ArticleFrontiers in cell and developmental biology2021
Galectin-3 Enhances Vascular Endothelial Growth Factor-A Receptor 2 Activity in the Presence of Vascular Endothelial Growth Factor.
Article in Frontiers in cell and developmental biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
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- Loss of ALK4 promotes cancer progression through regulating TGF-β receptor N-glycosylation.Nature communications · 2025Article
- Article
- Endomucin regulates the endothelial cytoskeleton independently of VEGF.Experimental eye research · 2025Article
- BAP31 Promotes Angiogenesis via Galectin-3 Upregulation in Neuroblastoma.International journal of molecular sciences · 2024Article
- Sex-specific role of galectin-3 in aortic stenosis.Biology of sex differences · 2023Article
- Microglial Galectin3 enhances endothelial metabolism and promotes pathological angiogenesis via Notch inhibition by competitively binding to Jag1.Cell death & disease · 2023Article
- Galectin-3 promotes secretion of proteases that decrease epithelium integrity in human colon cancer cells.Cell death & disease · 2023Article
- Therapeutic Mechanism and Key Active Ingredients of Shenfu Injection in Sepsis: A Network Pharmacology and Molecular Docking Approach.Evidence-based complementary and alternative medicine : eCAM · 2022Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Galectin-3 (Gal3) is a carbohydrate-binding protein reported to promote angiogenesis by influencing vascular endothelial growth factor-A receptor 2 (VEGFR2) signal transduction. Here we evaluated whether the ability of Gal3 to function as an angiogenic factor involved vascular endothelial growth factor (VEGF). To address this possibility we used human retinal microvascular endothelial cells (HRECs) to determine whether exogenous Gal3 requires VEGF to activate VEGFR2 signaling and if Gal3 is required for VEGF to activate VEGFR2. VEGFR2 phosphorylation and HREC migration assays, following either VEGF neutralization with ranibizumab or Gal3 silencing, revealed that VEGF endogenously produced by the HRECs was essential for the effect of exogenous Gal3 on VEGFR2 activation and cell migration, and that VEGF-induced VEGFR2 activation was not dependent on Gal3 in HRECs. Gal3 depletion led to no reduction in VEGF-induced cell function. Since Gal3 has been suggested to be a potential therapeutic target for VEGFR2-mediated angiogenesis, it is crucial to define the possible Gal3-mediated VEGFR2 signal transduction mechanism to aid the development of efficacious therapeutic strategies.
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