Modulation of Uridine Phosphorylase Gene Expression by Tumor Necrosis Factor-α Enhances the Antiproliferative Activity of the Capecitabine Intermediate 5′-Deoxy-5-fluorouridine in Breast Cancer Cells

2006 ◽  
Vol 69 (4) ◽  
pp. 1389-1395 ◽  
Author(s):  
Laxiang Wan ◽  
Deliang Cao ◽  
Jianmin Zeng ◽  
Ruilan Yan ◽  
Giuseppe Pizzorno
Keyword(s):  
Breast Cancer ◽  
Gene Expression ◽  
Tumor Necrosis Factor ◽  
Antiproliferative Activity ◽  
Breast Cancer Cells ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Uridine Phosphorylase ◽  
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 Silver Nanoparticle-Coated Ethyl Cellulose Inhibits Tumor Necrosis Factor-α of Breast Cancer Cells

2021 ◽  
Vol Volume 15 ◽  
pp. 2035-2046
Author(s):  
Ahmed AH Abdellatif ◽  
Mansour Alsharidah ◽  
Osamah Al Rugaie ◽  
Hesham M Tawfeek ◽  
Nahla Sameh Tolba
Keyword(s):  
Breast Cancer ◽  
Tumor Necrosis Factor ◽  
Cancer Cells ◽  
Silver Nanoparticle ◽  
Ethyl Cellulose ◽  
Breast Cancer Cells ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Factor Α ◽  
Necrosis Factor

Aspirin Inhibits Tumor Necrosis Factor-α Gene Expression in Murine Tissue Macrophages

1997 ◽  
Vol 52 (3) ◽  
pp. 421-429 ◽  
Author(s):  
Rodney E. Shackelford ◽  
Paul B. Alford ◽  
Yan Xue ◽  
Sheau-Fung Thai ◽  
Dolph O. Adams ◽  
...  
Keyword(s):  
Gene Expression ◽  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Murine Tissue ◽  
Factor Α ◽  
Necrosis Factor
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