ArticleThe Journal of biological chemistry2011
Vascular endothelial growth factor A (VEGF-A) induces endothelial and cancer cell migration through direct binding to integrin {alpha}9{beta}1: identification of a specific {alpha}9{beta}1 binding site.
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 48 papers.
What it found
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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.
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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.
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Who cites it
48 citing papers in PubMed, 73 citations in OpenAlex.
- Gut microbiota-activated PLCγ2 monocytes drive atrial fibrillation.Nature communications · 2026Article
- Force-Dependent Presence of Senescent Cells Expressing Vascular Endothelial Growth Factor During Orthodontic Tooth Movement.Biology · 2026Article
- Distinct roles of small extracellular vesicles from resident and infiltrating macrophages on glioma growth and mobility.Journal of Cancer · 2025Article
- Integrins regulation of wound healing processes: insights for chronic skin wound therapeutics.Frontiers in cellular and infection microbiology · 2024Review
- Integrins as a bridge between bacteria and cells: key targets for therapeutic wound healing.Burns & trauma · 2024Review
- Suppressing Inflammation for the Treatment of Diabetic Retinopathy and Age-Related Macular Degeneration: Dazdotuftide as a Potential New Multitarget Therapeutic Candidate.Biomedicines · 2023Review
- Lymphangiogenesis Guidance Mechanisms and Therapeutic Implications in Pathological States of the Cornea.Cells · 2023Review
- Molecular Mechanisms and Future Implications of VEGF/VEGFR in Cancer Therapy.Clinical cancer research : an official journal of the American Association for Cancer Research · 2023Review
- RecurrentCancers · 2022Article
- Bioinformatics of Differentially Expressed Genes in Phorbol 12-Myristate 13-Acetate-Induced Megakaryocytic Differentiation of K562 Cells by Microarray Analysis.International journal of molecular sciences · 2022Article
- Emerging roles of platelets in cancer biology and their potential as therapeutic targets.Frontiers in oncology · 2022Review
- CT-detected extramural venous invasion-related gene signature for the overall survival prediction in patients with gastric cancer.Cancer medicine · 2021Article
- Neovascular Macular Degeneration: A Review of Etiology, Risk Factors, and Recent Advances in Research and Therapy.International journal of molecular sciences · 2021Review
- Integrin-α9β1 as a Novel Therapeutic Target for Refractory Diseases: Recent Progress and Insights.Frontiers in immunology · 2021Review
- Acute cytotoxicity and increased vascular endothelial growth factor after in vitro nitrogen mustard vapor exposure.Annals of the New York Academy of Sciences · 2020Article
- Bevacizumab dose adjustment to improve clinical outcomes of glioblastoma.BMC medicine · 2020Article
- The Role of Rho GTPases in VEGF Signaling in Cancer Cells.Analytical cellular pathology (Amsterdam) · 2020Review
- VEGFA From Early Osteoblast Lineage Cells (Osterix+) Is Required in Mice for Fracture Healing.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2019Article
- Therapeutic effect ofIntegrative medicine research · 2019Article
- Phenotypic and Expressional Heterogeneity in the Invasive Glioma Cells.Translational oncology · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Integrin α9β1 mediates accelerated cell adhesion and migration through interactions with a number of diverse extracellular ligands. We have shown previously that it directly binds the vascular endothelial growth factors (VEGF) A, C, and D and contributes to VEGF-induced angiogenesis and lymphangiogenesis. Until now, the α9β1 binding site in VEGF has not been identified. Here, we report that the three-amino acid sequence, EYP, encoded by exon 3 of VEGF-A is essential for binding of VEGF to integrin α9β1 and induces adhesion and migration of endothelial and cancer cells. EYP is specific for α9β1 binding and neither requires nor activates VEGFR-2, the cognate receptor for VEGF-A. Following binding to EYP, integrin α9β1 transduces cell migration through direct activation of the integrin signaling intermediates Src and focal adhesion kinase. This interaction is biologically important because it mediates in vitro endothelial cell tube formation, wound healing, and cancer cell invasion. These novel findings identify EYP as a potential site for directed pharmacotherapy.
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Registered trials
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.