Evidence map›Paper›PMID 28033353›Full record

ArticlePloS one2016

2-Deoxyglucose Suppresses ERK Phosphorylation in LKB1 and Ras Wild-Type Non-Small Cell Lung Cancer Cells.

Linlin Sun, Xiuju Liu, Haian Fu, Wei Zhou, Diansheng Zhong

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.3field-weighted citation impact, top 21% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 27 citations in OpenAlex.

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  11. Inhibition of glycolysis ameliorate arthritis in adjuvant arthritis rats by inhibiting synoviocyte activation through AMPK/NF-кB pathway.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2020
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Linlin SunTianjin Key Laboratory of Lung Cancer Metastasis and Tumor Microenvironment, Lung Cancer Institute, Tianjin Medical University General Hospital, Tianjin, P.R. China.
Xiuju LiuDepartment of Hematology and Medical Oncology, Emory University School of Medicine, Atlanta, Georgia, United States of America.
Haian FuDepartment of Pharmacology and Emory Chemical Biology Discovery Center, Emory University School of Medicine, Atlanta, Georgia, United States of America.
Wei ZhouDepartment of Hematology and Medical Oncology, Emory University School of Medicine, Atlanta, Georgia, United States of America.
Diansheng ZhongTianjin Key Laboratory of Lung Cancer Metastasis and Tumor Microenvironment, Lung Cancer Institute, Tianjin Medical University General Hospital, Tianjin, P.R. China.
Emory University · USTianjin Medical University General Hospital · CN

Funding

Winship Cancer Institute Cancer Center Support GrantP30CA138292 · NCI · EMORY UNIVERSITY · PI Suresh S Ramalingam · 2009 to 2026
$47.5M
Targeting Microtubules and HDAC6 in NSCLCP01CA116676 · NCI · EMORY UNIVERSITY · PI KHURI, FADLO RAJA · 2006 to 2012
$8.0M
Pro-Oncogenic Role of LKB1 in NSCLCR01CA140571 · NCI · EMORY UNIVERSITY · PI ZHOU, WEI · 2011 to 2015
$1.6M
NCI NIH HHS P01 CA116676NCI NIH HHS P30 CA138292NCI NIH HHS R01 CA140571
6 · The paper itself

Abstract

Tumor cells rely on aerobic glycolysis to generate ATP, namely the "Warburg" effect. 2-deoxyglucose (2-DG) is well characterized as a glycolytic inhibitor, but its effect on cellular signaling pathways has not been fully elucidated. Herein, we sought to investigate the effect of 2-DG on ERK function in lung cancer cells. We found that 2-DG inhibits ERK phosphorylation in a time and dose-dependent manner in lung cancer cells. This inhibition requires functional LKB1. LKB1 knockdown in LKB1 wildtype cells correlated with an increase in the basal level of p-ERK. Restoration of LKB1 in LKB1-null cells significantly inhibits ERK activation. Blocking AMPK function with AMPK inhibitor, AMPK siRNA or DN-AMPK diminishes the inhibitory effect of 2-DG on ERK, suggesting that 2-DG-induced ERK inhibition is mediated by LKB1/AMPK signaling. Moreover, IGF1-induced ERK phosphorylation is significantly decreased by 2-DG. Conversely, a subset of oncogenic mutants of K-Ras, the main upstream regulator of ERK, blocks 2-DG-induced LKB1/AMPK signaling. These findings reveal the potential cross-talk between LKB1/AMPK and ERK signaling and help to better understand the mechanism of action of 2-DG.

Indexed as

AMP-Activated Protein Kinase KinasesAMP-Activated Protein KinasesCarcinoma, Non-Small-Cell LungCell Line, TumorDeoxyglucoseEnzyme ActivationExtracellular Signal-Regulated MAP KinasesHumansInsulin-Like Growth Factor ILung NeoplasmsMutationPhosphatidylinositol 3-KinasesPhosphorylationProtein Serine-Threonine KinasesProto-Oncogene Proteins c-aktras ProteinsAMP-Activated Protein Kinase KinasesAMP-Activated Protein KinasesDeoxyglucoseExtracellular Signal-Regulated MAP KinasesInsulin-Like Growth Factor IPhosphatidylinositol 3-KinasesProtein Serine-Threonine KinasesProto-Oncogene Proteins c-aktras ProteinsSTK11 protein, human

Identifiers

PMID28033353
PMCPMC5198974
OpenAlexW2561706117

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.