Oligophrenin-1 Is Associated with Cell Adhesion and Migration in Prostate Cancer

Pathobiology ◽  
2014 ◽  
Vol 81 (4) ◽  
pp. 190-198 ◽  
Author(s):  
Keisuke Goto ◽  
Naohide Oue ◽  
Tetsutaro Hayashi ◽  
Shunsuke Shinmei ◽  
Naoya Sakamoto ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cell Adhesion ◽  
Cell Adhesion And Migration ◽  
And Migration

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

Amygdalin Modulates Prostate Cancer Cell Adhesion and Migration In Vitro

2019 ◽  
Vol 72 (3) ◽  
pp. 528-537 ◽  
Author(s):  
Jens Mani ◽  
Jens Neuschäfer ◽  
Christian Resch ◽  
Jochen Rutz ◽  
Sebastian Maxeiner ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cell Adhesion ◽  
Cancer Cell ◽  
Prostate Cancer Cell ◽  
Cancer Cell Adhesion ◽  
Cell Adhesion And Migration ◽  
And Migration

scholarly journals CXCL12 Modulates Prostate Cancer Cell Adhesion by Altering the Levels or Activities ofβ1-Containing Integrins

2014 ◽  
Vol 2014 ◽  
pp. 1-11 ◽  
Author(s):  
Mehdi Dehghani ◽  
Sedigheh Kianpour ◽  
Ana Zangeneh ◽  
Zohreh Mostafavi-Pour
Keyword(s):  
Prostate Cancer ◽  
Cell Adhesion ◽  
Collagen I ◽  
Integrin Receptors ◽  
High Concentration ◽  
Kinase Activation ◽  
Potential Biomarker ◽  
Cell Adhesion And Migration ◽  
And Migration ◽  
Recombinant Fragments

The mechanisms by which prostate cancer (PCa) cell adhesion and migration are controlled during metastasis are not well understood. Here, we studied the effect of CXCL12 in PCa cell adhesion and spreading in DU145 and PC3 cell lines using as substrates collagen I, fibronectin (FN), and their recombinant fragments. CXCL12 treatment increasedβ1 integrin-dependent PC3 cell adhesion on FN which correlated with increased focal adhesion kinase activation. However neitherα5β1 norα4β1 subunits were involved in this adhesion. By contrast, CXCL12 decreased DU145 adhesion and spreading on FN by downregulatingα5 andβ1 integrin expression. To demonstrate the clinical relevance of CXCL12 in PCa, we measured CXCL12 levels in plasma by using ELISA and found that the chemokine is elevated in PCa patients when compared to controls. The high concentration of CXCL12 in patients suffering from PCa in comparison to those with benign disease or healthy individuals implicates CXCL12 as a potential biomarker for PCa. In addition these data show that CXCL12 may be crucial in controlling PCa cell adhesion on fibronectin and collagen I, possibly via crosstalk with integrin receptors and/or altering the expression levels of integrin subunits.

Differences in phosphatase modulation of α4 β1 and α5 β1 integrin-mediated adhesion and migration of B16F1 cells

1999 ◽  
Vol 77 (5) ◽  
pp. 409-420 ◽  
Author(s):  
Dolores Hangan-Steinman ◽  
Wai-chi Ho ◽  
Priti Shenoy ◽  
Bosco MC Chan ◽  
Vincent L Morris
Keyword(s):  
Cell Adhesion ◽  
Adhesive Strength ◽  
Cell Movement ◽  
Protein Tyrosine Phosphatases ◽  
Β1 Integrin ◽  
Phosphatase Inhibitors ◽  
Β1 Integrins ◽  
Cell Adhesion And Migration ◽  
And Migration ◽  
B16f1 Cell

It is well established that a biphasic relationship exists between the adhesive strength of β1 integrins and their ability to mediate cell movement. Thus, cell movement increases progressively with adhesive strength, but beyond a certain point of optimal interaction, cell movement is reduced with further increases in adhesive function. The interplay between the various kinase and phosphatase activities provides the balance in β1 integrin-mediated cell adhesion and migration. In the present study, the significance of protein tyrosine phosphatases (PTP) and ser/thr protein phosphatases (PP) in α4β1 and α5β1 integrin-mediated mouse melanoma B16F1 cell anchorage and migration on fibronectin was characterized using phosphatase inhibitors. At low fibronectin concentration, α5β1 functioned as the predominant receptor for cell movement; a role for α4β1 in B16F1 cell migration increased progressively with fibronectin concentration. Treatment of B16F1 cells with PTP inhibitors, sodium orthovanadate (Na3VO4) and phenylarsine oxide (PAO), or PP-1/2A inhibitor, okadaic acid (OA), abolished cell movement. Inhibition of cell movement by PAO and OA was associated by a reduction in the adhesive strength of α4β1 and α5β1. In contrast, treatment of B16F1 cells with Na3VO4 resulted in selective stimulation of the adhesive function of α5β1, but not α4β1. Therefore, our results demonstrate that (i) both PTP and PP-1/2A have roles in cell movement, (ii) modulation of cell movement by PTP and PP-1/2A may involve either a stimulation or reduction of β1 integrin adhesive strength, and (iii) distinct phosphatase-mediated signaling pathways for differential regulation of the various β1 integrins exist. Key words: phosphatases, integrins, cell movement, cell adhesion.

Sign in / Sign up

Export Citation Format

Share Document