Evidence map›Paper›PMID 26143491›Full record

ArticleOncotarget2015

AMP-activated kinase (AMPK) regulates activity of HER2 and EGFR in breast cancer.

Teraneh Z Jhaveri, Juhyung Woo, Xiaobin Shang, Ben Ho Park, Edward Gabrielson

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
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  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Phosphorylation of NaThe Journal of membrane biology · 2021
    Article
  10. Article
  11. Article
  12. Breast cancer (Dove Medical Press) · 2021
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. AMP-activated protein kinase and energy balance in breast cancer.American journal of translational research · 2017
    Review
  18. Review
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 1 country.

Teraneh Z JhaveriDepartments of Pathology and Oncology and The Sydney Kimmel Cancer Center, The Johns Hopkins School of Medicine, Baltimore, MD, USA.
Juhyung WooDepartments of Pathology and Oncology and The Sydney Kimmel Cancer Center, The Johns Hopkins School of Medicine, Baltimore, MD, USA.
Xiaobin ShangDepartments of Pathology and Oncology and The Sydney Kimmel Cancer Center, The Johns Hopkins School of Medicine, Baltimore, MD, USA.
Ben Ho ParkDepartments of Pathology and Oncology and The Sydney Kimmel Cancer Center, The Johns Hopkins School of Medicine, Baltimore, MD, USA.
Edward GabrielsonDepartments of Pathology and Oncology and The Sydney Kimmel Cancer Center, The Johns Hopkins School of Medicine, Baltimore, MD, USA.
Johns Hopkins University · USSidney Kimmel Cancer Center · US

Funding

TRAINING PROGRAM IN THE PATHOBIOLOGY OF CANCERT32CA067751 · NCI · JOHNS HOPKINS UNIVERSITY · PI GABRIELSON, EDWARD W. · 1996 to 2011
$4.0M
NCI NIH HHS T32 CA067751NCI NIH HHS T32 CA67751
6 · The paper itself

Abstract

AMP-activated Protein Kinase (AMPK) activity retards growth of many types of cancers. Investigating effects of AMPK activation on breast cancer cell signaling and survival, we found that breast cancer cell lines with amplification and over-expression of HER2 or EGFR are 2- to 5-fold more sensitive to cytotoxic effects of AICAR, a canonical pharmacological activator of AMPK, than breast cancer cell lines lacking HER2 or EGFR overexpression. Paralleling effects on cell survival, AICAR leads to dose- and time-dependent inhibition of HER2 and EGFR in HER2-amplified breast cancer cells, with activation of AMPK and suppression of HER2/ EGFR activity preceding commitment to cell death. Transfection of constitutively active AMPKα also leads to decreased HER2 and EGFR phosphorylation, reduced downstream signaling associated with these receptor tyrosine kinases (RTKs), and reduced breast cancer cell growth, confirming effects of AMPK activity on HER2/ EGFR. Ensuing co-immunoprecipitation experiments demonstrated an interaction of HER2 with AMPK and an in vitro phosphorylation assay found that HER2 and EGFR contain sequences that are potential substrates for AMPK. Our results lead us to postulate that AMPK regulates HER2 and EGFR activity in HER2-amplified breast cancer cells and thus activation of AMPK might provide therapeutic benefit in such cancers.

Indexed as

Aminoimidazole CarboxamideAMP-Activated Protein KinasesAnimalsBlotting, WesternBreast NeoplasmsCell LineCell Line, TumorCell SurvivalErb-b2 Receptor Tyrosine KinasesErbB ReceptorsHumansMCF-7 CellsMice, Inbred NODMice, SCIDRibonucleotidesRNA InterferenceAICA ribonucleotideAminoimidazole CarboxamideAMP-Activated Protein KinasesErb-b2 Receptor Tyrosine KinasesErbB ReceptorsRibonucleotidesAMP-activated protein kinase (AMPK)cancer cell metabolismcancer therapyEGFRHER2

Identifiers

PMID26143491
PMCPMC4558113
OpenAlexW1484764033

What OpenQuestion holds

Textmetadata
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.