scholarly journals Characterizing the convergence of protein kinase CK2 and caspase-3 reveals isoform-specific phosphorylation of caspase-3 by CK2α′: implications for pathological roles of CK2 in promoting cancer cell survival

Oncotarget ◽  
2013 ◽  
Vol 4 (4) ◽  
pp. 560-571 ◽  
Author(s):  
Jacob P. Turowec ◽  
Greg Vilk ◽  
Michelle Gabriel ◽  
David W. Litchfield
Keyword(s):  
Protein Kinase ◽  
Cell Survival ◽  
Cancer Cell ◽  
Protein Kinase Ck2 ◽  
Caspase 3 ◽  
Cancer Cell Survival ◽  
Kinase Ck2

scholarly journals Targeting protein kinase CK2 suppresses bladder cancer cell survival via the glucose metabolic pathway

Oncotarget ◽  
2016 ◽  
Vol 7 (52) ◽  
pp. 87361-87372 ◽  
Author(s):  
Xiaolei Zhang ◽  
Xiao Yang ◽  
Chengdi Yang ◽  
Peng Li ◽  
Wenbo Yuan ◽  
...  
Keyword(s):  
Bladder Cancer ◽  
Protein Kinase ◽  
Cell Survival ◽  
Cancer Cell ◽  
Metabolic Pathway ◽  
Protein Kinase Ck2 ◽  
Bladder Cancer Cell ◽  
Cancer Cell Survival ◽  
Kinase Ck2

Protein kinase CK2 regulates prostate cancer cell migration and proliferation through phosphorylation of PRH/HHEX

2016 ◽  
Vol 61 ◽  
pp. S97
Author(s):  
E. Marcolino de Assis ◽  
Y. Hasan Siddiqui ◽  
R.M. Kershaw ◽  
E.H. Humphreys ◽  
S. Chaudhri ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cell Migration ◽  
Protein Kinase ◽  
Cancer Cell ◽  
Protein Kinase Ck2 ◽  
Prostate Cancer Cell ◽  
Cancer Cell Migration ◽  
Cell Migration And Proliferation ◽  
Kinase Ck2

scholarly journals Src Regulates Tyr20 Phosphorylation of Transferrin Receptor-1 and Potentiates Breast Cancer Cell Survival

2011 ◽  
Vol 286 (41) ◽  
pp. 35708-35715 ◽  
Author(s):  
Jinlong Jian ◽  
Qing Yang ◽  
Xi Huang
Keyword(s):  
Breast Cancer ◽  
Cell Survival ◽  
Cancer Cells ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Transferrin Receptor ◽  
Iron Uptake ◽  
Caspase 3 ◽  
Transferrin Receptor 1 ◽  
Cancer Cell Survival

Transferrin receptor 1 (TfR1) is a ubiquitous type II membrane receptor with 61 amino acids in the N-terminal cytoplasmic region. TfR1 is highly expressed in cancer cells, particularly under iron deficient conditions. Overexpression of TfR1 is thought to meet the increased requirement of iron uptake necessary for cell growth. In the present study, we used transferrin (Tf), a known ligand of TfR1, and gambogic acid (GA), an apoptosis-inducing agent and newly identified TfR1 ligand to investigate the signaling role of TfR1 in breast cancer cells. We found that GA but not Tf induced apoptosis in a TfR1-dependent manner in breast cancer MDA-MB-231 cells. Estrogen receptor-positive MCF-7 cells lack caspase-3 and were not responsive to GA treatment. GA activated the three major signaling pathways of the MAPK family, as well as caspase-3, -8, and Poly(ADP-ribose)polymerase apoptotic pathway. Interestingly, only Src inhibitor PP2 greatly sensitized the cells to GA-mediated apoptosis. Further investigations by confocal fluorescence microscopy and immunoprecipitation revealed that Src and TfR1 are constitutively bound. Using TfR1-deficient CHO TRVB cells, point mutation studies showed that Tyr20 within the 20YTRF23 motif of the cytoplasmic region of TfR1 is the phosphorylation site by Src. TfR1 Tyr20 phosphomutants were more sensitive to GA-mediated apoptosis. Our results indicate that, albeit its iron uptake function, TfR1 is a signaling molecule and tyrosine phosphorylation at position 20 by Src enhances anti-apoptosis and potentiates breast cancer cell survival.

scholarly journals CX-4945 Induces Methuosis in Cholangiocarcinoma Cell Lines by a CK2-Independent Mechanism

Cancers ◽  
2018 ◽  
Vol 10 (9) ◽  
pp. 283 ◽  
Author(s):  
Jomnarong Lertsuwan ◽  
Kornkamon Lertsuwan ◽  
Anyaporn Sawasdichai ◽  
Nathapol Tasnawijitwong ◽  
Ka Lee ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Cell Lines ◽  
Cancer Cell ◽  
Cell Invasion ◽  
Protein Kinase Ck2 ◽  
Extracellular Fluid ◽  
Multiple Cancer ◽  
Cholangiocarcinoma Cell ◽  
Kinase Ck2

Cholangiocarcinoma is a disease with a poor prognosis and increasing incidence and hence there is a pressing unmet clinical need for new adjuvant treatments. Protein kinase CK2 (previously casein kinase II) is a ubiquitously expressed protein kinase that is up-regulated in multiple cancer cell types. The inhibition of CK2 activity using CX-4945 (Silmitasertib) has been proposed as a novel treatment in multiple disease settings including cholangiocarcinoma. Here, we show that CX-4945 inhibited the proliferation of cholangiocarcinoma cell lines in vitro. Moreover, CX-4945 treatment induced the formation of cytosolic vacuoles in cholangiocarcinoma cell lines and other cancer cell lines. The vacuoles contained extracellular fluid and had neutral pH, features characteristic of methuosis. In contrast, simultaneous knockdown of both the α and α′ catalytic subunits of protein kinase CK2 using small interfering RNA (siRNA) had little or no effect on the proliferation of cholangiocarcinoma cell lines and failed to induce the vacuole formation. Surprisingly, low doses of CX-4945 increased the invasive properties of cholangiocarcinoma cells due to an upregulation of matrix metallopeptidase 7 (MMP-7), while the knockdown of CK2 inhibited cell invasion. Our data suggest that CX-4945 inhibits cell proliferation and induces cell death via CK2-independent pathways. Moreover, the increase in cell invasion brought about by CX-4945 treatment suggests that this drug might increase tumor invasion in clinical settings.

Protein kinase CK2 promotes cancer cell viability via up-regulation of cyclooxygenase-2 expression and enhanced prostaglandin E2 production

2011 ◽  
Vol 112 (11) ◽  
pp. 3167-3175 ◽  
Author(s):  
Roger Yefi ◽  
Daniela P. Ponce ◽  
Ignacio Niechi ◽  
Eduardo Silva ◽  
Pablo Cabello ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Prostaglandin E2 ◽  
Cell Viability ◽  
Cancer Cell ◽  
Protein Kinase Ck2 ◽  
Cyclooxygenase 2 ◽  
Kinase Ck2
Sign in / Sign up

Export Citation Format

Share Document