scholarly journals Puerarin prevents tumor necrosis factor-α-induced apoptosis of PC12 cells via activation of the PI3K/Akt signaling pathway

2017 ◽  
Vol 14 (1) ◽  
pp. 813-818 ◽  
Author(s):  
Feng Liang ◽  
Shenggao Xie
Keyword(s):  
Tumor Necrosis Factor ◽  
Signaling Pathway ◽  
Pc12 Cells ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Akt Signaling ◽  
Akt Signaling Pathway ◽  
Induced Apoptosis ◽  
Factor Α ◽  
Necrosis Factor

Inhibition of the PI3K-Akt Signaling Pathway Reduces Tumor Necrosis Factor-α Production in Response to Titanium Particles in Vitro

2007 ◽  
Vol 89 (5) ◽  
pp. 1019-1027 ◽  
Author(s):  
Matthew V. Smith ◽  
Michael J. Lee ◽  
Andrew S. Islam ◽  
Jacqueline L. Rohrer ◽  
Victor M. Goldberg ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Signaling Pathway ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Akt Signaling ◽  
Akt Signaling Pathway ◽  
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.

Influence of cytokines tumor necrosis factor-α and interferon-γ on signaling cascades associated with apoptosis in rat PC12 cells

2001 ◽  
Vol 316 (3) ◽  
pp. 157-160 ◽  
Author(s):  
Christiane Enzinger ◽  
Barbara Wirleitner ◽  
Günther Böck ◽  
Gabriele Baier-Bitterlich ◽  
Dietmar Fuchs
Keyword(s):  
Tumor Necrosis Factor ◽  
Pc12 Cells ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Interferon Γ ◽  
Signaling Cascades ◽  
Factor Α ◽  
Necrosis Factor

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
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