Evidence map›Paper›PMID 28190785›Full record

ReviewCytokine & growth factor reviews2017

Crosstalk between insulin-like growth factor (IGF) receptor and integrins through direct integrin binding to IGF1.

Yoshikazu Takada, Yoko K Takada, Masaaki Fujita

Open access · greenAbstract readReview
In one paragraph

Review in Cytokine & growth factor reviews, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

46 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Modulation of the Mechanosensory Matrisome by Serotonergic Signaling.Results and problems in cell differentiation · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Article
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  10. The role of IGF/IGF-1R signaling in the regulation of cancer stem cells.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2024
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
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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

3 authors at 2 institutions in 3 countries.

Yoshikazu TakadaDepartments of Dermatology, Biochemistry and Molecular Medicine, School of Medicine, University of California, Davis, Sacramento, CA 95817, United States; Graduate Institute of Translational Medicine, College of Medical Science and Technology, Taipei Medical University, 250 Wu-Hsing Street, Taipei 11031, Taiwan, ROC. Electronic address: ytakada@ucdavis.edu.
Yoko K TakadaDepartments of Dermatology, Biochemistry and Molecular Medicine, School of Medicine, University of California, Davis, Sacramento, CA 95817, United States; Graduate Institute of Translational Medicine, College of Medical Science and Technology, Taipei Medical University, 250 Wu-Hsing Street, Taipei 11031, Taiwan, ROC.
Masaaki FujitaDepartment of Clinical Immunology and Rheumatology, The Tazuke-Kofukai Medical Research Institute, Kitano Hospital, Osaka, Japan.
Taipei Medical University · TWKitano Hospital · JP

Funding

Potential of a dominant-negative FGF mutant as a therapeutic in cancerR01CA131015 · NCI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI TAKADA, YOSHIKAZU · 2009 to 2012
$1.3M
GESI: a novel technology for functional imaging in living cellsR33CA196445 · NCI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI LAM, KIT S · 2016 to 2018
$1.1M
NCI NIH HHS R01 CA131015NCI NIH HHS R33 CA196445
6 · The paper itself

Abstract

It has been generally accepted that integrin cell adhesion receptors are involved in growth factor signaling (integrin-growth factor crosstalk), since antagonists to integrins often suppress growth factor signaling. Partly because integrins have been originally identified as cell adhesion receptors to extracellular matrix (ECM) proteins, current models of the crosstalk between IGF1 and integrins propose that ECM ligands (e.g., vitronectin) bind to integrins and IGF1 binds to IGF receptor type 1 (IGF1R), and two separate signals merge inside the cells. Our research proves otherwise. We discovered that IGF1 interacts directly with integrins, and induces integrin-IGF-IGF1R complex formation on the cell surface. IGF1 signaling can be detected in the absence of ECM (anchorage-independent conditions). Integrin antagonists block both ECM-integrin interaction and IGF-integrin interaction, and do not distinguish the two. This is one possible reason why integrin-IGF1 interaction has not been detected. With these new discoveries, we believe that the direct IGF-integrin interaction should be incorporated into models of IGF1 signaling. The integrin-binding defective mutant of IGF1 is defective in inducing IGF signaling, although the mutant still binds to IGF1R. Notably, the IGF1 mutant is dominant-negative and suppresses cell proliferation induced by wt IGF1, and suppresses tumorigenesis in vivo, and thus the IGF1 mutant has potential as a therapeutic.

Indexed as

Receptor Cross-TalkSignal TransductionAnimalsCell AdhesionCell ProliferationCell Transformation, NeoplasticHumansInsulin-Like Growth Factor IIntegrinsMiceProtein BindingProtein TransportReceptor, IGF Type 1Receptors, SomatomedinIGF1 protein, humanIGF1R protein, humanInsulin-Like Growth Factor IIntegrinsReceptor, IGF Type 1Receptors, SomatomedinCrosstalkDominant-negative antagonistIGF1IntegrinSignaling

Identifiers

PMID28190785
PMCPMC5401657
OpenAlexW2584924004

What OpenQuestion holds

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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.