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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2-3
|
pubmed:dateCreated |
1992-4-13
|
pubmed:abstractText |
The mechanism by which interleukin-1 alpha (IL-1 alpha) activates NF-kappa B DNA-binding activity is not completely understood. While it is well established that protein kinase C can activate NF-kappa B, neither protein kinase C nor protein kinase A appears to be critical in the induction of NF-kappa B by IL-1 alpha. Since a number of growth factors signal via protein tyrosine kinase, in this study we examined a possible involvement of protein tyrosine kinase in the IL-1 alpha-induced NF-kappa B. The results showed that in the murine pre-B cell line 70Z/3 and in the murine T cell line EL-4 6.1 C10 IL-1 alpha-induced NF-kappa B was associated with transient increase in protein tyrosine kinase activity. Pre-treatment of these cell lines with herbimycin A, an inhibitor of tyrosine kinase activity, blocked the IL-1 alpha-enhanced protein tyrosine kinase activity and the IL-1 alpha-induced NF-kappa B DNA-binding activity. Herbimycin A at concentrations sufficient to block IL-1 alpha-induced NF-kappa B did not block the phorbol 12-myristate 13-acetate (PMA)-induced NF-kappa B. The data suggest that IL-1 alpha and PMA activate NF-kappa B by different pathways and that induction of NF-kappa B DNA-binding activity by IL-1 might be dependent on protein tyrosine phosphorylation.
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pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Benzoquinones,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Lactams, Macrocyclic,
http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Quinones,
http://linkedlifedata.com/resource/pubmed/chemical/herbimycin
|
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
0014-5793
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
24
|
pubmed:volume |
298
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
240-4
|
pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:1544454-Amino Acid Sequence,
pubmed-meshheading:1544454-B-Lymphocytes,
pubmed-meshheading:1544454-Base Sequence,
pubmed-meshheading:1544454-Benzoquinones,
pubmed-meshheading:1544454-DNA,
pubmed-meshheading:1544454-Enzyme Activation,
pubmed-meshheading:1544454-Humans,
pubmed-meshheading:1544454-Interleukin-1,
pubmed-meshheading:1544454-Kinetics,
pubmed-meshheading:1544454-Lactams, Macrocyclic,
pubmed-meshheading:1544454-Molecular Sequence Data,
pubmed-meshheading:1544454-NF-kappa B,
pubmed-meshheading:1544454-Protein-Tyrosine Kinases,
pubmed-meshheading:1544454-Quinones,
pubmed-meshheading:1544454-T-Lymphocytes,
pubmed-meshheading:1544454-Tumor Cells, Cultured
|
pubmed:year |
1992
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pubmed:articleTitle |
Herbimycin A blocks IL-1-induced NF-kappa B DNA-binding activity in lymphoid cell lines.
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pubmed:affiliation |
Department of Medicine, University of Washington, Seattle 98195.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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