scholarly journals Glucose Modulates Basement Membrane Fibroblast Growth Factor-2 via Alterations in Endothelial Cell Permeability

2007 ◽  
Vol 282 (19) ◽  
pp. 14635-14644 ◽  
Author(s):  
Alisa S. Morss ◽  
Elazer R. Edelman
Keyword(s):  
Endothelial Cell ◽  
Growth Factor ◽  
Basement Membrane ◽  
Fibroblast Growth Factor ◽  
Cell Permeability ◽  
Fibroblast Growth Factor 2 ◽  
Fibroblast Growth ◽  
Endothelial Cell Permeability

scholarly journals Caveolin-1 orchestrates fibroblast growth factor 2 signaling control of angiogenesis in placental artery endothelial cell caveolae

2012 ◽  
Vol 227 (6) ◽  
pp. 2480-2491 ◽  
Author(s):  
Lin Feng ◽  
Wu-Xiang Liao ◽  
Quan Luo ◽  
Hong-Hai Zhang ◽  
Wen Wang ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Fibroblast Growth Factor 2 ◽  
Fibroblast Growth ◽  
Caveolin 1

scholarly journals Fibroblast growth factor-2 alleviates the capillary leakage and inflammation in sepsis

2020 ◽  
Vol 26 (1) ◽  
Author(s):  
Xiaojun Pan ◽  
Shunyao Xu ◽  
Zhen Zhou ◽  
Fen Wang ◽  
Lingjie Mao ◽  
...  
Keyword(s):  
Growth Factor ◽  
Lung Injury ◽  
Fibroblast Growth Factor ◽  
Cecal Ligation ◽  
Endothelial Cell Migration ◽  
Cell Permeability ◽  
Fibroblast Growth Factor 2 ◽  
Inflammatory Factors ◽  
Fibroblast Growth ◽  
Capillary Leakage

Abstract Background Acute lung injury (ALI), which is induced by numerous pathogenic factors, especially sepsis, can generate alveolar damage, pulmonary edema and vascular hyper-permeability ultimately leading to severe hypoxemia. Fibroblast growth factor-2 (FGF2) is an important member of the FGF family associated with endothelial cell migration and proliferation, and injury repairment. Here, we conducted this study aiming to evaluate the therapeutic effect of FGF2 in sepsis-induced ALI. Methods Recombinant FGF2 was abdominally injected into septic mice induced by cecal ligation and puncture (CLP), and then the inflammatory factors of lung tissue, vascular permeability and lung injury-related indicators based on protein levels and gene expression were detected. In vitro, human pulmonary microvascular endothelial cells (HPMEC) and mouse peritoneal macrophages (PMs) were challenged by lipopolysaccharides (LPS) with or without FGF2 administration in different groups, and then changes in inflammation indicators and cell permeability ability were tested. Results The results revealed that FGF2 treatment reduced inflammation response, attenuated pulmonary capillary leakage, alleviated lung injury and improved survival in septic mice. The endothelial injury and macrophages inflammation induced by LPS were inhibited by FGF2 administration via AKT/P38/NF-κB signaling pathways. Conclusion These findings indicated a therapeutic role of FGF2 in ALI through ameliorating capillary leakage and inflammation.

scholarly journals Fibroblast growth factor 2 regulates endothelial cell sensitivity to sunitinib

Oncogene ◽  
2010 ◽  
Vol 30 (10) ◽  
pp. 1183-1193 ◽  
Author(s):  
J C Welti ◽  
M Gourlaouen ◽  
T Powles ◽  
S C Kudahetti ◽  
P Wilson ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Fibroblast Growth Factor 2 ◽  
Fibroblast Growth ◽  
Cell Sensitivity

scholarly journals Interaction of Fibroblast Growth Factor-2 (FGF-2) with Free Gangliosides: Biochemical Characterization and Biological Consequences in Endothelial Cell Cultures

1999 ◽  
Vol 10 (2) ◽  
pp. 313-327 ◽  
Author(s):  
Marco Rusnati ◽  
Elena Tanghetti ◽  
Chiara Urbinati ◽  
Giovanni Tulipano ◽  
Sergio Marchesini ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Sialic Acid ◽  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Cell Cultures ◽  
Direct Interaction ◽  
Fibroblast Growth Factor 2 ◽  
Fibroblast Growth ◽  
Endothelial Cell Cultures ◽  
Galactosyl Ceramide

Exogenous gangliosides affect the angiogenic activity of fibroblast growth factor-2 (FGF-2), but their mechanism of action has not been elucidated. Here, a possible direct interaction of sialo-glycolipids with FGF-2 has been investigated. Size exclusion chromatography demonstrates that native, but not heat-denatured, 125I-FGF-2 binds to micelles formed by gangliosides GT1b, GD1b, or GM1. Also, gangliosides protect native FGF-2 from trypsin digestion at micromolar concentrations, the order of relative potency being GT1b > GD1b > GM1 = GM2 = sulfatide > GM3 = galactosyl-ceramide, whereas asialo-GM1, neuraminic acid, and N-acetylneuramin-lactose were ineffective. Scatchard plot analysis of the binding data of fluorochrome-labeled GM1 to immobilized FGF-2 indicates that FGF–2/GM1 interaction occurs with aK d equal to 6 μM. This interaction is inhibited by the sialic acid-binding peptide mastoparan and by the synthetic fragments FGF-2(112–129) and, to a lesser extent, FGF-2(130–155), whereas peptides FGF-2(10–33), FGF-2(39–59), FGF-2(86–96), and the basic peptide HIV-1 Tat(41–60) were ineffective. These data identify the COOH terminus of FGF-2 as a putative ganglioside-binding region. Exogenous gangliosides inhibit the binding of 125I-FGF-2 to high-affinity tyrosine-kinase FGF-receptors (FGFRs) of endothelial GM 7373 cells at micromolar concentrations. The order of relative potency was GT1b > GD1b > GM1 > sulfatide a = sialo-GM1. Accordingly, GT1b,GD1b, GM1, and GM2, but not GM3 and asialo-GM1, prevent the binding of 125I-FGF-2 to a soluble, recombinant form of extracellular FGFR-1. Conversely, the soluble receptor and free heparin inhibit the interaction of fluorochrome-labeled GM1 to immobilized FGF-2. In agreement with their FGFR antagonist activity, free gangliosides inhibit the mitogenic activity exerted by FGF-2 on endothelial cells in the same range of concentrations. Also in this case, GT1b was the most effective among the gangliosides tested while asialo-GM1, neuraminic acid,N-acetylneuramin-lactose, galactosyl-ceramide, and sulfatide were ineffective. In conclusion, the data demonstrate the capacity of exogenous gangliosides to interact with FGF-2. This interaction involves the COOH terminus of the FGF-2 molecule and depends on the structure of the oligosaccharide chain and on the presence of sialic acid residue(s) in the ganglioside molecule. Exogenous gangliosides act as FGF-2 antagonists when added to endothelial cell cultures. Since gangliosides are extensively shed by tumor cells and reach elevated levels in the serum of tumor-bearing patients, our data suggest that exogenous gangliosides may affect endothelial cell function by a direct interaction with FGF-2, thus modulating tumor neovascularization.

scholarly journals Bradykinin B2 Receptor Contributes to Inflammatory Responses in Human Endothelial Cells by the Transactivation of the Fibroblast Growth Factor Receptor FGFR-1

2018 ◽  
Vol 19 (9) ◽  
pp. 2638 ◽  
Author(s):  
Erika Terzuoli ◽  
Federico Corti ◽  
Ginevra Nannelli ◽  
Antonio Giachetti ◽  
Sandra Donnini ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Fibroblast Growth Factor Receptor ◽  
Inflammatory Responses ◽  
Growth Factor Receptor ◽  
Cell Permeability ◽  
Fibroblast Growth ◽  
Endothelial Cell Permeability ◽  
And Migration

Elevated levels of bradykinin (BK) and fibroblast growth factor-2 (FGF-2) have been implicated in the pathogenesis of inflammatory and angiogenic disorders. In angiogenesis, both stimuli induce a pro-inflammatory signature in endothelial cells, activating an autocrine/paracrine amplification loop that sustains the neovascularization process. Here we investigated the contribution of the FGF-2 pathway in the BK-mediated human endothelial cell permeability and migration, and the role of the B2 receptor (B2R) of BK in this cross-talk. BK (1 µM) upregulated the FGF-2 expression and promoted the FGF-2 signaling, both in human umbilical vein endothelial cells (HUVEC) and in retinal capillary endothelial cells (HREC) by the activation of Fibroblast growth factor receptor-1 (FGFR-1) and its downstream signaling (fibroblast growth factor receptor substrate: FRSα, extracellular signal–regulated kinases1/2: ERK1/2, and signal transducer and activator of transcription 3: STAT3 phosphorylation). FGFR-1 phosphorylation triggered by BK was c-Src mediated and independent from FGF-2 upregulation. Either HUVEC and HREC exposed to BK showed increased permeability, disassembly of adherens and tight-junction, and increased cell migration. B2R blockade by the selective antagonist, fasitibant, significantly inhibited FGF-2/FGFR-1 signaling, and in turn, BK-mediated endothelial cell permeability and migration. Similarly, the FGFR-1 inhibitor, SU5402, and the knock-down of the receptor prevented the BK/B2R inflammatory response in endothelial cells. In conclusion, this work demonstrates the existence of a BK/B2R/FGFR-1/FGF-2 axis in endothelial cells that might be implicated in propagation of angiogenic/inflammatory responses. A B2R blockade, by abolishing the initial BK stimulus, strongly attenuated FGFR-1-driven cell permeability and migration.

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