Tumor necrosis factor-α plus actinomycin D-induced apoptosis of L929 cells is prevented by nitric oxide

Surgery Today ◽  
1999 ◽  
Vol 29 (10) ◽  
pp. 1059-1067 ◽  
Author(s):  
Shigeru Hakoda ◽  
Hiroyasu Ishikura ◽  
Naoshi Takeyama ◽  
Takaya Tanaka
Keyword(s):  
Nitric Oxide ◽  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Actinomycin D ◽  
L929 Cells ◽  
Induced Apoptosis ◽  
Factor Α ◽  
Necrosis Factor

Targeting Nitric Oxide (NO) Deliveryin Vivo. Design of a Liver-Selective NO Donor Prodrug That Blocks Tumor Necrosis Factor-α-Induced Apoptosis and Toxicity in the Liver

1997 ◽  
Vol 40 (13) ◽  
pp. 1947-1954 ◽  
Author(s):  
Joseph E. Saavedra ◽  
Timothy R. Billiar ◽  
Debra L. Williams ◽  
Young-Myeong Kim ◽  
Simon C. Watkins ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
No Donor ◽  
Induced Apoptosis ◽  
Factor Α ◽  
Necrosis Factor

scholarly journals Tumor Necrosis Factor-α Increases ATP Content in Metabolically Inhibited L929 Cells Preceding Cell Death

1997 ◽  
Vol 272 (48) ◽  
pp. 30167-30177 ◽  
Author(s):  
José A. Sánchez-Alcázar ◽  
Jesús Ruı́z-Cabello ◽  
Inmaculada Hernández-Muñoz ◽  
Pilar Sánchez Pobre ◽  
Paz de la Torre ◽  
...  
Keyword(s):  
Cell Death ◽  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Atp Content ◽  
L929 Cells ◽  
Factor Α ◽  
Necrosis Factor ◽  
Preceding Cell

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.

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