Evidence map›Paper›PMID 17030947›Full record

ArticleThe Journal of experimental medicine2006

Integrin signaling is critical for pathological angiogenesis.

Ganapati H Mahabeleshwar, Weiyi Feng, David R Phillips, Tatiana V Byzova

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed
8.0field-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

111 citing papers in PubMed, 207 citations in OpenAlex.

  1. Article
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  3. Review
  4. Review
  5. Article
  6. Integrins as Drug Targets in Vascular and Related Diseases.International journal of drug discovery and pharmacology · 2024
    Article
  7. Article
  8. Article
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  17. Review
  18. Article
  19. Article
  20. Prolyl 3-Hydroxylase 2 Is a Molecular Player of Angiogenesis.International journal of molecular sciences · 2021
    Article

51 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

4 authors at 3 institutions in 1 country.

Ganapati H MahabeleshwarDepartment of Molecular Cardiology, Joseph J. Jacobs Center for Thrombosis and Vascular Biology, NB50, The Cleveland Clinic Foundation, Cleveland, OH 44195, USA.
Weiyi Feng
David R Phillips
Tatiana V Byzova
Cleveland Clinic · USJacobs (United States) · USPortola Pharmaceuticals (United States) · US

Funding

Structure Basis for Talin-mediated Integrin ActivationP01HL073311 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI BYZOVA, TATIANA V · 2004 to 2019
$27.4M
Regulation of Integrins in Neovasculature DevelopmentR01HL071625 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI BYZOVA, TATIANA V · 2003 to 2021
$7.3M
NHLBI NIH HHS HL071625NHLBI NIH HHS HL073311NHLBI NIH HHS P01 HL073311NHLBI NIH HHS R01 HL071625
6 · The paper itself

Abstract

The process of postnatal angiogenesis plays a crucial role in pathogenesis of numerous diseases, including but not limited to tumor growth/metastasis, diabetic retinopathy, and in tissue remodeling upon injury. However, the molecular events underlying this complex process are not well understood and numerous issues remain controversial, including the regulatory function of integrin receptors. To analyze the role of integrin phosphorylation and signaling in angiogenesis, we generated knock-in mice that express a mutant beta3 integrin unable to undergo tyrosine phosphorylation. Two distinct models of pathological angiogenesis revealed that neovascularization is impaired in mutant beta3 knock-in mice. In an ex vivo angiogenesis assay, mutant beta3 knock-in endothelial cells did not form complete capillaries in response to vascular endothelial growth factor (VEGF) stimulation. At the cellular level, defective tyrosine phosphorylation in mutant beta3 knock-in cells resulted in impaired adhesion, spreading, and migration of endothelial cells. At the molecular level, VEGF stimulated complex formation between VEGF receptor-2 and beta3 integrin in wild-type but not in mutant beta3 knock-in endothelial cells. Moreover, phosphorylation of VEGF receptor-2 was significantly reduced in cells expressing mutant beta3 compared to wild type, leading to impaired integrin activation in these cells. These findings provide novel mechanistic insights into the role of integrin-VEGF axis in pathological angiogenesis.

Indexed as

AnimalsCell Line, TumorCells, CulturedEndothelial CellsIntegrin beta3Melanoma, ExperimentalMiceMice, Inbred C57BLMice, Mutant StrainsNeovascularization, PathologicPhosphorylationSignal TransductionIntegrin beta3

Identifiers

PMID17030947
PMCPMC2118124
OpenAlexW2021844666

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.