scholarly journals Downregulation of protein kinase CK2 induces autophagic cell death through modulation of the mTOR and MAPK signaling pathways in human glioblastoma cells

2012 ◽  
Vol 41 (6) ◽  
pp. 1967-1976 ◽  
Author(s):  
BIRGITTE B. OLSEN ◽  
TINA H. SVENSTRUP ◽  
BARBARA GUERRA
Keyword(s):  
Cell Death ◽  
Protein Kinase ◽  
Signaling Pathways ◽  
Protein Kinase Ck2 ◽  
Mapk Signaling ◽  
Autophagic Cell Death ◽  
Glioblastoma Cells ◽  
Human Glioblastoma ◽  
Kinase Ck2 ◽  
Mapk Signaling Pathways

scholarly journals D11-Mediated Inhibition of Protein Kinase CK2 Impairs HIF-1α-Mediated Signaling in Human Glioblastoma Cells

2017 ◽  
Vol 10 (4) ◽  
pp. 5 ◽  
Author(s):  
Susanne Schaefer ◽  
Tina Svenstrup ◽  
Mette Fischer ◽  
Barbara Guerra
Keyword(s):  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Glioblastoma Cells ◽  
Human Glioblastoma ◽  
Human Glioblastoma Cells ◽  
Kinase Ck2

scholarly journals CSIG-14. PROTEIN KINASE CK2 REGULATES THE EXPRESSION OF NERVE/GLIAL ANTIGEN (NG)2 IN GLIOBLASTOMA

2019 ◽  
Vol 21 (Supplement_6) ◽  
pp. vi47-vi47
Author(s):  
Beate Schmitt ◽  
Christoph Sippl ◽  
Steffi Urbschat ◽  
Joachim Oertel ◽  
Matthias Laschke ◽  
...  
Keyword(s):  
Cell Migration ◽  
Protein Kinase ◽  
Tumor Growth ◽  
Protein Kinase Ck2 ◽  
Glioblastoma Cells ◽  
Human Glioblastoma ◽  
Human Glioblastoma Cells ◽  
Cell Migration And Proliferation ◽  
Kinase Ck2 ◽  
The Impact

Abstract Nerve/glial antigen (NG)2 enhances cell proliferation, migration as well as chemoresistance and is associated with a poor clinical outcome in glioblastoma. Since regulatory mechanisms of NG2 expression are still largely unknown, we herein investigated the impact of protein kinase CK2 inhibition on NG2 expression in human glioblastoma cells. CK2 was inhibited in NG2-positive human glioblastoma cell lines (A1207, U87) and primary human glioblastoma cells by pharmacological treatment (CX-4945, TBB) or siRNA. NG2 expression was analyzed by flow cytometry, Western Blot and qRT-PCR. Cytotoxicity and viability were assessed by WST-1, LDH and BrdU assays. Scratch, sprouting and BrdU assays as well as growth curves were performed to examine cell migration and proliferation. Truncated fragments of the human NG2 promotor were generated and their transcriptional activity was assessed using reporter gene assays. The effect of CK2 inhibition on tumor growth was investigated in xenografts within the flanks of NOD/SCID mice. Finally, effects of CK2 inhibition were analyzed in primary human glioblastoma cells. We found that inhibition of CK2 significantly reduces NG2 protein levels in A1207 (19%±6.2; Mean±SD), U87 (35%±11.3) and primary human glioblastoma cells (41%) when compared to controls. Further analyses revealed that this is due to a decreased NG2 mRNA level. Of note, we identified a 200 base pair fragment, including a binding site for the CK2-dependent transcription factor SP-1. Functional assays showed no cytotoxic effects of the decreased NG2 expression after CK2 inhibition, whereas cell migration and proliferation were markedly reduced. Moreover, we found that CX-4945 treatment decreases tumor growth, which is associated with a diminished NG2 expression (56%±13.0) when compared to controls. In conclusion, we identified CK2 as a novel regulator of NG2 gene expression in human glioblastoma cells. Hence, pharmacological inhibition of CK2 may represent a novel strategy in the therapy of NG2-positive glioblastoma.

scholarly journals Autophagic cell death induced by TrkA receptor activation in human glioblastoma cells

2007 ◽  
Vol 0 (0) ◽  
pp. 070717094311002-??? ◽  
Author(s):  
Katharina Hansen ◽  
Bettina Wagner ◽  
Wolfgang Hamel ◽  
Michaela Schweizer ◽  
Friedrich Haag ◽  
...  
Keyword(s):  
Cell Death ◽  
Receptor Activation ◽  
Autophagic Cell Death ◽  
Glioblastoma Cells ◽  
Trka Receptor ◽  
Human Glioblastoma ◽  
Human Glioblastoma Cells

scholarly journals Role of Mitogen- and Stress-Activated Kinases in Ischemic Injury

2002 ◽  
Vol 22 (6) ◽  
pp. 631-647 ◽  
Author(s):  
Elaine A. Irving ◽  
Mark Bamford
Keyword(s):  
Cell Death ◽  
Cerebral Ischemia ◽  
Protein Kinase ◽  
Signaling Pathways ◽  
Focal Cerebral Ischemia ◽  
Mapk Signaling ◽  
Mitogen Activated Protein Kinase ◽  
Amino Terminal ◽  
Biological Responses ◽  
Mitogen Activated Protein

Protein kinase-mediated signaling cascades constitute the major route by which cells respond to their extracellular environment. Of these, three well-characterized mitogen-activated protein kinase (MAPK) signaling pathways are those that use the extracellular signal-regulated kinase (ERK1/2) or the stress-activated protein kinase (p38/SAPK2 or JNK/SAPK) pathways. Mitogenic stimulation of the MAPK-ERK1/2 pathway modulates the activity of many transcription factors, leading to biological responses such as proliferation and differentiation. In contrast, the p38/SAPK2 and JNK/SAPK (c-Jun amino-terminal kinase/stress-activated protein kinase) pathways are only weakly, if at all, activated by mitogens, but are strongly activated by stress stimuli. There is now a growing body of evidence showing that these kinase signaling pathways become activated following a variety of injury stimuli including focal cerebral ischemia. Whether their activation, however, is merely an epiphenomenon of the process of cell death, or is actually involved in the mechanisms underlying ischemia-induced degeneration, remains to be fully understood. This review provides an overview of the current understanding of kinase pathway activation following cerebral ischemia and discusses the evidence supporting a role for these kinases in the mechanisms underlying ischemia-induced cell death.

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