scholarly journals Sugars and cell adhesion: The role of ST6GalNAc1 in prostate cancer progression

2016 ◽  
Keyword(s):  
Prostate Cancer ◽  
Cell Adhesion ◽  
Cancer Progression ◽  
Prostate Cancer Progression

167: Role of trefoil factor-3 peptide (TFF3) in prostate cancer progression

2014 ◽  
Vol 50 ◽  
pp. S37 ◽  
Author(s):  
M. Nowak ◽  
C. Merz ◽  
A. Von Maessenhausen ◽  
W. Vogel ◽  
D. Boehm ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cancer Progression ◽  
Prostate Cancer Progression ◽  
Trefoil Factor ◽  
Trefoil Factor 3

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 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.

Vitamin D and prostate cancer: The role of membrane initiated signaling pathways in prostate cancer progression

2010 ◽  
Vol 121 (1-2) ◽  
pp. 413-416 ◽  
Author(s):  
Sandra Karlsson ◽  
Josefin Olausson ◽  
Dan Lundh ◽  
Peter Sögård ◽  
Abul Mandal ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Vitamin D ◽  
Signaling Pathways ◽  
Cancer Progression ◽  
Prostate Cancer Progression
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