer element called C15, which is located 3 kb.p. downstream from the transcription start site, activates the HpArs promoter. We also report that the enhancer activity of the C15 fragment was mediated by elements, PU1 and PD1.
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PMID:Proximal cis-regulatory elements of sea urchin arylsulfatase gene. 978 79

A 50 bp region from -194 bp to -144 bp of the arylsulfatase gene (HpArs) of the sea urchin, Hemicentrotus pulcherrimus, is related to the temporally regulated expression of this gene. This region contains a Sox (Sry-related HMG box)-binding site, and the introduction of sequence mutations to this site significantly reduced the activity of the HpArs promoter, even in the presence of the C15 enhancer, which consists of HpOtx and CAAT motifs. A protein that binds to the Sox-binding site in the 50 bp region of the HpArs gene was detected in nuclear extracts of mesenchyme blastulae and a protein synthesized in vitro using SoxB1 cDNA of another sea urchin, Strongylocentrotus purpuratus, also bound to this Sox site. These results suggest that HpSox, which is maternally expressed and remains abundant by the pluteus stage, is clearly implicated in regulation of the HpArs gene. The presence of a negatively acting cis element in this 50 bp region has also been detected.
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PMID:Sox regulates transcription of the sea urchin arylsulfatase gene. 1096 43