scholarly journals Reduced glutathione depletion causes necrosis and sensitization to tumor necrosis factor-α-induced apoptosis in cultured mouse hepatocytes

Hepatology ◽  
2002 ◽  
Vol 36 (1) ◽  
pp. 55-64 ◽  
Author(s):  
Hidenari Nagai ◽  
Katsuhiko Matsumaru ◽  
Guoping Feng ◽  
Neil Kaplowitz
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Reduced Glutathione ◽  
Glutathione Depletion ◽  
Mouse Hepatocytes ◽  
Induced Apoptosis ◽  
Factor Α ◽  
Necrosis Factor

scholarly journals Estradiol Abrogates Apoptosis in Breast Cancer Cells through Inactivation of BAD: Ras-dependent Nongenomic Pathways Requiring Signaling through ERK and Akt

2004 ◽  
Vol 15 (7) ◽  
pp. 3266-3284 ◽  
Author(s):  
Romaine Ingrid Fernando ◽  
Jay Wimalasena
Keyword(s):  
Breast Cancer ◽  
Tumor Necrosis Factor ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Dominant Negative ◽  
Induced Apoptosis ◽  
Factor Α ◽  
Necrosis Factor

Estrogens such as 17-β estradiol (E2) play a critical role in sporadic breast cancer progression and decrease apoptosis in breast cancer cells. Our studies using estrogen receptor-positive MCF7 cells show that E2 abrogates apoptosis possibly through phosphorylation/inactivation of the proapoptotic protein BAD, which was rapidly phosphorylated at S112 and S136. Inhibition of BAD protein expression with specific antisense oligonucleotides reduced the effectiveness of tumor necrosis factor-α, H2O2, and serum starvation in causing apoptosis. Furthermore, the ability of E2 to prevent tumor necrosis factor-α-induced apoptosis was blocked by overexpression of the BAD S112A/S136A mutant but not the wild-type BAD. BAD S112A/S136A, which lacks phosphorylation sites for p90RSK1 and Akt, was not phosphorylated in response to E2 in vitro. E2 treatment rapidly activated phosphatidylinositol 3-kinase (PI-3K)/Akt and p90RSK1 to an extent similar to insulin-like growth factor-1 treatment. In agreement with p90RSK1 activation, E2 also rapidly activated extracellular signal-regulated kinase, and this activity was down-regulated by chemical and biological inhibition of PI-3K suggestive of cross talk between signaling pathways responding to E2. Dominant negative Ras blocked E2-induced BAD phosphorylation and the Raf-activator RasV12T35S induced BAD phosphorylation as well as enhanced E2-induced phosphorylation at S112. Chemical inhibition of PI-3K and mitogen-activated protein kinase kinase 1 inhibited E2-induced BAD phosphorylation at S112 and S136 and expression of dominant negative Ras-induced apoptosis in proliferating cells. Together, these data demonstrate a new nongenomic mechanism by which E2 prevents apoptosis.

scholarly journals Osteopontin Deficiency Suppresses Tumor Necrosis Factor-α–Induced Apoptosis in Chondrocytes

Cartilage ◽  
2012 ◽  
Vol 3 (1) ◽  
pp. 79-85 ◽  
Author(s):  
K. Yumoto ◽  
A. Nifuji ◽  
S.R. Rittling ◽  
Y. Tsuchiya ◽  
S. Kon ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Induced Apoptosis ◽  
Factor Α ◽  
Necrosis Factor

scholarly journals Mycobacterium bovis BCG promotes tumor cell survival from tumor necrosis factor-α-induced apoptosis

2014 ◽  
Vol 13 (1) ◽  
pp. 210 ◽  
Author(s):  
Sahana Holla ◽  
Devram Ghorpade ◽  
Vikas Singh ◽  
Kushagra Bansal ◽  
Kithiganahalli Balaji
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Cell ◽  
Cell Survival ◽  
Mycobacterium Bovis ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Tumor Cell Survival ◽  
Induced Apoptosis ◽  
Factor Α ◽  
Necrosis Factor

Tumor necrosis factor-α and ceramide induce cell death through different mechanisms in rat mesangial cells

1999 ◽  
Vol 276 (3) ◽  
pp. F390-F397 ◽  
Author(s):  
Yan-Lin Guo ◽  
Baobin Kang ◽  
Li-Jun Yang ◽  
John R. Williamson
Keyword(s):  
Cell Death ◽  
Protein Kinase ◽  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Mesangial Cells ◽  
Tnf Α ◽  
Induced Apoptosis ◽  
Factor Α ◽  
Necrosis Factor

It has been proposed that ceramide acts as a cellular messenger to mediate tumor necrosis factor-α (TNF-α)-induced apoptosis. Based on this hypothesis, it was postulated that resistance of some cells to TNF-α cytotoxicity was due to an insufficient production of ceramide on stimulation by TNF-α. The present study was initiated to investigate whether this was the case in mesangial cells, which normally are insensitive to TNF-α-induced apoptosis. Our results indicate that although C2ceramide was toxic to mesangial cells, the cell death it induced differed both morphologically and biochemically from that induced by TNF-α in the presence of cycloheximide (CHX). The most apparent effect of C2ceramide was to cause cells to swell, followed by disruption of the cell membrane. It is evident that C2ceramide caused cell death by necrosis, whereas TNF-α in the presence of CHX killed the cells by apoptosis. C2ceramide did not mimic the effects of TNF-α on the activation of c-Jun NH2-terminal protein kinase and nuclear factor-κB transcription factor. Although mitogen-activated protein kinase [extracellular signal-related kinase (ERK)] was activated by both C2ceramide and TNF-α, such activation appeared to be mediated by different mechanisms as judged from the kinetics of ERK activation. Furthermore, the cleavage of cytosolic phospholipase A2during cell death induced by C2ceramide and by TNF-α in the presence of CHX showed distinctive patterns. The present study provides evidence that apoptosis and necrosis use distinctive signaling machinery to cause cell death.

Protective Effect of N-Acetylcysteine in Tumor Necrosis Factor-α-Induced Apoptosis in U937 Cells: The Role of Mitochondria

1995 ◽  
Vol 220 (1) ◽  
pp. 232-240 ◽  
Author(s):  
Andrea Cossarizza ◽  
Claudio Franceschi ◽  
Daniela Monti ◽  
Stefano Salvioli ◽  
Enrica Bellesia ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Protective Effect ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
U937 Cells ◽  
Induced Apoptosis ◽  
Factor Α ◽  
Necrosis Factor
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