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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
25
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pubmed:dateCreated |
1995-1-11
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pubmed:abstractText |
The ubiquitous transcription factor NF-kappa B is regulated by its cytoplasmic inhibitor I kappa B. A variety of cellular stimuli cause the dissociation of NF-kappa B from I kappa B, allowing NF-kappa B to translocate to the nucleus and regulate gene expression. Although the activation of NF-kappa B in vivo is associated with the phosphorylation and degradation of I kappa B alpha, it has remained unclear how each of these events contributes to this process. Recently, studies utilizing protease inhibitors have suggested that the proteolysis of I kappa B alpha is a necessary event in the activation of NF-kappa B. We demonstrate in this study that these and an additional protease inhibitor also completely repress inducible phosphorylation of I kappa B alpha. This surprising result suggests a more complex role of proteases in NF-kappa B activation. In addition, data presented here indicate that many of these inhibitors also directly modify NF-kappa B and inhibit its DNA binding activity. Due to the pleiotropic effects of these protease inhibitors, it is difficult to conclude from their use how I kappa B alpha phosphorylation and degradation contribute to NF-kappa B activation. In the present study, a more direct approach demonstrates that phosphorylation of I kappa B alpha alone is not sufficient for NF-kappa B activation.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-1425669,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-1508666,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-1517230,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-1829648,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-1903539,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-1956402,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-2157987,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-2177654,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-2384149,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-2535672,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-2548081,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-2808367,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-3129195,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-3140380,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-3893537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-8087845,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-8096091,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-8108414,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-8164680,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-8188652,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-8255759,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-8262046,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-8278379,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-8319912,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-8334993,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-8371761,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-8449662,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-8460169,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-8497253,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-8505309,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7991551-942051
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
91
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11884-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7991551-Base Sequence,
pubmed-meshheading:7991551-DNA, Neoplasm,
pubmed-meshheading:7991551-DNA-Binding Proteins,
pubmed-meshheading:7991551-HeLa Cells,
pubmed-meshheading:7991551-Humans,
pubmed-meshheading:7991551-I-kappa B Proteins,
pubmed-meshheading:7991551-Molecular Sequence Data,
pubmed-meshheading:7991551-NF-kappa B,
pubmed-meshheading:7991551-Oligonucleotide Probes,
pubmed-meshheading:7991551-Phosphorylation,
pubmed-meshheading:7991551-Protease Inhibitors,
pubmed-meshheading:7991551-Protein Binding,
pubmed-meshheading:7991551-T-Lymphocytes,
pubmed-meshheading:7991551-Tumor Cells, Cultured
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pubmed:year |
1994
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pubmed:articleTitle |
Inducible phosphorylation of I kappa B alpha is not sufficient for its dissociation from NF-kappa B and is inhibited by protease inhibitors.
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pubmed:affiliation |
Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill 27599.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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