Evidence map›Paper›PMID 28415760›Full record

ArticleOncotarget2017

Binding of galectin-1 to integrin β1 potentiates drug resistance by promoting survivin expression in breast cancer cells.

KeeSoo Nam, Seog-Ho Son, Sunhwa Oh, Donghwan Jeon, Hyungjoo Kim, Dong-Young Noh, Sangmin Kim, Incheol Shin

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed, 1 pooled it
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

41 citing papers in PubMed, 1 synthesis or guideline pooled it, 56 citations in OpenAlex.

  1. STAT3 as a potential therapeutic target in triple negative breast cancer: a systematic review.Journal of experimental & clinical cancer research : CR · 2019
    Pooled it
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  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

8 authors at 3 institutions in 1 country.

KeeSoo NamDepartment of Life Science, Hanyang University, Seoul, 133-791, Korea.
Seog-Ho SonDepartment of Life Science, Hanyang University, Seoul, 133-791, Korea.
Sunhwa OhDepartment of Life Science, Hanyang University, Seoul, 133-791, Korea.
Donghwan JeonDepartment of Life Science, Hanyang University, Seoul, 133-791, Korea.
Hyungjoo KimDepartment of Life Science, Hanyang University, Seoul, 133-791, Korea.
Dong-Young NohCancer Research Institute, Seoul National University College of Medicine, Seoul, 110-744 Korea.
Sangmin KimDepartment of Surgery, Samsung Medical Center, Seoul, 135-710, Korea.
Incheol ShinDepartment of Life Science, Hanyang University, Seoul, 133-791, Korea.
Hanyang University · KRSamsung Medical Center · KRSeoul National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Galectin-1 is a β-galactoside binding protein secreted by many types of aggressive cancer cells. Although many studies have focused on the role of galectin-1 in cancer progression, relatively little attention has been paid to galectin-1 as an extracellular therapeutic target. To elucidate the molecular mechanisms underlying galectin-1-mediated cancer progression, we established galectin-1 knock-down cells via retroviral delivery of short hairpin RNA (shRNA) against galectin-1 in two triple-negative breast cancer (TNBC) cell lines, MDA-MB-231 and Hs578T. Ablation of galectin-1 expression decreased cell proliferation, migration, invasion, and doxorubicin resistance. We found that these effects were caused by decreased galectin-1-integrin β1 interactions and suppression of the downstream focal adhesion kinase (FAK)/c-Src pathway. We also found that silencing of galectin-1 inhibited extracellular signal-regulated kinase (ERK)/signal transducer and activator of transcription 3 (STAT3) signaling, thereby down-regulating survivin expression. This finding implicates STAT3 as a transcription factor for survivin. Finally, rescue of endogenous galectin-1 knock-down and recombinant galectin-1 treatment both recovered signaling through the FAK/c-Src/ERK/STAT3/survivin pathway. Taken together, these results suggest that extracellular galectin-1 contributes to cancer progression and doxorubicin resistance in TNBC cells. These effects appear to be mediated by galectin-1-induced up-regulation of the integrin β1/FAK/c-Src/ERK/STAT3/survivin pathway. Our results imply that extracellular galectin-1 has potential as a therapeutic target for triple-negative breast cancer.

Indexed as

Gene Expression Regulation, NeoplasticAntineoplastic AgentsApoptosisBreast NeoplasmsCell Line, TumorCell MovementCell ProliferationDoxorubicinDrug Resistance, NeoplasmExtracellular Signal-Regulated MAP KinasesFemaleFocal Adhesion Protein-Tyrosine KinasesGalectin 1Gene SilencingHumansInhibitor of Apoptosis ProteinsAntineoplastic AgentsBIRC5 protein, humanDoxorubicinExtracellular Signal-Regulated MAP KinasesFocal Adhesion Protein-Tyrosine KinasesGalectin 1Inhibitor of Apoptosis ProteinsIntegrin beta1STAT3 Transcription FactorSurvivindrug resistancegalectin-1integrin β1STAT3survivin

Identifiers

PMID28415760
PMCPMC5482619
OpenAlexW2598100825

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.