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http://purl.uniprot.org/citations/18230613http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18230613http://www.w3.org/2000/01/rdf-schema#comment"Endothelial dysfunction plays a central role in diabetic vascular disease, but its molecular bases are not completely defined. We showed previously that the actin-binding protein proflin-1 was increased in the diabetic endothelium and that attenuated expression of profilin-1 protected against atherosclerosis. Also 7-ketocholesterol up-regulated profilin-1 in endothelial cells via transcriptional mechanisms. The present study addressed the pathways responsible for profilin-1 gene expression in 7-ketocholesterol-stimulated endothelial cells and in the diabetic aorta. In luciferase reporter assays, the response to 7-ketocholesterol within the 5'-flanking region of profilin-1 was dependent on a single STAT response element. In aortic endothelial cells, 7-ketocholesterol enhanced STAT3 activation, which required JAK2 and tyrosine 394 phosphorylation of oxysterol-binding protein-1. These changes were recapitulated in the aorta of diabetic rats. Also 7-ketocholesterol in cultured endothelial cells and diabetes in the aorta elicited the recruitment of STAT3 and relevant coregulatory factors to the oxysterol-responsive region of the profilin-1 promoter. These events were required for profilin-1 up-regulation. These studies identify a previously unrecognized oxysterol-binding protein-mediated mode of activation of STAT3 that controls the expression of the proatherogenic protein profilin-1 in response to 7-ketocholesterol and the diabetic milieu."xsd:string
http://purl.uniprot.org/citations/18230613http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m710092200"xsd:string
http://purl.uniprot.org/citations/18230613http://purl.uniprot.org/core/author"Kazlauskas A."xsd:string
http://purl.uniprot.org/citations/18230613http://purl.uniprot.org/core/author"Romeo G.R."xsd:string
http://purl.uniprot.org/citations/18230613http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18230613http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/18230613http://purl.uniprot.org/core/pages"9595-9605"xsd:string
http://purl.uniprot.org/citations/18230613http://purl.uniprot.org/core/title"Oxysterol and diabetes activate STAT3 and control endothelial expression of profilin-1 via OSBP1."xsd:string
http://purl.uniprot.org/citations/18230613http://purl.uniprot.org/core/volume"283"xsd:string
http://purl.uniprot.org/citations/18230613http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18230613
http://purl.uniprot.org/citations/18230613http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18230613
http://purl.uniprot.org/uniprot/A6I0C1#attribution-C0C5A50FB851E2FA1C70445E0691CA02http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18230613
http://purl.uniprot.org/uniprot/D4A9D8#attribution-C0C5A50FB851E2FA1C70445E0691CA02http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18230613
http://purl.uniprot.org/uniprot/#_D4A9D8-mappedCitation-18230613http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18230613
http://purl.uniprot.org/uniprot/#_P52631-mappedCitation-18230613http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18230613
http://purl.uniprot.org/uniprot/#_A0A8I6GJJ3-mappedCitation-18230613http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18230613
http://purl.uniprot.org/uniprot/P52631http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18230613
http://purl.uniprot.org/uniprot/D4A9D8http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18230613
http://purl.uniprot.org/uniprot/A0A8I6GJJ3http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18230613