| pubmed-article:11799106 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11799106 | lifeskim:mentions | umls-concept:C0038435 | lld:lifeskim |
| pubmed-article:11799106 | lifeskim:mentions | umls-concept:C0151686 | lld:lifeskim |
| pubmed-article:11799106 | lifeskim:mentions | umls-concept:C0012860 | lld:lifeskim |
| pubmed-article:11799106 | lifeskim:mentions | umls-concept:C0040690 | lld:lifeskim |
| pubmed-article:11799106 | lifeskim:mentions | umls-concept:C0242184 | lld:lifeskim |
| pubmed-article:11799106 | lifeskim:mentions | umls-concept:C1704632 | lld:lifeskim |
| pubmed-article:11799106 | lifeskim:mentions | umls-concept:C0871261 | lld:lifeskim |
| pubmed-article:11799106 | lifeskim:mentions | umls-concept:C0079419 | lld:lifeskim |
| pubmed-article:11799106 | lifeskim:mentions | umls-concept:C2911692 | lld:lifeskim |
| pubmed-article:11799106 | lifeskim:mentions | umls-concept:C1706817 | lld:lifeskim |
| pubmed-article:11799106 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
| pubmed-article:11799106 | lifeskim:mentions | umls-concept:C1516044 | lld:lifeskim |
| pubmed-article:11799106 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:11799106 | pubmed:dateCreated | 2002-3-18 | lld:pubmed |
| pubmed-article:11799106 | pubmed:abstractText | Transforming growth factor beta (TGF-beta1) suppresses the growth of mink lung Mv1Lu epithelial cells, whereas testicular hyaluronidase abolishes the growth inhibition. Exposure of Mv1Lu cells to TGF-beta1 rapidly resulted in down-regulation of cytosolic IkappaBalpha and hyaluronidase prevented this effect, suggesting a possible role of IkappaBalpha in the growth regulation. Ectopic expression of wild-type and dominant negative IkappaBalpha prevented TGF-beta1-mediated growth suppression. Nonetheless, the blocking effect of IkappaBalpha is not related to regulation of NF-kappaB function by its N-terminal ankyrin-repeat region (amino acids 1-243). Removal of the PEST (proline-glutamic acid-serine-threonine) domain-containing C terminus (amino acids 244-314) abolished the IkappaBalpha function, and the C terminus alone blocked the TGF-beta1 growth-inhibitory effect. Co-immunoprecipitation by anti-p53 antibody using Mv1Lu and other types of cells, as well as rat liver and spleen, revealed that a portion of cytosolic IkappaBalpha physically interacted with p53. In contrast, Mdm2, an inhibitor of p53, was barely detectable in the immunoprecipitates. The cytosolic p53 x IkappaBalpha complex rapidly dissociated in response to apoptotic stress, etoposide- and UV-mediated DNA damage, hypoxia, and TGF-beta1-mediated growth suppression. Also, a rapid increase in the formation of the nuclear p53 x IkappaBalpha complex was observed during exposure to etoposide and UV. In contrast, TGF-beta1-mediated promotion of fibroblast growth failed to mediate p53 x IkappaBalpha dissociation. Mapping by yeast two-hybrid showed that the non-ankyrin C terminus of IkappaBalpha physically interacted with the proline-rich region and a phosphorylation site, serine 46, in p53. Deletion of serine 46 or alteration of serine 46 to glycine abolished the p53 x IkappaBalpha interaction. Alteration to threonine retained the binding interaction, suggesting that serine 46 phosphorylation is involved in the p53 x IkappaBalpha complex formation. Functionally, enhancement of p53 apoptosis was observed when p53 and IkappaBalpha were transiently co-expressed in cells. Together, the IkappaBalpha x p53 complex plays an important role in responses involving growth regulation, apoptosis, and hypoxic stress. | lld:pubmed |
| pubmed-article:11799106 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11799106 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11799106 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11799106 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:11799106 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11799106 | pubmed:author | pubmed-author:ChangNan-Shan... | lld:pubmed |
| pubmed-article:11799106 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11799106 | pubmed:day | 22 | lld:pubmed |
| pubmed-article:11799106 | pubmed:volume | 277 | lld:pubmed |
| pubmed-article:11799106 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11799106 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11799106 | pubmed:pagination | 10323-31 | lld:pubmed |
| pubmed-article:11799106 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:11799106 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11799106 | pubmed:articleTitle | The non-ankyrin C terminus of Ikappa Balpha physically interacts with p53 in vivo and dissociates in response to apoptotic stress, hypoxia, DNA damage, and transforming growth factor-beta 1-mediated growth suppression. | lld:pubmed |
| pubmed-article:11799106 | pubmed:affiliation | Guthrie Research Institute, Laboratory of Molecular Immunology, Guthrie Medical Center, Sayre, Pennsylvania, 18840, USA. nschang@inet.guthrie.org | lld:pubmed |
| pubmed-article:11799106 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11799106 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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