scholarly journals 2-Methoxy-5-Amino-N-Hydroxybenzamide Sensitizes Colon Cancer Cells to TRAIL-Induced Apoptosis by Regulating Death Receptor 5 and Survivin Expression

2011 ◽  
Vol 10 (10) ◽  
pp. 1969-1981 ◽  
Author(s):  
Carmine Stolfi ◽  
Roberta Caruso ◽  
Eleonora Franzè ◽  
Angelamaria Rizzo ◽  
Angela Rotondi ◽  
...  
2012 ◽  
Vol 29 (2) ◽  
pp. 474-480 ◽  
Author(s):  
SAN-YUAN TANG ◽  
MEI-ZUO ZHONG ◽  
GUANG-JIN YUAN ◽  
SU-PING HOU ◽  
LEI-LAN YIN ◽  
...  

2011 ◽  
Vol 301 (2) ◽  
pp. 193-202 ◽  
Author(s):  
C. Lepage ◽  
D.Y. Léger ◽  
J. Bertrand ◽  
F. Martin ◽  
J.L. Beneytout ◽  
...  

2014 ◽  
Vol 4 (1) ◽  
Author(s):  
Mano Horinaka ◽  
Tatsushi Yoshida ◽  
Mitsuhiro Tomosugi ◽  
Shusuke Yasuda ◽  
Yoshihiro Sowa ◽  
...  

Cancers ◽  
2020 ◽  
Vol 12 (9) ◽  
pp. 2514
Author(s):  
Xinyu Zhou ◽  
Sietske N. Zijlstra ◽  
Abel Soto-Gamez ◽  
Rita Setroikromo ◽  
Wim J. Quax

Artemisinin derivatives, widely known as commercial anti-malaria drugs, may also have huge potential in treating cancer cells. It has been reported that artemisinin derivatives can overcome resistance to tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in liver and cervical cancer cells. In our study, we demonstrated that artesunate (ATS) and dihydroartemisinin (DHA) are more efficient in killing colon cancer cells compared to artemisinin (ART). ATS/DHA induces the expression of DR5 in a P53 dependent manner in HCT116 and DLD-1 cells. Both ATS and DHA overcome the resistance to DHER-induced apoptosis in HCT116, mainly through upregulating death receptor 5 (DR5). We also demonstrate that DHA sensitizes HCT116 cells to DHER-induced apoptosis via P53 regulated DR5 expression in P53 knockdown assays. Nevertheless, a lower effect was observed in DLD-1 cells, which has a single Ser241Phe mutation in the P53 DNA binding domain. Thus, the status of P53 could be one of the determinants of TRAIL resistance in some cancer cells. Finally, the combination treatment of DHA and the TRAIL variant DHER increases cell death in 3D colon cancer spheroid models, which shows its potential as a novel therapy.


2010 ◽  
Vol 285 (46) ◽  
pp. 35418-35427 ◽  
Author(s):  
Bokyung Sung ◽  
Jayaraj Ravindran ◽  
Sahdeo Prasad ◽  
Manoj K. Pandey ◽  
Bharat B. Aggarwal

FEBS Journal ◽  
2019 ◽  
Vol 286 (3) ◽  
pp. 555-571 ◽  
Author(s):  
Baojie Zhang ◽  
Ingrid A. M. Roosmalen ◽  
Carlos R. Reis ◽  
Rita Setroikromo ◽  
Wim J. Quax

2009 ◽  
Vol 296 (5) ◽  
pp. G1060-G1068 ◽  
Author(s):  
Do Y. Lim ◽  
Jung Han Yoon Park

Fisetin, or 3,3′,4′,7-tetrahydroxyflavone, is present in fruits and vegetables and has been previously reported to inhibit the proliferation of a variety of cancer cells (Lu X, Jung J, Cho HJ, Lim do Y, Lee HS, Chun HS, Kwon DY, Park JH. J Nutr 135: 2884–2890, 2005). We have demonstrated in a previous work that 20–60 μmol/l fisetin inhibits cyclin-dependent kinase activities resulting in cell cycle arrest in HT-29 colon cancer cells. In the present study, we attempted to characterize the mechanisms by which fisetin induces apoptosis in HCT-116 cells. DNA condensations, cleavage of poly(ADP-ribose) polymerase (PARP), and cleavage of caspases 9, 7, and 3 were induced in HCT-116 cells treated with 5–20 μmol/l of fisetin. Fisetin induced a reduction in the protein levels of antiapoptotic Bcl-xL and Bcl-2 and an increase in the levels of proapoptotic Bak and Bim. Fisetin did not affect the Bax protein levels, but induced the mitochondrial translocation of this protein. Fisetin also enhanced the permeability of the mitochondrial membrane and induced the release of cytochrome c and Smac/Diablo. Additionally, fisetin caused an increase in the protein levels of cleaved caspase-8, Fas ligand, death receptor 5, and TNF-related apoptosis-inducing ligand, and the caspase-8 inhibitor Z-IETD-FMK suppressed fisetin-induced apoptosis and the activation of caspase-3. Furthermore, fisetin increases p53 protein levels, and the inhibition of p53 expression by small interference RNA resulted in a decrease in the fisetin-induced translocation of Bax to the mitochondria, release of mono- and oligonucleosome in the cytoplasm, and PARP cleavage. These results show that fisetin induces apoptosis in HCT-116 cells via the activation of the death receptor- and mitochondrial-dependent pathway and subsequent activation of the caspase cascade. The induction of p53 results in the translocation of Bax to the mitochondria, which contributes to fisetin-induced apoptosis in HCT-116 cells.


Biomedicines ◽  
2020 ◽  
Vol 8 (4) ◽  
pp. 84 ◽  
Author(s):  
Oh Sung Kwon ◽  
Ji Hoon Jung ◽  
Eun Ah Shin ◽  
Ji Eon Park ◽  
Woon Yi Park ◽  
...  

Though epigallocatechin-3-gallate (EGCG), a major compound of green tea, has anti-diabetes, anti-obesity, anti-inflammatory, and antitumor effects, the underlying antitumor molecular mechanism of EGCG was not fully understood so far. Here the sensitizing effect of EGCG to tumor-necrosis-factor-related apoptosis-inducing ligand (TRAIL) was examined in colorectal cancers. Cotreatment of EGCG and TRAIL synergistically enhanced cytotoxicity and sub G1 accumulation, increased the number of terminal deoxynucleotidyl transferase-dT-mediated dUTP nick end labelling (TUNEL)-positive cells in SW480 and HCT116 cells. Furthermore, this cotreatment promoted the cleavages of poly (adenosine diphosphate-ribose) polymerase (PARP) and induced caspase 8 activation compared to TRAIL or EGCG alone in SW480 and HCT116 cells. Of note, cotreatment of EGCG and TRAIL increased the expression of death receptor 5 (DR5) at protein and mRNA levels and also DR5 cell surface level in colon cancer cells. Conversely, depletion of DR5 reduced the apoptotic activity of cotreatment of EGCG and TRAIL to increase cytotoxicity, sub-G1 population and PARP cleavages in colon cancer cells. Overall, our findings provide evidence that EGCG can be a sensitizer of TRAIL via DR5 and caspase 8 mediated apoptosis in colorectal cancer cells.


2016 ◽  
Vol 291 (32) ◽  
pp. 16923-16923 ◽  
Author(s):  
Bokyung Sung ◽  
Jayaraj Ravindran ◽  
Sahdeo Prasad ◽  
Manoj K. Pandey ◽  
Bharat B. Aggarwal

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