Evidence map›Paper›PMID 21532888›Full record

ArticleNeoplasia (New York, N.Y.)2011

p38γ mitogen-activated protein kinase contributes to oncogenic properties maintenance and resistance to poly (ADP-ribose)-polymerase-1 inhibition in breast cancer.

Fanyan Meng, Haijun Zhang, Gang Liu, Bas Kreike, Wei Chen, Seema Sethi, Fred R Miller, Guojun Wu

Open access · goldAbstract read
In one paragraph

Article in Neoplasia (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

36 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. P38 kinase in gastrointestinal cancers.Cancer gene therapy · 2023
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. The Role of p38γ in Cancer: From review to outlook.International journal of biological sciences · 2021
    Review
  10. Article
  11. Review
  12. Role of p38γ MAPK in regulation of EMT and cancer stem cells.Biochimica et biophysica acta. Molecular basis of disease · 2018
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Enhanced antitumor activity and attenuated cardiotoxicity of Epirubicin combined with Paeonol against breast cancer.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Article
  18. Article
  19. Clinicopathological significance of p38β, p38γ, and p38δ and its biological roles in esophageal squamous cell carcinoma.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Article
  20. Cancer stem cells and early stage basal-like breast cancer.World journal of obstetrics and gynecology · 2016
    Article
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

8 authors at 3 institutions in 2 countries.

Fanyan MengThe Breast Cancer Biology Program, Barbara Ann Karmanos Cancer Institute, Detroit, MI, USA.
Haijun Zhang
Gang Liu
Bas Kreike
Wei Chen
Seema Sethi
Fred R Miller
Guojun Wu
The Barbara Ann Karmanos Cancer Institute · USWayne State University · USThe Netherlands Cancer Institute · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

p38γ MAPK, one of the four members of p38 mitogen-activated protein kinases (MAPKs), has previously been shown to harbor oncogenic functions. However, the biologic function of p38γ MAPK in breast cancer has not been well defined. In this study, we have shown that p38γ MAPK is overexpressed in highly metastatic human and mouse breast cancer cell lines and p38γ MAPK expression is preferentially associated with basal-like and metastatic phenotypes of breast tumor samples. Ectopic expression of p38γ MAPK did not lead to an increase in oncogenic properties in vitro in most tested mammary epithelial cells. However, knockdown of p38γ MAPK expression resulted in a dramatic decrease in cell proliferation, colony formation, cell migration, invasion in vitro and significant retardation of tumorigenesis, and long-distance metastasis to the lungs in vivo. Moreover, knockdown of p38γ MAPK triggered the activation of AKT signaling. Inhibition of this feedback loop with various PI3K/AKT signaling inhibitors facilitated the effect of targeting p38γ MAPK. We further found that overexpression of p38γ MAPK did not promote cell resistance to chemotherapeutic agents doxorubicin and paclitaxel but significantly increased cell resistance to PJ-34, a DNA damage agent poly (ADP-ribose)-polymerase-1 (PARP) inhibitor in vitro and in vivo. Finally, we identified that p38γ MAPK overexpression led to marked cell cycle arrest in G(2)/M phase. Our study for the first time clearly demonstrates that p38γ MAPK is a promising target for the design of targeted therapies for basal-like breast cancer with metastatic characteristics and for overcoming potential resistance against the PARP inhibitor.

Indexed as

AnimalsBreast NeoplasmsCell CycleCell Line, TumorCell MovementCell ProliferationCell Transformation, NeoplasticDoxorubicinHumansMiceMitogen-Activated Protein Kinase 12Neoplasm InvasivenessNeoplasm MetastasisPaclitaxelPhenanthrenesPhosphatidylinositol 3-KinaseDoxorubicinMitogen-Activated Protein Kinase 12N-(oxo-5,6-dihydrophenanthridin-2-yl)-N,N-dimethylacetamide hydrochloridePaclitaxelPARP1 protein, humanPhenanthrenesPhosphatidylinositol 3-KinasePoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) Polymerase InhibitorsPoly(ADP-ribose) PolymerasesProto-Oncogene Proteins c-akt

Identifiers

PMID21532888
PMCPMC3084624
OpenAlexW1830327315

What OpenQuestion holds

Textmetadata
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.