scholarly journals Protein Kinase G-Iα Hyperactivation and VASP Phosphorylation in Promoting Ovarian Cancer Cell Migration and Platinum Resistance

10.5772/53468 ◽  
2013 ◽  
Author(s):  
Janica C. ◽  
Ronald R.
Keyword(s):  
Ovarian Cancer ◽  
Cell Migration ◽  
Protein Kinase ◽  
Cancer Cell ◽  
Ovarian Cancer Cell ◽  
Protein Kinase G ◽  
Platinum Resistance ◽  
Cancer Cell Migration ◽  
Vasp Phosphorylation

scholarly journals Gonadotropin-induced ovarian cancer cell migration and proliferation require extracellular signal-regulated kinase 1/2 activation regulated by calcium and protein kinase Cδ

2010 ◽  
Vol 17 (2) ◽  
pp. 335-349 ◽  
Author(s):  
Inga Mertens-Walker ◽  
Christine Bolitho ◽  
Robert C Baxter ◽  
Deborah J Marsh
Keyword(s):  
Ovarian Cancer ◽  
Cell Migration ◽  
Protein Kinase ◽  
Cancer Cell ◽  
Ovarian Cancer Cell ◽  
Cancer Cell Migration ◽  
Extracellular Signal Regulated Kinase ◽  
Extracellular Signal ◽  
Gf 109203X ◽  
Cell Migration And Proliferation

The gonadotropin hypothesis proposes that elevated serum gonadotropin levels may increase the risk of epithelial ovarian cancer (EOC). We have studied the effect of treating EOC cell lines (OV207 and OVCAR-3) with FSH or LH. Both gonadotropins activated the mitogen-activated protein kinase (MAPK)/extracellular signal-regulated kinase 1/2 (ERK1/2) pathway and increased cell migration that was inhibited by the MAPK 1 inhibitor PD98059. Both extra- and intracellular calcium ion signalling were implicated in gonadotropin-induced ERK1/2 activation as treatment with either the calcium chelator EGTA or an inhibitor of intracellular calcium release, dantrolene, inhibited gonadotropin-induced ERK1/2 activation. Verapamil was also inhibitory, indicating that gonadotropins activate calcium influx via L-type voltage-dependent calcium channels. The cAMP/protein kinase A (PKA) pathway was not involved in the mediation of gonadotropin action in these cells as gonadotropins did not increase intracellular cAMP formation and inhibition of PKA did not affect gonadotropin-induced phosphorylation of ERK1/2. Activation of ERK1/2 was inhibited by the protein kinase C (PKC) inhibitor GF 109203X as well as by the PKCδ inhibitor rottlerin, and downregulation of PKCδ was inhibited by small interfering RNA (siRNA), highlighting the importance of PKCδ in the gonadotropin signalling cascade. Furthermore, in addition to inhibition by PD98059, gonadotropin-induced ovarian cancer cell migration was also inhibited by verapamil, GF 109203X and rottlerin. Similarly, gonadotropin-induced proliferation was inhibited by PD98059, verapamil, GF 109203X and PKCδ siRNA. Taken together, these results demonstrate that gonadotropins induce both ovarian cancer cell migration and proliferation by activation of ERK1/2 signalling in a calcium- and PKCδ-dependent manner.

A synthetic peptide inhibits human ovarian cancer cell motility

RSC Advances ◽  
2015 ◽  
Vol 5 (102) ◽  
pp. 83801-83808 ◽  
Author(s):  
Yan Wei ◽  
Di Huang ◽  
Kaiqun Wang ◽  
Jingjing Du ◽  
Yinchun Hu
Keyword(s):  
Ovarian Cancer ◽  
Cell Migration ◽  
Cancer Cell ◽  
Synthetic Peptide ◽  
Ovarian Cancer Cell ◽  
Human Ovarian Cancer ◽  
Cancer Cell Migration ◽  
Human Ovarian Cancer Cell ◽  
Cancer Cell Motility ◽  
Small G Protein

The synthetic SV-peptide inhibits cancer cell migration through inhibition of FAK–Rho signaling and influences the small G protein family expression.

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