Source:http://linkedlifedata.com/resource/pubmed/id/10187764
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
15
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| pubmed:dateCreated |
1999-5-3
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| pubmed:abstractText |
Human astrocytoma T67 cells constitutively express a neuronal NO synthase (NOS-I) and, following administration of lipopolysaccharide (LPS) plus interferon-gamma (IFNgamma), an inducible NOS isoform (NOS-II). Previous results indicated that a treatment of T67 cells with the combination of LPS plus IFNgamma, by affecting NOS-I activity, also inhibited NO production in a very short time. Here, we report that under basal conditions, a NOS-I protein of about 150 kDa was weakly and partially tyrosine-phosphorylated, as verified by immunoprecipitation and Western blotting. Furthermore, LPS plus IFNgamma increased the tyrosine phosphorylation of NOS-I, with a concomitant inhibition of its enzyme activity. The same effect was observed in the presence of vanadate, an inhibitor of phosphotyrosine-specific phosphatases. On the contrary, genistein, an inhibitor of protein-tyrosine kinases, reduced tyrosine phosphorylation of NOS-I, enhancing its enzyme activity. Finally, using reverse transcriptase-polymerase chain reaction, we have observed that a suboptimal induction of NOS-II mRNA expression in T67 cells was enhanced by vanadate (or L-NAME) and inhibited by genistein. Because exogenous NO has been found to suppress NOS-II expression, the decrease of NO production that we have obtained from the inactivation of NOS-I by LPS/IFNgamma-induced tyrosine phosphorylation provides the best conditions for NOS-II expression in human astrocytoma T67 cells.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Genistein,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon-gamma,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/NOS1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/NOS2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase Type I,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase Type II,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Vanadates
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| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
9
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| pubmed:volume |
274
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
9915-7
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| pubmed:dateRevised |
2011-10-27
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| pubmed:meshHeading |
pubmed-meshheading:10187764-Astrocytoma,
pubmed-meshheading:10187764-Enzyme Induction,
pubmed-meshheading:10187764-Genistein,
pubmed-meshheading:10187764-Humans,
pubmed-meshheading:10187764-Interferon-gamma,
pubmed-meshheading:10187764-Lipopolysaccharides,
pubmed-meshheading:10187764-Nerve Tissue Proteins,
pubmed-meshheading:10187764-Nitric Oxide Synthase,
pubmed-meshheading:10187764-Nitric Oxide Synthase Type I,
pubmed-meshheading:10187764-Nitric Oxide Synthase Type II,
pubmed-meshheading:10187764-Phosphorylation,
pubmed-meshheading:10187764-Polymerase Chain Reaction,
pubmed-meshheading:10187764-RNA, Messenger,
pubmed-meshheading:10187764-Tumor Cells, Cultured,
pubmed-meshheading:10187764-Tyrosine,
pubmed-meshheading:10187764-Vanadates
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| pubmed:year |
1999
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| pubmed:articleTitle |
Rapid inactivation of NOS-I by lipopolysaccharide plus interferon-gamma-induced tyrosine phosphorylation.
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| pubmed:affiliation |
Department of Biology, University of Rome, ROMA TRE, Viale Marconi 446, I-00146 Rome, Italy.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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