Evidence map›Paper›PMID 20197472›Full record

ArticleCancer research2010

Disruption of laminin-integrin-CD151-focal adhesion kinase axis sensitizes breast cancer cells to ErbB2 antagonists.

Xiuwei H Yang, Ludmila M Flores, Qinglin Li, Pengcheng Zhou, Fenghui Xu, Ian E Krop, Martin E Hemler

Open access · greenAbstract read
In one paragraph

Article in Cancer research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
6.6field-weighted citation impact, top 2% 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

76 citing papers in PubMed, 137 citations in OpenAlex.

  1. Cell-Instructive Biomaterials with Native-Like Biochemical Complexity.Annual review of biomedical engineering · 2025
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  8. Dysregulated Signalling Pathways Driving Anticancer Drug Resistance.International journal of molecular sciences · 2023
    Review
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  11. The importance of being CAFs (in cancer resistance to targeted therapies).Journal of experimental & clinical cancer research : CR · 2022
    Review
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  15. Article
  16. Article
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  18. Review
  19. The matrix in cancer.Nature reviews. Cancer · 2021
    Review
  20. Article

16 more citing papers are in PubMed but not listed here.

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

7 authors at 3 institutions in 1 country.

Xiuwei H YangDepartment of Cancer Immunology and AIDS, Dana-Farber Cancer Institute and Harvard Medical School, University of Massachusetts, Boston, Massachusetts, USA. xya222@uky.edu
Ludmila M Flores
Qinglin Li
Pengcheng Zhou
Fenghui Xu
Ian E Krop
Martin E Hemler
Dana-Farber Cancer Institute · USHarvard University · USUniversity of Massachusetts Boston · US

Funding

Support of carcinoma metastasis by integrin a6-CD151-PKC complexesR01CA042368 · NCI · DANA-FARBER CANCER INSTITUTE · PI HEMLER, MARTIN E · 1986 to 2019
$5.4M
NCI NIH HHS CA42368NCI NIH HHS R01 CA042368
6 · The paper itself

Abstract

Resistance to anti-ErbB2 agents is a significant problem in the treatment of human ErbB2+ breast cancers. We show here that adhesion of human ErbB2+ breast cancer cells to basement membrane laminin-5 provides substantial resistance to trastuzumab and lapatinib, agents that respectively target the extracellular and kinase domains of ErbB2. Knockdown of laminin-binding integrins (alpha6beta4, alpha3beta1) or associated tetraspanin protein CD151 reversed laminin-5 resistance and sensitized ErbB2+ cells to trastuzumab and lapatinib. CD151 knockdown, together with trastuzumab treatment, inhibited ErbB2 activation and downstream signaling through Akt, Erk1/2, and focal adhesion kinase (FAK). Hence, ErbB2 function in mammary tumor cells is promoted by integrin-mediated adhesion to laminin-5, with strong support by CD151, leading to signaling through FAK. Consequently, removal or inhibition of any of these components (laminin-5, integrin, CD151, FAK) markedly sensitizes cells to anti-ErbB2 agents. These new insights should be useful when devising strategies for overcoming drug resistance in ErbB2+ cancers.

Indexed as

Antibodies, MonoclonalAntibodies, Monoclonal, HumanizedAntigens, CDAntineoplastic AgentsBreast NeoplasmsCell Adhesion MoleculesCell Line, TumorDrug SynergismEnzyme ActivationErb-b2 Receptor Tyrosine KinasesFocal Adhesion Protein-Tyrosine KinasesHumansIntegrin alpha3beta1Integrin alpha6beta4KalininLapatinibAntibodies, MonoclonalAntibodies, Monoclonal, HumanizedAntigens, CDAntineoplastic AgentsCD151 protein, humanCell Adhesion MoleculesErb-b2 Receptor Tyrosine KinasesFocal Adhesion Protein-Tyrosine KinasesIntegrin alpha3beta1Integrin alpha6beta4KalininLapatinibProtein Kinase InhibitorsQuinazolinesTetraspanin 24Trastuzumab

Identifiers

PMID20197472
PMCPMC3310185
OpenAlexW2124393085

What OpenQuestion holds

Textmetadata
LicenceTDM
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.