scholarly journals Statins induce cell apoptosis through a modulation of AKT/FOXO1 pathway in prostate cancer cells

2019 ◽  
Vol Volume 11 ◽  
pp. 7231-7242 ◽  
Author(s):  
Jun-Li Deng ◽  
Rui Zhang ◽  
Ying Zeng ◽  
Yuan-Shan Zhu ◽  
Guo Wang
Keyword(s):  
Prostate Cancer ◽  
Cancer Cells ◽  
Cell Apoptosis ◽  
Prostate Cancer Cells ◽  
Induce Cell Apoptosis

794 MICRORNA-204 PROMOTES CELL APOPTOSIS BY TARGETING TO BCL-2 IN BLADDER AND PROSTATE CANCER CELLS

2013 ◽  
Vol 189 (4S) ◽  
Author(s):  
Thomas Hwang ◽  
Yi-Chia Lin ◽  
Te-Fu Tsai ◽  
Hung-En Chen ◽  
Kuang-Yu Chou ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cancer Cells ◽  
Cell Apoptosis ◽  
Prostate Cancer Cells

Gambogic Acid Induces Cell Apoptosis and Inhibits MAPK Pathway in PTEN−/−/p53−/− Prostate Cancer Cells In Vitro and Ex Vivo

2017 ◽  
Vol 24 (2) ◽  
pp. 109-116 ◽  
Author(s):  
Hong Pan ◽  
Li-yuan Lu ◽  
Xue-qian Wang ◽  
Bin-xue Li ◽  
Kathleen Kelly ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cancer Cells ◽  
Cell Apoptosis ◽  
Ex Vivo ◽  
Mapk Pathway ◽  
Gambogic Acid ◽  
Prostate Cancer Cells

KLF9, a transcription factor induced in flutamide-caused cell apoptosis, inhibits AKT activation and suppresses tumor growth of prostate cancer cells

The Prostate ◽  
2014 ◽  
Vol 74 (9) ◽  
pp. 946-958 ◽  
Author(s):  
Pengliang Shen ◽  
Jiabin Sun ◽  
Guiqin Xu ◽  
Li Zhang ◽  
Zhaojuan Yang ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Transcription Factor ◽  
Tumor Growth ◽  
Cancer Cells ◽  
Cell Apoptosis ◽  
Prostate Cancer Cells ◽  
Akt Activation

scholarly journals Upregulation of Circular RNA Itchy E3 Ubiquitin Protein Ligase Inhibits Cell Proliferation and Promotes Cell Apoptosis Through Targeting MiR-197 in Prostate Cancer

2019 ◽  
Vol 18 ◽  
pp. 153303381988686 ◽  
Author(s):  
Yuan Yuan ◽  
Xiaogang Chen ◽  
Enying Huang
Keyword(s):  
Prostate Cancer ◽  
Cell Proliferation ◽  
Western Blot ◽  
Cancer Cells ◽  
Cell Apoptosis ◽  
Circular Rna ◽  
Micro Rna ◽  
Prostate Cancer Cells ◽  
Ubiquitin Protein Ligase ◽  
Proliferation And Apoptosis

Objective: This study aimed to investigate the effect of circular RNA itchy E3 ubiquitin protein ligase on cell proliferation and apoptosis and to explore its target micro-RNAs in prostate cancer cells. Methods: Circular RNA itchy E3 ubiquitin protein ligase expression in human prostate cancer cells and normal prostate epithelial cells was determined by real time-quantitative polymerase chain reaction assay. Circular RNA itchy E3 ubiquitin protein ligase overexpression plasmids (circular RNA itchy E3 ubiquitin protein ligase(+) group and control overexpression plasmids group were transfected with PC-3 cells. Rescue experiment was performed by transfection of circular RNA itchy E3 ubiquitin protein ligase overexpression and micro-197 overexpression plasmids (circular RNA itchy E3 ubiquitin protein ligase overexpression plasmids/micro RNA (+) group) into PC-3 cells. Cell Counting Kit-8 and annexin V/propidium iodide assays were conducted to evaluate cell proliferation and apoptosis, respectively. Western blot was performed to determine the expressions of apoptotic-related markers. Results: Circular RNA itchy E3 ubiquitin protein ligase expression was decreased in DU 145, 22RV1, VCaP, and PC-3 cells compared to RWPE cells. In PC-3 cells, cell proliferation rate was reduced in circular RNA itchy E3 ubiquitin protein ligase overexpression plasmids group compared to control overexpression plasmids group at 48 hours and 72 hours. Cell apoptosis rate was elevated in circular RNA itchy E3 ubiquitin protein ligase overexpression plasmids group compared to control overexpression plasmids group at 48 hours, and Western blot showed the similar results. Micro RNA-197 but not micro RNA-31 or micro RNA-432 was the target micro-RNA of circular RNA itchy E3 ubiquitin protein ligase. In rescue experiments, cell proliferation rate was elevated, but apoptosis rate was reduced in circular RNA itchy E3 ubiquitin protein ligase overexpression plasmids/micro RNA (+) group compared to circular RNA itchy E3 ubiquitin protein ligase overexpression plasmids group, indicating that circular RNA itchy E3 ubiquitin protein ligase upregulation inhibited cell proliferation but promoted apoptosis through downregulating micro RNA-197. Conclusion: Circular RNA itchy E3 ubiquitin protein ligase upregulation suppresses cell proliferation but promotes apoptosis through targeting micro RNA-197 in prostate cancer. Our study may provide a new insight for the treatment of prostate cancer.

scholarly journals Upregulation of PAWR by small activating RNAs induces cell apoptosis in human prostate cancer cells

2016 ◽  
Vol 35 (4) ◽  
pp. 2487-2493 ◽  
Author(s):  
KAI YANG ◽  
JIE SHEN ◽  
SHAN-WEN CHEN ◽  
JIE QIN ◽  
XIANG-YI ZHENG ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cancer Cells ◽  
Cell Apoptosis ◽  
Human Prostate ◽  
Human Prostate Cancer ◽  
Prostate Cancer Cells

Dihydroartemisinin induces cell apoptosis through repression of UHRF1 in prostate cancer cells

2021 ◽  
Vol Publish Ahead of Print ◽  
Author(s):  
Tong Xia ◽  
Sihao Liu ◽  
Ge Xu ◽  
Siji Zhou ◽  
Ziguo Luo
Keyword(s):  
Prostate Cancer ◽  
Cancer Cells ◽  
Cell Apoptosis ◽  
Prostate Cancer Cells

scholarly journals Salen-Mn compounds induces cell apoptosis in human prostate cancer cells through promoting AMPK activity and cell autophagy

Oncotarget ◽  
2017 ◽  
Vol 8 (49) ◽  
pp. 86277-86286 ◽  
Author(s):  
Xiaoshuang Tang ◽  
Jing Jia ◽  
Feng Li ◽  
Wei Liu ◽  
Chao Yang ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cancer Cells ◽  
Cell Apoptosis ◽  
Human Prostate ◽  
Human Prostate Cancer ◽  
Prostate Cancer Cells ◽  
Ampk Activity

scholarly journals AKT-Independent Protection of Prostate Cancer Cells from Apoptosis Mediated through Complex Formation between the Androgen Receptor and FKHR

2003 ◽  
Vol 23 (1) ◽  
pp. 104-118 ◽  
Author(s):  
Pengfei Li ◽  
Heehyoung Lee ◽  
Shaodong Guo ◽  
Terry G. Unterman ◽  
Guido Jenster ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Androgen Receptor ◽  
Cell Survival ◽  
Cancer Cells ◽  
Cancer Cell ◽  
Cell Apoptosis ◽  
Prostate Cancer Cell ◽  
Transcriptional Analysis ◽  
Prostate Cancer Cells ◽  
Amino Terminal

ABSTRACT Recent studies suggested that the protection of cell apoptosis by AKT involves phosphorylation and inhibition of FKHR and related FOXO forkhead transcription factors and that androgens provide an AKT-independent cell survival signal in prostate cancer cells. Here, we report receptor-dependent repression of FKHR function by androgens in prostate cancer cells. Transcriptional analysis demonstrated that activation of the androgen receptor caused an inhibition of both wild-type FKHR and a mutant in which all three known AKT sites were mutated to alanines, showing that the repression is AKT independent. In vivo and in vitro coprecipitation studies demonstrated that the repression is mediated through protein-protein interaction between FKHR and the androgen receptor. Mapping analysis localized the interacting domains to the carboxyl terminus between amino acids 350 and 655 of FKHR and to the amino-terminal A/B region and the ligand binding domain of the receptor. Further analysis demonstrated that the activated androgen receptor blocked FKHR's DNA binding activity and impaired its ability to induce Fas ligand expression and prostate cancer cell apoptosis and cell cycle arrest. These studies identify a new mechanism for androgen-mediated prostate cancer cell survival that appears to be independent of the activity of the receptor on androgen response element-mediated transcription and establish FKHR and related FOXO forkhead proteins as important nuclear targets for both AKT-dependent and -independent survival signals in prostate cancer cells.

scholarly journals Bloom Syndrome Protein Activates AKT and PRAS40 in Prostate Cancer Cells

2019 ◽  
Vol 2019 ◽  
pp. 1-19 ◽  
Author(s):  
Kun Chen ◽  
Houqiang Xu ◽  
Jiafu Zhao
Keyword(s):  
Prostate Cancer ◽  
Cancer Cells ◽  
Cell Apoptosis ◽  
Tumor Development ◽  
Bloom Syndrome ◽  
Therapeutic Interventions ◽  
Antibody Array ◽  
Prostate Cancer Cells ◽  
Molecular Events ◽  
Syndrome Protein

Purpose. Prostate cancer (PC) is a common malignant tumor and a leading cause of cancer-related death in men worldwide. In order to design new therapeutic interventions for PC, an understanding of the molecular events underlying PC tumorigenesis is required. Bloom syndrome protein (BLM) is a RecQ-like helicase, which helps maintain genetic stability. BLM dysfunction has been implicated in tumor development, most recently during PC tumorigenesis. However, the molecular basis for BLM-induced PC progression remains poorly characterized. In this study, we investigated whether BLM modulates the phosphorylation of an array of prooncogenic signaling pathways to promote PC progression. Methods. We analyzed differentially expressed proteins (DEPs) using iTRAQ technology. Site-directed knockout of BLM in PC-3 prostate cancer cells was performed using CRISPR/Cas9-mediated homologous recombination gene editing to confirm the effects of BLM on DEPs. PathScan® Antibody Array Kits were used to analyze the phosphorylation of nodal proteins in PC tissue. Immunohistochemistry and automated western blot (WES) analyses were used to validate these findings. Results. We found that silencing BLM in PC-3 cells significantly reduced their proliferative capacity. In addition, BLM downregulation significantly reduced levels of phosphorylated protein kinase B (AKT (Ser473)) and proline-rich AKT substrate of 40 kDa (PRAS40 (Thr246)), and this was accompanied by enhanced ROS (reactive oxygen species) levels. In addition, we found that AKT and PRAS40 inhibition reduced BLM, increased ROS levels, and induced PC cell apoptosis. Conclusions. We demonstrated that BLM activates AKT and PRAS40 to promote PC cell proliferation and survival. We further propose that ROS act in concert with BLM to facilitate PC oncogenesis, potentially via further enhancing AKT signaling and downregulating PTEN expression. Importantly, inhibiting the BLM-AKT-PRAS40 axis induced PC cell apoptosis. Thus, we highlight new avenues for novel anti-PC treatments.

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