Evidence map›Paper›PMID 21555521›Full record

ArticleThe Journal of biological chemistry2011

Phosphorylation of caspase-7 by p21-activated protein kinase (PAK) 2 inhibits chemotherapeutic drug-induced apoptosis of breast cancer cell lines.

Xiang Li, Weihong Wen, Kangdong Liu, Feng Zhu, Margarita Malakhova, Cong Peng, Tingting Li, Hong-Gyum Kim, Weiya Ma, Yong Yeon Cho and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

37 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
  2. Article
  3. Regulation of Cancer Metastasis by PAK2.International journal of molecular sciences · 2024
    Review
  4. Article
  5. Article
  6. Review
  7. The gasdermin family: emerging therapeutic targets in diseases.Signal transduction and targeted therapy · 2024
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. The Superior Cytotoxicity of Dual Targeting of BCR/ABL and PI3K in K562 Cells: Proposing a Novel Therapeutic Potential for the Treatment of CML.Indian journal of hematology & blood transfusion : an official journal of Indian Society of Hematology and Blood Transfusion · 2022
    Article
  13. Article
  14. Review
  15. Cell-Cycle Cross Talk with Caspases and Their Substrates.Cold Spring Harbor perspectives in biology · 2020
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

13 authors at 4 institutions in 2 countries.

Xiang LiThe Hormel Institute, University of Minnesota, Austin, Minnesota 55912, USA.
Weihong Wen
Kangdong Liu
Feng Zhu
Margarita Malakhova
Cong Peng
Tingting Li
Hong-Gyum Kim
Weiya Ma
Yong Yeon Cho
Ann M Bode
Ziming Dong
Zigang Dong
Hormel (United States) · USUniversity of Minnesota · USLuoyang Central Hospital Affiliated to Zhengzhou University · CNZhengzhou University · CN

Funding

Ultraviolet-Induced Signal TrasductionR01CA077646 · NCI · UNIVERSITY OF MINNESOTA TWIN CITIES · PI DONG, ZIGANG · 1999 to 2010
$2.3M
The role of histone phosphorylation in arsenic-induced cell transformation and skR01ES016548 · NIEHS · UNIVERSITY OF MINNESOTA · PI DONG, ZIGANG · 2008 to 2012
$1.7M
Anticarcinogenic Mechanisms of Tea ConstituentsR37CA081064 · NCI · UNIVERSITY OF MINNESOTA · PI DONG, ZIGANG · 2008 to 2012
$1.5M
Inhibition of Carcinogenesis by Tea and Tea ConstituentsR01CA120388 · NCI · UNIVERSITY OF MINNESOTA · PI DONG, ZIGANG · 2006 to 2010
$1.3M
NCI NIH HHS CA077646NCI NIH HHS CA120388NCI NIH HHS R01 CA077646NCI NIH HHS R01 CA120388NCI NIH HHS R37 CA081064NIEHS NIH HHS ES016548NIEHS NIH HHS R01 ES016548PHS HHS CAR37CA081064
6 · The paper itself

Abstract

p21-activated kinase (PAK) 2, a member of the PAK family of serine/threonine protein kinases, plays an important role in physiological processes such as motility, survival, mitosis, and apoptosis. However, the role of PAK2 in resistance to chemotherapy is unclear. Here we report that PAK2 is highly expressed in human breast cancer cell lines and human breast invasive carcinoma tissue compared with a human non-tumorigenic mammary epithelial cell line and adjacent normal breast tissue, respectively. Interestingly, we found that PAK2 can bind with caspase-7 and phosphorylate caspase-7 at the Ser-30, Thr-173, and Ser-239 sites. Functionally, the phosphorylation of caspase-7 decreases its activity, thereby inhibiting cellular apoptosis. Our data indicate that highly expressed PAK2 mediates chemotherapeutic resistance in human breast invasive ductal carcinoma by negatively regulating caspase-7 activity.

Indexed as

Drug Resistance, NeoplasmAmino Acid SequenceAntineoplastic AgentsApoptosisBase SequenceBreast NeoplasmsCarcinoma, DuctalCaspase 7Cell Line, TumorGene Expression Regulation, NeoplasticGene Knockdown TechniquesHumansp21-Activated KinasesPhosphorylationProtein TransportAntineoplastic AgentsCaspase 7p21-Activated Kinases

Identifiers

PMID21555521
PMCPMC3121375
OpenAlexW2117367533

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.