An Analysis of Gene Array Data Related to Cell Adhesion and Prostate Cancer

2002 ◽  
pp. 91-111 ◽  
Author(s):  
Borko D. Jovanovic ◽  
Shuguang Huang ◽  
Yuequin Liu ◽  
Karen N. Naguib ◽  
Raymond C. Bergan
Keyword(s):  
Prostate Cancer ◽  
Cell Adhesion ◽  
Gene Array ◽  
Array Data

scholarly journals Lipogenic signalling modulates prostate cancer cell adhesion and migration via modification of Rho GTPases

Oncogene ◽  
2020 ◽  
Vol 39 (18) ◽  
pp. 3666-3679 ◽  
Author(s):  
Mario De Piano ◽  
Valeria Manuelli ◽  
Giorgia Zadra ◽  
Jonathan Otte ◽  
Per-Henrik D. Edqvist ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cell Adhesion ◽  
Cancer Cell ◽  
Rho Gtpases ◽  
Prostate Cancer Cell ◽  
Cancer Cell Adhesion ◽  
Cell Adhesion And Migration ◽  
And Migration

scholarly journals Piperlongumine inhibits migration and proliferation of castration-resistant prostate cancer cells via triggering persistent DNA damage

2021 ◽  
Vol 21 (1) ◽  
Author(s):  
Ding-fang Zhang ◽  
Zhi-chun Yang ◽  
Jian-qiang Chen ◽  
Xiang-xiang Jin ◽  
Yin-da Qiu ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cell Proliferation ◽  
Dna Damage ◽  
Cell Adhesion ◽  
Anticancer Activity ◽  
Cancer Cells ◽  
Castration Resistant Prostate Cancer ◽  
Prostate Cancer Cells ◽  
Dna Damage And Repair ◽  
Castration Resistant

Abstract Background Metastatic castration-resistant prostate cancer (CRPC) is the leading cause of death among men diagnosed with prostate cancer. Piperlongumine (PL) is a novel potential anticancer agent that has been demonstrated to exhibit anticancer efficacy against prostate cancer cells. However, the effects of PL on DNA damage and repair against CRPC have remained unclear. The aim of this study was to further explore the anticancer activity and mechanisms of action of PL against CRPC in terms of DNA damage and repair processes. Methods The effect of PL on CRPC was evaluated by MTT assay, long-term cell proliferation, reactive oxygen species assay, western blot assay, flow cytometry assay (annexin V/PI staining), β-gal staining assay and DAPI staining assay. The capacity of PL to inhibit the invasion and migration of CRPC cells was assessed by scratch-wound assay, cell adhesion assay, transwell assay and immunofluorescence (IF) assay. The effect of PL on DNA damage and repair was determined via IF assay and comet assay. Results The results showed that PL exhibited stronger anticancer activity against CRPC compared to that of taxol, cisplatin (DDP), doxorubicin (Dox), or 5-Fluorouracil (5-FU), with fewer side effects in normal cells. Importantly, PL treatment significantly decreased cell adhesion to the extracellular matrix and inhibited the migration of CRPC cells through affecting the expression and distribution of focal adhesion kinase (FAK), leading to concentration-dependent inhibition of CRPC cell proliferation and concomitantly increased cell death. Moreover, PL treatment triggered persistent DNA damage and provoked strong DNA damage responses in CRPC cells. Conclusion Collectively, our findings demonstrate that PL potently inhibited proliferation, migration, and invasion of CRPC cells and that these potent anticancer effects were potentially achieved via triggering persistent DNA damage in CRPC cells.

Prostate Cancer Cell Adhesion to Bone Marrow Endothelium

2004 ◽  
Vol 64 (6) ◽  
pp. 2083-2089 ◽  
Author(s):  
Victor I. Romanov ◽  
Terry Whyard ◽  
Howard L. Adler ◽  
Wayne C. Waltzer ◽  
Stanley Zucker
Keyword(s):  
Prostate Cancer ◽  
Bone Marrow ◽  
Cell Adhesion ◽  
Cancer Cell ◽  
Prostate Cancer Cell ◽  
Cancer Cell Adhesion

The cadherin cell-cell adhesion pathway in prostate cancer progression

1997 ◽  
Vol 79 (S1) ◽  
pp. 37-43 ◽  
Author(s):  
R. PAUL ◽  
C.M. EWING ◽  
D.F. JARRARD ◽  
W.B. ISAACS
Keyword(s):  
Prostate Cancer ◽  
Cell Adhesion ◽  
Cancer Progression ◽  
Prostate Cancer Progression ◽  
Cell Cell

scholarly journals Validation of RNAi Silencing Efficiency Using Gene Array Data shows 18.5% Failure Rate across 429 Independent Experiments

2016 ◽  
Vol 5 ◽  
pp. e366 ◽  
Author(s):  
Gyöngyi Munkácsy ◽  
Zsófia Sztupinszki ◽  
Péter Herman ◽  
Bence Bán ◽  
Zsófia Pénzváltó ◽  
...  
Keyword(s):  
Failure Rate ◽  
Gene Array ◽  
Array Data ◽  
Rnai Silencing

scholarly journals Tumor protein D52 (isoform 3) contributes to prostate cancer cell growth via targeting nuclear factor-κB transactivation in LNCaP cells

Tumor Biology ◽  
2017 ◽  
Vol 39 (5) ◽  
pp. 101042831769838 ◽  
Author(s):  
Chandrashekhar Dasari ◽  
Dattu Prasad Yaghnam ◽  
Reinhard Walther ◽  
Ramesh Ummanni
Keyword(s):  
Prostate Cancer ◽  
Cell Adhesion ◽  
Cancer Progression ◽  
Underlying Mechanism ◽  
Nuclear Factor Κb ◽  
Tissue Inhibitor Of Metalloproteinase ◽  
Nuclear Factor ◽  
Prostate Cancer Progression ◽  
Lncap Cells ◽  
Cancer Cell Growth

Our previous study showed that TPD52 overexpression could increase migration and proliferation of LNCaP cells contributing to the development of prostate cancer. However, mechanism of TPD52 in prostate cancer initiation and progression remains elusive. In this study, we investigated the possible underlying mechanism of TPD52 in prostate cancer progression. In LNCaP cells, TPD52 expression was altered by transfecting with either EGFP-TPD52 or specific short hairpin RNA. Overexpression of TPD52 protected LNCaP cells from apoptosis through elevated anti-apoptotic proteins XIAP, Bcl-2, and Cyclin D1, whereas Bax was downregulated. Mechanistically, we found that TPD52 confers transactivation of nuclear factor-κB, thereby enhancing its target gene expression in LNCaP cells. TPD52 promotes LNCaP cell invasion probably via increased matrix metalloproteinase 9 expression and its activity while tissue inhibitor of metalloproteinase expression is significantly downregulated. Notably, TPD52 might be involved in cell adhesion, promoting tumor metastasis by inducing loss of E-cadherin, expression of vimentin and vascular cell adhesion molecule, and additionally activation of focal adhesion kinase. Furthermore, TPD52 directly interacts with nuclear factor-κB p65 (RelA) and promotes accumulation of phosphorylated nuclear factor-κB (p65)S536 that is directly linked with nuclear factor-κB transactivation. Indeed, depletion of TPD52 or inhibition of nuclear factor-κB in TPD52-positive cells inhibited secretion of tumor-related cytokines and contributes to the activation of STAT3, nuclear factor-κB, and Akt. Interestingly, in TPD52 overexpressing LNCaP cells, nuclear factor-κB inhibition prevented the autocrine/paracrine activation of STAT3. TPD52 activates STAT3 through ascertaining a cross talk between the nuclear factor-κB and the STAT3 signaling systems. Collectively, these results reveal mechanism by which TPD52 is associated with prostate cancer progression and highlight the approach for therapeutic targeting of TPD52 in prostate cancer.

Sign in / Sign up

Export Citation Format

Share Document