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http://purl.uniprot.org/citations/23665321http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23665321http://www.w3.org/2000/01/rdf-schema#comment"We investigated whether arginase inhibition suppressed interleukin (IL)-1β-stimulated proliferation in vascular smooth muscle cells (VSMCs) and the possible mechanisms involved. IL-1β stimulation increased VSMC proliferation, while the arginase inhibitor BEC and transfection of the antisense (AS) oligonucleotide against arginase I decreased VSMC proliferation and was associated with increased protein content of the cell cycle regulator p21Waf1/Cip1. IL-1β incubation induced inducible nitric oxide synthase (iNOS) mRNA expression and protein levels in a dose-dependent manner, but did not affect arginase I and II expression. Consistent with this data, IL-1β stimulation resulted in increase in NO production that was significantly augmented by arginase inhibition. The specific iNOS inhibitor 1400W abolished IL-1β-mediated NO production and further accentuated IL-1β-stimulated cell proliferation. Incubation with NO donors GSNO and DETA/NO in the presence of IL-1β abolished VSMCs proliferation and increased p21Waf1/Cip1 protein content. Furthermore, incubation with the cGMP analogue 8-Br-cGMP prevented IL-1β-induced VSMCs proliferation. In conclusion, arginase inhibition augmented iNOS-dependent NO production that resulted in suppression of IL-1β-induced VSMCs proliferation in a cGMP-dependent manner."xsd:string
http://purl.uniprot.org/citations/23665321http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2013.05.002"xsd:string
http://purl.uniprot.org/citations/23665321http://purl.uniprot.org/core/author"Yoon J."xsd:string
http://purl.uniprot.org/citations/23665321http://purl.uniprot.org/core/author"Ryoo S."xsd:string
http://purl.uniprot.org/citations/23665321http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23665321http://purl.uniprot.org/core/name"Biochem Biophys Res Commun"xsd:string
http://purl.uniprot.org/citations/23665321http://purl.uniprot.org/core/pages"428-433"xsd:string
http://purl.uniprot.org/citations/23665321http://purl.uniprot.org/core/title"Arginase inhibition reduces interleukin-1beta-stimulated vascular smooth muscle cell proliferation by increasing nitric oxide synthase-dependent nitric oxide production."xsd:string
http://purl.uniprot.org/citations/23665321http://purl.uniprot.org/core/volume"435"xsd:string
http://purl.uniprot.org/citations/23665321http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23665321
http://purl.uniprot.org/citations/23665321http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23665321
http://purl.uniprot.org/uniprot/#_A6JUJ9-mappedCitation-23665321http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23665321
http://purl.uniprot.org/uniprot/#_A6JUK0-mappedCitation-23665321http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23665321
http://purl.uniprot.org/uniprot/#_A6JUK1-mappedCitation-23665321http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23665321
http://purl.uniprot.org/uniprot/#_P07824-mappedCitation-23665321http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23665321
http://purl.uniprot.org/uniprot/A6JUK0http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/23665321
http://purl.uniprot.org/uniprot/A6JUJ9http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/23665321
http://purl.uniprot.org/uniprot/P07824http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/23665321
http://purl.uniprot.org/uniprot/A6JUK1http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/23665321