Oleanolic Acid Induces Metabolic Adaptation in Cancer Cells by Activating the AMP-Activated Protein Kinase Pathway

2014 ◽  
Vol 62 (24) ◽  
pp. 5528-5537 ◽  
Author(s):  
Jia Liu ◽  
Lanhong Zheng ◽  
Ning Wu ◽  
Leina Ma ◽  
Jiateng Zhong ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Cancer Cells ◽  
Oleanolic Acid ◽  
Metabolic Adaptation ◽  
Amp Activated Protein Kinase ◽  
Kinase Pathway

Cancer therapy: staying current with AMPK

2008 ◽  
Vol 412 (2) ◽  
pp. e3-e5 ◽  
Author(s):  
David A. Fruman ◽  
Aimee L. Edinger
Keyword(s):  
Protein Kinase ◽  
Cancer Therapy ◽  
Cancer Cells ◽  
New Work ◽  
Chromosome 10 ◽  
Biochemical Journal ◽  
Phosphatase And Tensin Homologue ◽  
Amp Activated Protein Kinase ◽  
Kinase Pathway

Does the LKB1–AMPK (AMP-activated protein kinase) pathway act to suppress tumorigenesis or to rescue cancer cells from metabolic collapse? New work from the Alessi laboratory in this issue of the Biochemical Journal shows conclusively that AMPK activators delay the growth of tumours that occur spontaneously in PTEN (phosphatase and tensin homologue deleted on chromosome 10) heterozygous mice.

scholarly journals Differential regulation of AMP-activated protein kinase in healthy and cancer cells explains why V-ATPase inhibition selectively kills cancer cells

2019 ◽  
Vol 294 (46) ◽  
pp. 17239-17248
Author(s):  
Karin Bartel ◽  
Rolf Müller ◽  
Karin von Schwarzenberg
Keyword(s):  
Reactive Oxygen Species ◽  
Protein Kinase ◽  
Cancer Cells ◽  
Reactive Oxygen Species Production ◽  
Differential Regulation ◽  
Oxygen Species ◽  
Atpase Inhibitors ◽  
Species Production ◽  
Amp Activated Protein Kinase ◽  
Atpase Inhibition

The cellular energy sensor AMP-activated protein kinase (AMPK) is a metabolic hub regulating various pathways involved in tumor metabolism. Here we report that vacuolar H+-ATPase (V-ATPase) inhibition differentially affects regulation of AMPK in tumor and nontumor cells and that this differential regulation contributes to the selectivity of V-ATPase inhibitors for tumor cells. In nonmalignant cells, the V-ATPase inhibitor archazolid increased phosphorylation and lysosomal localization of AMPK. We noted that AMPK localization has a prosurvival role, as AMPK silencing decreased cellular growth rates. In contrast, in cancer cells, we found that AMPK is constitutively active and that archazolid does not affect its phosphorylation and localization. Moreover, V-ATPase–independent AMPK induction in tumor cells protected them from archazolid-induced cytotoxicity, further underlining the role of AMPK as a prosurvival mediator. These observations indicate that AMPK regulation is uncoupled from V-ATPase activity in cancer cells and that this makes them more susceptible to cell death induction by V-ATPase inhibitors. In both tumor and healthy cells, V-ATPase inhibition induced a distinct metabolic regulatory cascade downstream of AMPK, affecting ATP and NADPH levels, glucose uptake, and reactive oxygen species production. We could attribute the prosurvival effects to AMPK's ability to maintain redox homeostasis by inhibiting reactive oxygen species production and maintaining NADPH levels. In summary, the results of our work indicate that V-ATPase inhibition has differential effects on AMPK-mediated metabolic regulation in cancer and healthy cells and explain the tumor-specific cytotoxicity of V-ATPase inhibition.

Apoptosis triggered by isoquercitrin in bladder cancer cells by activating the AMPK-activated protein kinase pathway

2017 ◽  
Vol 8 (10) ◽  
pp. 3707-3722 ◽  
Author(s):  
Ping Wu ◽  
Siyuan Liu ◽  
Jianyu Su ◽  
Jianping Chen ◽  
Lin Li ◽  
...  
Keyword(s):  
Bladder Cancer ◽  
Protein Kinase ◽  
Cancer Cells ◽  
Cancer Cell ◽  
Cell Metabolism ◽  
Bladder Cancer Cell ◽  
Bladder Cancer Cells ◽  
Immunoblotting Assay ◽  
Cancer Cell Metabolism ◽  
Kinase Pathway

Our findings provide comprehensive evidence that isoquercitrin (ISO) influenced T24 bladder cancer cell metabolism by activating the AMPK pathway as identified by combination with metabolomics and immunoblotting assay.

scholarly journals Regulation of glycogen synthesis by the laforin–malin complex is modulated by the AMP-activated protein kinase pathway

2007 ◽  
Vol 17 (5) ◽  
pp. 667-678 ◽  
Author(s):  
Maria Carmen Solaz-Fuster ◽  
José Vicente Gimeno-Alcañiz ◽  
Susana Ros ◽  
Maria Elena Fernandez-Sanchez ◽  
Belen Garcia-Fojeda ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Glycogen Synthesis ◽  
Amp Activated Protein Kinase ◽  
Kinase Pathway
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