Bryostatin-1 causes radiosensitization of BMG-1 malignant glioma cells through differential activation of protein kinase-Cδ not evident in the non-malignant AA8 fibroblasts

2014 ◽  
Vol 401 (1-2) ◽  
pp. 49-59 ◽  
Author(s):  
Raghubendra Singh Dagur ◽  
Shashank Hambarde ◽  
Sudhir Chandna
Keyword(s):  
Protein Kinase ◽  
Malignant Glioma ◽  
Glioma Cells ◽  
Bryostatin 1 ◽  
Differential Activation ◽  
Malignant Glioma Cells ◽  
Protein Kinase Cδ

scholarly journals Up-regulation of ANKDR49, a poor prognostic factor, regulates cell proliferation of gliomas

2017 ◽  
Vol 37 (4) ◽  
Author(s):  
Chunyan Hao ◽  
Hubin Duan ◽  
Hao Li ◽  
Mingyang Pei ◽  
Yueting Liu ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Protein Kinase ◽  
Malignant Glioma ◽  
Glioma Cells ◽  
Translation Initiation Factor ◽  
The Cancer Genome Atlas ◽  
Initiation Factor ◽  
Poor Prognostic Factor ◽  
Malignant Glioma Cells ◽  
U87 Cells

The Ankyrin repeat domain 49 (ANKRD49) is an evolutionarily conserved protein, which is related to mediate protein–protein interaction. However, the function of ANKRD49 in human glioma remains elusive. Mining through The Cancer Genome Atlas (TCGA) database, we found that the expression of ANKRD49 was increased in glioma tissues and that high expression of ANKRD49 was strongly associated with high disease grade and poor overall survival. To investigate the role of ANKRD49 in malignant glioma, lentivirus expressing shRNA targetting ANKRD49 was constructed in U251 and U87 malignant glioma cells. We demonstrated that ANKRD49 knockdown reduced the proliferation rate of U251 and U87 cells. Further mechanism analysis indicated that depletion of ANKRD49 led to the cell-cycle arrest and induced apoptosis in U251 and U87 cells. ANKRD49 knockdown also changed the expression of key effectors that are involved in stress response, cell cycle, and apoptosis, including p-HSP27 (heat shock protein 27), p-Smad2 (SMAD family member 2), p-p53, p-p38, p-MAPK (mitogen-activated protein kinase), p-SAPK/JNK (stress-activated protein kinase/c-jun n-terminal kinase), cleveagated Caspase-7, p-Chk1 (checkpoint kinase 1), and p-eIF2a (eukaryotic translation initiation factor 2a). Taken together, our findings implicate that ANKRD49 promotes the proliferation of human malignant glioma cells. ANKRD49 maybe an attractive target for malignant glioma therapy.

MicroRNA 335 Is Required for Differentiation of Malignant Glioma Cells Induced by Activation of cAMP/Protein Kinase A Pathway

2011 ◽  
Vol 81 (3) ◽  
pp. 292-298 ◽  
Author(s):  
Minfeng Shu ◽  
Yuehan Zhou ◽  
Wenbo Zhu ◽  
Haipeng Zhang ◽  
Sihan Wu ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Malignant Glioma ◽  
Protein Kinase A ◽  
Glioma Cells ◽  
Malignant Glioma Cells ◽  
Kinase A

scholarly journals Inhibition of the DNA-Dependent Protein Kinase Catalytic Subunit Radiosensitizes Malignant Glioma Cells by Inducing Autophagy

2005 ◽  
Vol 65 (10) ◽  
pp. 4368-4375 ◽  
Author(s):  
Shigeru Daido ◽  
Akitsugu Yamamoto ◽  
Keishi Fujiwara ◽  
Raymond Sawaya ◽  
Seiji Kondo ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Malignant Glioma ◽  
Glioma Cells ◽  
Catalytic Subunit ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Malignant Glioma Cells

Ex vivo malignant glioma cells are sensitive to Fas (CD95/APO-1) ligand-mediated apoptosis

1998 ◽  
Vol 87 (1-2) ◽  
pp. 105-113 ◽  
Author(s):  
Karl Frei ◽  
Benjamin Ambar ◽  
Naoto Adachi ◽  
Yasuhiro Yonekawa ◽  
Adriano Fontana
Keyword(s):  
Malignant Glioma ◽  
Ex Vivo ◽  
Glioma Cells ◽  
Malignant Glioma Cells
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