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http://purl.uniprot.org/citations/37487659http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/37487659http://www.w3.org/2000/01/rdf-schema#comment"Human sulfotransferases 1A3 (SULT1A3) has received particular interest, due to their functions of catalyzing the sulfonation of numerous phenolic substrates, including bioactive endogenous molecules and therapeutic agents. However, the regulation of SULT1A3 expression and the underlying mechanism remain unclear. Here, we aimed to investigate the regulation effects of bile acid-activated farnesoid X receptor (FXR) on SULT1A3 expression, and to shed light on the mechanism thereof. Our results demonstrated that FXR agonists (CDCA and GW4064) significantly inhibit the expression of SULT1A3 at mRNA and protein levels. In addition, overexpression of FXR led to decrease in SULT1A3 expression and knockdown of FXR significantly induced the expression of SULT1A3 in protein and mRNA levels, confirming that FXR expression manifestly showed negative regulatory effect on basal SULT1A3 expression. Furthermore, a combination of luciferase reporter gene and CHIP assays showed that FXR repressed SULT1A3 transcription through direct binding to the region at base pair positions -664 to -654. In conclusion, this study for the first time confirmed FXR was a negative transcriptional regulator of human SULT1A3 enzyme."xsd:string
http://purl.uniprot.org/citations/37487659http://purl.org/dc/terms/identifier"doi:10.1111/cbdd.14312"xsd:string
http://purl.uniprot.org/citations/37487659http://purl.uniprot.org/core/author"Cao J."xsd:string
http://purl.uniprot.org/citations/37487659http://purl.uniprot.org/core/author"Dou Y."xsd:string
http://purl.uniprot.org/citations/37487659http://purl.uniprot.org/core/author"Hou L."xsd:string
http://purl.uniprot.org/citations/37487659http://purl.uniprot.org/core/author"Li J."xsd:string
http://purl.uniprot.org/citations/37487659http://purl.uniprot.org/core/author"Liu Z."xsd:string
http://purl.uniprot.org/citations/37487659http://purl.uniprot.org/core/author"Li Y."xsd:string
http://purl.uniprot.org/citations/37487659http://purl.uniprot.org/core/author"Sun H."xsd:string
http://purl.uniprot.org/citations/37487659http://purl.uniprot.org/core/author"Wang M."xsd:string
http://purl.uniprot.org/citations/37487659http://purl.uniprot.org/core/author"Qin J."xsd:string
http://purl.uniprot.org/citations/37487659http://purl.uniprot.org/core/author"Zhang M."xsd:string
http://purl.uniprot.org/citations/37487659http://purl.uniprot.org/core/author"Pei S."xsd:string
http://purl.uniprot.org/citations/37487659http://purl.uniprot.org/core/date"2023"xsd:gYear
http://purl.uniprot.org/citations/37487659http://purl.uniprot.org/core/name"Chem Biol Drug Des"xsd:string
http://purl.uniprot.org/citations/37487659http://purl.uniprot.org/core/pages"1014-1023"xsd:string
http://purl.uniprot.org/citations/37487659http://purl.uniprot.org/core/title"Farnesoid X receptor represses human sulfotransferase 1A3 expression through direct binding to the promoter."xsd:string
http://purl.uniprot.org/citations/37487659http://purl.uniprot.org/core/volume"102"xsd:string
http://purl.uniprot.org/citations/37487659http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/37487659
http://purl.uniprot.org/citations/37487659http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/37487659
http://purl.uniprot.org/uniprot/#_B6ZGS9-mappedCitation-37487659http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/37487659
http://purl.uniprot.org/uniprot/#_B7Z423-mappedCitation-37487659http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/37487659
http://purl.uniprot.org/uniprot/#_B2R7F1-mappedCitation-37487659http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/37487659
http://purl.uniprot.org/uniprot/#_F1DAL1-mappedCitation-37487659http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/37487659