| pubmed-article:8612692 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8612692 | lifeskim:mentions | umls-concept:C0596402 | lld:lifeskim |
| pubmed-article:8612692 | lifeskim:mentions | umls-concept:C1518440 | lld:lifeskim |
| pubmed-article:8612692 | lifeskim:mentions | umls-concept:C1456820 | lld:lifeskim |
| pubmed-article:8612692 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:8612692 | lifeskim:mentions | umls-concept:C1523116 | lld:lifeskim |
| pubmed-article:8612692 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:8612692 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8612692 | pubmed:dateCreated | 1996-6-5 | lld:pubmed |
| pubmed-article:8612692 | pubmed:abstractText | The murine fibrosarcoma cell line WEHI 164 is well known for its susceptibility to tumor necrosis factor (TNFalpha). We have studied the activation of the transcription factor NF-kappaB when WEHI 164 cells are challenged with TNFalpha. NF-kappaB is retained in the cytoplasm of unchallenged cells by its inhibitor IkappaB-alpha. Upon cellular stimulation, IkappaB-alpha is functionally inactivated and NF-kappaB translocated to the nucleus. The extent of the cytotoxic effect and that of nuclear translocation of NF-kappaB show the same TNFalpha dependence. TNFalpha induces a rapid and transient activation of NF-kappaB in WEHI 164 cells which is followed by a second, long lasting phase in which the amount of NF-kappaB complex in the nucleus remains at about 50% of maximum. Upon TNFalpha treatment, IkappaB-alpha is rapidly degraded. However, newly synthesized IkappaB-alpha can be demonstrated later in the cell cytosol. A persistent nuclear localization of NF-kappaB is an obligatory step for the cytotoxic effect to take place. Thus, WEHI 164 cells treated with TNFalpha for up to 6 h can be rescued as long as NF-kappa relocalizes to the cytoplasm in its inactive form. On the other hand, TNFalpha treatments as short as 15 min cause the cytotoxic effect provided that NF-kappaB remains in the nucleus. The activation of NF-kappaB is controlled by both phosphorylation and proteolysis. The activation of NF-kappaB can be blocked by the cysteine protease inhibitor calpain inhibitor I and the serine protease inhibitor TPCK. Signal-induced phosphorylation of IkappaB-alpha does not lead to the dissociation of the inhibitor from NF-kappaB. Phosphorylation appears to regulate the inhibitory activity of IkappaB-alpha both positively and negatively. since inhibitors of protein kinases have opposite effects. Thus, treatment of cells with staurosporin induced a partial activation of NF-kappaB and was synergistic with TNFalpha induced activation. Calphostin C, on the other hand, can block the activation of NF-kappaB by TNFalpha, also blocking its proteolytic degradation. | lld:pubmed |
| pubmed-article:8612692 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8612692 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8612692 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8612692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8612692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8612692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8612692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8612692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8612692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8612692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8612692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8612692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8612692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8612692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8612692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8612692 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8612692 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:8612692 | pubmed:issn | 0014-4827 | lld:pubmed |
| pubmed-article:8612692 | pubmed:author | pubmed-author:BravoRR | lld:pubmed |
| pubmed-article:8612692 | pubmed:author | pubmed-author:RamosSS | lld:pubmed |
| pubmed-article:8612692 | pubmed:author | pubmed-author:LazoP SPS | lld:pubmed |
| pubmed-article:8612692 | pubmed:author | pubmed-author:SegadeFF | lld:pubmed |
| pubmed-article:8612692 | pubmed:author | pubmed-author:WrobelKK | lld:pubmed |
| pubmed-article:8612692 | pubmed:author | pubmed-author:ClaudioEE | lld:pubmed |
| pubmed-article:8612692 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8612692 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:8612692 | pubmed:volume | 224 | lld:pubmed |
| pubmed-article:8612692 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8612692 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8612692 | pubmed:pagination | 63-71 | lld:pubmed |
| pubmed-article:8612692 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:8612692 | pubmed:meshHeading | pubmed-meshheading:8612692-... | lld:pubmed |
| pubmed-article:8612692 | pubmed:meshHeading | pubmed-meshheading:8612692-... | lld:pubmed |
| pubmed-article:8612692 | pubmed:meshHeading | pubmed-meshheading:8612692-... | lld:pubmed |
| pubmed-article:8612692 | pubmed:meshHeading | pubmed-meshheading:8612692-... | lld:pubmed |
| pubmed-article:8612692 | pubmed:meshHeading | pubmed-meshheading:8612692-... | lld:pubmed |
| pubmed-article:8612692 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8612692 | pubmed:articleTitle | Molecular mechanisms of TNFalpha cytotoxicity: activation of NF-kappaB and nuclear translocation. | lld:pubmed |
| pubmed-article:8612692 | pubmed:affiliation | Departamento de Bioquimica y Biologia Molecular, Universidad de Oviedo,Spain. | lld:pubmed |
| pubmed-article:8612692 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8612692 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8612692 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8612692 | lld:pubmed |
