Reversion of v-H-ras-Trasformed NIH 3T3 Cells by Apigenin Through Inhibiting Mitogen-Activated Protein Kinase and Its Downstream Oncogenes

1995 ◽  
Vol 212 (3) ◽  
pp. 767-775 ◽  
Author(s):  
M.L. Kuo ◽  
N.C. Yang
Keyword(s):  
Protein Kinase ◽  
Mitogen Activated Protein Kinase ◽  
3T3 Cells ◽  
Mitogen Activated Protein ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

scholarly journals Prostaglandin F2αStimulates Formation of p21ras-GTP Complex and Mitogen-activated Protein Kinase in NIH-3T3 Cells via Gq-protein-coupled Pathway

1995 ◽  
Vol 270 (15) ◽  
pp. 8984-8990 ◽  
Author(s):  
Tsuyoshi Watanabe ◽  
Iwao Waga ◽  
Zen-ichiro Honda ◽  
Kiyoshi Kurokawa ◽  
Takao Shimizu
Keyword(s):  
Protein Kinase ◽  
Mitogen Activated Protein Kinase ◽  
3T3 Cells ◽  
Mitogen Activated Protein ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

Activation of mitogen-activated protein kinase kinase by v-Raf in NIH 3T3 cells and in vitro

Science ◽  
1992 ◽  
Vol 257 (5075) ◽  
pp. 1404-1407 ◽  
Author(s):  
P Dent ◽  
W Haser ◽  
T. Haystead ◽  
L. Vincent ◽  
T. Roberts ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Mitogen Activated Protein Kinase ◽  
3T3 Cells ◽  
Mitogen Activated Protein ◽  
Nih 3T3 ◽  
Protein Kinase Kinase ◽  
Nih 3T3 Cells

scholarly journals Enhanced ROS Production in Oncogenically Transformed Cells Potentiates c-Jun N-Terminal Kinase and p38 Mitogen-Activated Protein Kinase Activation and Sensitization to Genotoxic Stress

2001 ◽  
Vol 21 (20) ◽  
pp. 6913-6926 ◽  
Author(s):  
Moran Benhar ◽  
Idan Dalyot ◽  
David Engelberg ◽  
Alexander Levitzki
Keyword(s):  
Protein Kinase ◽  
Mitogen Activated Protein Kinase ◽  
Transformed Cells ◽  
3T3 Cells ◽  
Stress Kinases ◽  
Mitogen Activated Protein ◽  
Stress Kinase ◽  
Transformed Cell Lines ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

ABSTRACT Many primary tumors as well as transformed cell lines display high sensitivity to chemotherapeutic drugs and radiation. The molecular mechanisms that underlie this sensitivity are largely unknown. Here we show that the sensitization of transformed cells to stress stimuli is due to the potentiation of the c-Jun N-terminal kinase (JNK) and p38 mitogen-activated protein kinase pathways. Activation of these pathways by the antitumor drug cis-platin (CDDP) and by other stress agents is markedly enhanced and is induced by lower stress doses in NIH 3T3 cells overexpressing epidermal growth factor receptor, HER1–2 kinase, or oncogenic Ras than in nontransformed NIH 3T3 cells. Inhibition of stress kinase activity by specific inhibitors reduces CDDP-mediated cell death in transformed cells, whereas overactivation of stress kinase pathways augments cells death. Potentiation of stress kinases is a common feature of cells transformed by different oncogenes, including cells derived from human tumors, and is shown here to be independent of the activity of the particular transforming oncoprotein. We further show that the mechanism that underlies potentiation of stress kinases in transformed cells involves reactive oxygen species (ROS), whose production is elevated in these cells. JNK/p38 activation is inhibited by antioxidants and in particular by inhibitors of the mitochondrial respiratory chain and NADPH oxidase. Conversely, by artificially elevating ROS levels in nontransformed NIH 3T3 cells we were able to induce potentiation of JNK/p38 activation. Taken together, our findings suggest that ROS-dependent potentiation of stress kinase pathways accounts for the sensitization of transformed cells to stress and anticancer drugs.

scholarly journals The p42/p44 Mitogen-activated Protein Kinase Activation Triggers p27Kip1Degradation Independently of CDK2/Cyclin E in NIH 3T3 Cells

2001 ◽  
Vol 276 (37) ◽  
pp. 34958-34965 ◽  
Author(s):  
Christelle Delmas ◽  
Stéphane Manenti ◽  
Aicha Boudjelal ◽  
Carole Peyssonnaux ◽  
Alain Eychène ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Cyclin E ◽  
Mitogen Activated Protein Kinase ◽  
3T3 Cells ◽  
Kinase Activation ◽  
Protein Kinase Activation ◽  
Mitogen Activated Protein ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

scholarly journals Regulation of Exit from Quiescence by p27 and Cyclin D1-CDK4

1998 ◽  
Vol 18 (11) ◽  
pp. 6605-6615 ◽  
Author(s):  
Mohamed H. Ladha ◽  
Kwang Y. Lee ◽  
Todd M. Upton ◽  
Michael F. Reed ◽  
Mark E. Ewen
Keyword(s):  
Cyclin D1 ◽  
Dominant Negative ◽  
Mitogen Activated Protein Kinase ◽  
Cyclin Dependent Kinase ◽  
3T3 Cells ◽  
Rate Limiting Step ◽  
Mitogen Activated Protein ◽  
Nih 3T3 ◽  
Rate Limiting ◽  
Nih 3T3 Cells

ABSTRACT The synthesis of cyclin D1 and its assembly with cyclin-dependent kinase 4 (CDK4) to form an active complex is a rate-limiting step in progression through the G1 phase of the cell cycle. Using an activated allele of mitogen-activated protein kinase kinase 1 (MEK1), we show that this kinase plays a significant role in positively regulating the expression of cyclin D1. This was found both in quiescent serum-starved cells and in cells expressing dominant-negative Ras. Despite the observation that cyclin D1 is a target of MEK1, in cycling cells, activated MEK1, but not cyclin D1, is capable of overcoming a G1 arrest induced by Ras inactivation. Either wild-type or catalytically inactive CDK4 cooperates with cyclin D1 in reversing the G1 arrest induced by inhibition of Ras activity. In quiescent NIH 3T3 cells expressing either ectopic cyclin D1 or activated MEK1, cyclin D1 is able to efficiently associate with CDK4; however, the complex is inactive. A significant percentage of the cyclin D1-CDK4 complexes are associated with p27 in serum-starved activated MEK1 or cyclin D1 cell lines. Reduction of p27 levels by expression of antisense p27 allows for S-phase entry from quiescence in NIH 3T3 cells expressing ectopic cyclin D1, but not in parental cells.

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