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http://purl.uniprot.org/citations/14563703http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14563703http://www.w3.org/2000/01/rdf-schema#comment"The cysteine protease cathepsin L exhibits hormone-regulated expression during ovulation. In situ hybridization analyses of immature and pregnant mare serum gonadotropin-treated mouse and rat ovaries showed that cathepsin L expression in granulosa cells of small, growing follicles increased in periovulatory follicles after human chorionic gonadotropin stimulation. In the rat ovary, cathepsin L was also expressed in follicles with signs of atresia. To determine the molecular mechanisms that mediate the diverse regulation of this gene in granulosa cells, rat cathepsin L promoter-reporter constructs were analyzed by transient transfection assays in rat granulosa cells and EMSAs. A construct containing the transcriptional start site and -244 bp of upstream promoter sequence (-244/+33 bp) exhibited inducibility by forskolin, the phorbol ester phorbol myristate acetate, and an additive effect of both. Within this region, three functional specificity protein 1 (Sp1) sites, an overlapping early growth response protein-1 site, and a cAMP regulatory element-binding protein site were identified. Single or double mutants of the above-mentioned sites did not alter forskolin/phorbol myristate acetate inducibility of the promoter. Mutation of all three Sp1/specificity protein 3 (Sp3) sites, which also mutated the early growth response protein-1 site, reduced the promoter activation. Mutation of the cAMP regulatory element-binding protein site in the triple Sp1 mutant construct completely blocked the inducibility of the promoter. When these same constructs were transfected into MCF-7 human breast cancer cells or were cotransfected with an Sp1 expression vector in Drosophila SL2 cells, similar results were obtained. Collectively, the data document that three Sp1/specificity protein 3 binding GC-rich regions and a functional cAMP regulatory element constitute an important transcriptional regulatory complex for expression of the cathepsin L gene in rat granulosa cells."xsd:string
http://purl.uniprot.org/citations/14563703http://purl.org/dc/terms/identifier"doi:10.1210/en.2003-0963"xsd:string
http://purl.uniprot.org/citations/14563703http://purl.uniprot.org/core/author"Richards J.S."xsd:string
http://purl.uniprot.org/citations/14563703http://purl.uniprot.org/core/author"Sriraman V."xsd:string
http://purl.uniprot.org/citations/14563703http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14563703http://purl.uniprot.org/core/name"Endocrinology"xsd:string
http://purl.uniprot.org/citations/14563703http://purl.uniprot.org/core/pages"582-591"xsd:string
http://purl.uniprot.org/citations/14563703http://purl.uniprot.org/core/title"Cathepsin L gene expression and promoter activation in rodent granulosa cells."xsd:string
http://purl.uniprot.org/citations/14563703http://purl.uniprot.org/core/volume"145"xsd:string
http://purl.uniprot.org/citations/14563703http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14563703
http://purl.uniprot.org/citations/14563703http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/14563703
http://purl.uniprot.org/uniprot/P07154#attribution-49D847346EA212708C5347F8FF8A9E32http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/14563703
http://purl.uniprot.org/uniprot/#_A0A8I6AKK6-mappedCitation-14563703http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14563703
http://purl.uniprot.org/uniprot/#_A0A8L2QDP6-mappedCitation-14563703http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14563703
http://purl.uniprot.org/uniprot/#_A0A1Y7VJC1-mappedCitation-14563703http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14563703
http://purl.uniprot.org/uniprot/#_A0A1Y7VNM3-mappedCitation-14563703http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14563703
http://purl.uniprot.org/uniprot/#_A0A1Y7VNQ4-mappedCitation-14563703http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14563703
http://purl.uniprot.org/uniprot/#_A0A1Y7VP49-mappedCitation-14563703http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14563703
http://purl.uniprot.org/uniprot/#_A6KCV1-mappedCitation-14563703http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14563703
http://purl.uniprot.org/uniprot/#_F1M9G7-mappedCitation-14563703http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14563703
http://purl.uniprot.org/uniprot/#_Q91XT1-mappedCitation-14563703http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14563703
http://purl.uniprot.org/uniprot/#_Q01714-mappedCitation-14563703http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14563703
http://purl.uniprot.org/uniprot/#_Q3UHZ4-mappedCitation-14563703http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14563703
http://purl.uniprot.org/uniprot/#_P07154-mappedCitation-14563703http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14563703