Tumor necrosis factor-α induces epithelial–mesenchymal transition of renal cell carcinoma cells via a nuclear factor kappa B-independent mechanism

2011 ◽  
Vol 236 (9) ◽  
pp. 1022-1029 ◽  
Author(s):  
Sheng-Tang Wu ◽  
Guang-Huan Sun ◽  
Chih-Ying Hsu ◽  
Chang-Shuo Huang ◽  
Yu-Hsin Wu ◽  
...  
Keyword(s):  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Nuclear Factor Kappa B ◽  
Epithelial Mesenchymal Transition ◽  
Carcinoma Cells ◽  
Nuclear Factor ◽  
Mesenchymal Transition ◽  
Independent Mechanism ◽  
Factor Α ◽  
Necrosis Factor

Tumor necrosis factor-α modulates epithelial mesenchymal transition mediators ZEB2 and S100A4 to promote cholangiocarcinoma progression

2014 ◽  
Vol 21 (9) ◽  
pp. 703-711 ◽  
Author(s):  
Anchalee Techasen ◽  
Nisana Namwat ◽  
Watcharin Loilome ◽  
Kassaporn Duangkumpha ◽  
Anucha Puapairoj ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Epithelial Mesenchymal Transition ◽  
Mesenchymal Transition ◽  
Factor Α ◽  
Necrosis Factor

Tumor necrosis factor-α (TNF-α) stimulates the epithelial–mesenchymal transition regulator Snail in cholangiocarcinoma

2012 ◽  
Vol 29 (5) ◽  
pp. 3083-3091 ◽  
Author(s):  
Anchalee Techasen ◽  
Nisana Namwat ◽  
Watcharin Loilome ◽  
Pornpan Bungkanjana ◽  
Narong Khuntikeo ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Epithelial Mesenchymal Transition ◽  
Mesenchymal Transition ◽  
Tnf Α ◽  
Factor Α ◽  
Necrosis Factor

scholarly journals NFκB and Caspase-3 Activity in Apoptotic Hepatocytes of Galactosamine-sensitized Mice Treated with TNFα

2002 ◽  
Vol 50 (12) ◽  
pp. 1599-1609 ◽  
Author(s):  
Dan Tapalaga ◽  
Gisa Tiegs ◽  
Sabine Angermüller
Keyword(s):  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Nuclear Factor Kappa B ◽  
Caspase 3 ◽  
Nuclear Fraction ◽  
Nuclear Factor ◽  
Factor Α ◽  
Transcription Factor Nfκb ◽  
Necrosis Factor ◽  
Control Samples

Tumor necrosis factor-α (TNFα) induces apoptosis in hepatocytes only under transcriptional arrest induced by galactosamine (GalN). In this study we demonstrated the shuttle of the transcription factor NFκB (nuclear factor-kappa B) in the liver tissue of mice within 30 min-4.5 hr hours after GalN/TNFα treatment. NFκB translocation from cytoplasm to the nucleus is initiated by its separation from the inhibitory IκB proteins which include lIκBα, IκBβ, and IκB∊. Thirty minutes after GalN/TNFα administration, NFκBp65 in hepatocellular nuclei becomes increasingly detectable and reaches its highest level after 2.5 hr. Then export back into cytoplasm begins but, surprisingly, approximately 30% of NFκB remains in the nuclear fraction and appears as an immunoprecipitate in the nuclei of apoptotic hepatocytes. Non-apoptotic hepatocytes do not show any reaction product in the nuclei 4.5 hr after treatment. Correspondingly, the amount of dissociated IκBβ decreases in the cytoplasm up to 2.5 hr and increases again afterwards, although it does not reach the level of the control samples. No evidence of IκBβ in the nuclei was found either immunocytochemically or biochemically. Caspase-3 activity, which is responsible for apoptosis, increases significantly after 3.5 hr. At that time, apoptotic hepatocytes can occasionally be observed and, 4.5 hr after GalN/TNFα treatment, constitute approximately 30% of the hepatocytes.

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