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 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.

Evidence for the interaction of fibroblast growth factor-2 with the lymphatic endothelial cell marker LYVE-1

Blood ◽  
2013 ◽  
Vol 121 (7) ◽  
pp. 1229-1237 ◽  
Author(s):  
Natalia Platonova ◽  
Geraldine Miquel ◽  
Birgit Regenfuss ◽  
Said Taouji ◽  
Claus Cursiefen ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Growth Factor ◽  
Fibroblast Growth Factor ◽  
Lymphatic Endothelial Cell ◽  
Fibroblast Growth Factor 2 ◽  
Fibroblast Growth ◽  
Cell Marker ◽  
Endogenous Expression ◽  
Key Points ◽  
Endothelial Cell Marker

Key Points FGF2 is able to directly interact with LYVE-1 and glycosylation of LYVE-1 is important for the interaction with FGF2. LYVE-1 inhibits FGF2-dependent lymphangiogenesis and FGF2 modulates LYVE-1's endogenous expression and reverses the effect of TNFβ.

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