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rdf:type |
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lifeskim:mentions |
umls-concept:C0031715,
umls-concept:C0040649,
umls-concept:C0054846,
umls-concept:C0079904,
umls-concept:C0132555,
umls-concept:C0205263,
umls-concept:C1420556,
umls-concept:C1424530,
umls-concept:C1515655,
umls-concept:C1711351,
umls-concept:C2349975
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pubmed:issue |
23
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pubmed:dateCreated |
2004-5-31
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pubmed:abstractText |
Nitric oxide (NO) produced by inducible nitric-oxide synthase (NOSII) is mainly regulated at the transcriptional level by the nuclear factor-kappaB (NF-kappaB). In the present study, we further analyzed the role of NF-kappaB in the in vivo transcriptional regulation of NOSII gene by comparing two clones isolated from the EMT-6 mouse mammary cancer cell line. In response to interleukin (IL)-1beta or lipopolysaccharide (LPS), EMT-6 clone J (EMT-6J) cells produce 3-fold more NO than EMT-6 clone H (EMT-6H) cells, an effect correlated with enhanced activation of NF-kappaB in EMT-6J cells. In response to IL-1beta, the kinetics of degradation of NF-kappaB inhibitors IkappaB-alpha and IkappaB-beta, the nucleo-cytoplasmic shuttling of the transcription factor and its binding to a specific DNA sequence were similar in both clones. In contrast, an IL-1beta-induced phosphorylation of serine residues in NF-kappaB p65 subunit was observed in EMT-6J, but not in EMT-6H, cells. This IL-1beta-induced phosphorylation of p65 was specifically prevented by pretreatment of EMT-6J cells with the casein kinase II inhibitor DRB. Small interfering RNA-mediated depletion of casein kinase II-alpha subunit also decreased NF-kappaB transcriptional activity and NOSII gene transcription in IL-1beta and LPS-stimulated EMT-6J cells to the levels observed in EMT-6H cells treated in the same conditions. Altogether, these data indicate that casein kinase II-mediated phosphorylation of p65 subunit can enhance the transcriptional activity of NF-kappaB in vivo. This post-translational modification of the transcription factor can be responsible for increased NOSII gene transcription and NO production in tumor cells exposed to either IL-1beta or LPS.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Casein Kinase II,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase Type II,
http://linkedlifedata.com/resource/pubmed/chemical/Nos2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor RelA
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
279
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
23953-60
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15033982-Animals,
pubmed-meshheading:15033982-Blotting, Northern,
pubmed-meshheading:15033982-Casein Kinase II,
pubmed-meshheading:15033982-Cell Line,
pubmed-meshheading:15033982-Cell Line, Tumor,
pubmed-meshheading:15033982-Cell Nucleus,
pubmed-meshheading:15033982-Cytoplasm,
pubmed-meshheading:15033982-DNA,
pubmed-meshheading:15033982-Enzyme Activation,
pubmed-meshheading:15033982-Genes, Reporter,
pubmed-meshheading:15033982-Immunoblotting,
pubmed-meshheading:15033982-Interleukin-1,
pubmed-meshheading:15033982-Kinetics,
pubmed-meshheading:15033982-Lipopolysaccharides,
pubmed-meshheading:15033982-Mice,
pubmed-meshheading:15033982-Microscopy, Fluorescence,
pubmed-meshheading:15033982-Mutagenesis, Site-Directed,
pubmed-meshheading:15033982-NF-kappa B,
pubmed-meshheading:15033982-Nitric Oxide,
pubmed-meshheading:15033982-Nitric Oxide Synthase,
pubmed-meshheading:15033982-Nitric Oxide Synthase Type II,
pubmed-meshheading:15033982-Phosphorylation,
pubmed-meshheading:15033982-Plasmids,
pubmed-meshheading:15033982-Protein Binding,
pubmed-meshheading:15033982-Protein Processing, Post-Translational,
pubmed-meshheading:15033982-Protein Structure, Tertiary,
pubmed-meshheading:15033982-Protein-Serine-Threonine Kinases,
pubmed-meshheading:15033982-RNA, Small Interfering,
pubmed-meshheading:15033982-Serine,
pubmed-meshheading:15033982-Time Factors,
pubmed-meshheading:15033982-Transcription, Genetic,
pubmed-meshheading:15033982-Transcription Factor RelA,
pubmed-meshheading:15033982-Transcriptional Activation,
pubmed-meshheading:15033982-Transfection
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pubmed:year |
2004
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pubmed:articleTitle |
Casein kinase II-mediated phosphorylation of NF-kappaB p65 subunit enhances inducible nitric-oxide synthase gene transcription in vivo.
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pubmed:affiliation |
Cancer Immunotherapy Laboratory, Ecole Pratique des Hautes Etudes, INSERM U517, Faculty of Medicine, Dijon, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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